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Conserved domains on  [gi|569004274|ref|XP_006526197|]
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ubiquitin carboxyl-terminal hydrolase 14 isoform X1 [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

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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 ...
80-454 1.75e-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: 493.77  E-value: 1.75e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 159
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsgretdsssapavtPSKKKSLIDQYFGVEFETTMKCTESE-EEE 238
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 239 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 318
Cdd:cd02657  141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 319 KDVKFPLMLDVYELCTPelqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 398
Cdd:cd02657  221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569004274 399 HQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 454
Cdd:cd02657  249 HQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
1-50 7.29e-27

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: 102.70  E-value: 7.29e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569004274   1 MVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKNGMTVLMMGSAD 50
Cdd:cd16104   25 LVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-454 1.75e-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: 493.77  E-value: 1.75e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 159
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsgretdsssapavtPSKKKSLIDQYFGVEFETTMKCTESE-EEE 238
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 239 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 318
Cdd:cd02657  141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 319 KDVKFPLMLDVYELCTPelqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 398
Cdd:cd02657  221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569004274 399 HQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 454
Cdd:cd02657  249 HQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
79-453 2.60e-77

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 243.89  E-value: 2.60e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274   79 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 156
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  157 FPQFAekgeqgQYLQQDANECWIQMMRVLQQKLEaieddsgretdsssapAVTPSKKKSLIDQYFGVEFETTMKCTESEE 236
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLN----------------GNHSTENESLITDLFRGQLKSRLKCLSCGE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  237 EEVTKGKENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYk 308
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  309 eKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVSFRSkfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnc 388
Cdd:pfam00443 217 -NRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------------------------------------------ 253
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004274  389 gyYDLQAVLTHQGrSSSSGHYVSWVRRKQD-EWIKFDDDKVSIVTPEDILRLsgggdwHIAYVLLY 453
Cdd:pfam00443 254 --YRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
1-50 7.29e-27

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: 102.70  E-value: 7.29e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569004274   1 MVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKNGMTVLMMGSAD 50
Cdd:cd16104   25 LVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
80-436 2.25e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 93.71  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIR-SVPELKDALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 151
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 152 flhmafpqfaekgeqgQYLQQDANEcwiqmmrVLQQKLEAIE-DDSGRETDSSSAPavTPSKKKSLIDQYFGVEFETTMK 230
Cdd:COG5533   76 ----------------MGSQEDAHE-------LLGKLLDELKlDLVNSFTIRIFKT--TKDKKKTSTGDWFDIIIELPDQ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 231 cteseeeevtKGKENQLQLSCFINQeVKYLF---TGLKLRLQEEITKQSPTLQRNAlyiksskISRLPAYLTIQMVRFFY 307
Cdd:COG5533  131 ----------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEELEVQAKQEYEVS-------FVKLPKILTIQLKRFAN 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 308 kekESVNAKVLKDVkfplmldvyelctpelqekmvsfrskfkdleDKKVNQqpnandknsppkeikyePFSFADDIGSNN 387
Cdd:COG5533  193 ---LGGNQKIDTEV-------------------------------DEKFEL-----------------PVKHDQILNIVK 221
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 569004274 388 CGYYDLQAVLTHQGrSSSSGHYVSWVRRKqDEWIKFDDDKVSIVTPEDI 436
Cdd:COG5533  222 ETYYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEA 268
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
1-48 1.77e-06

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: 45.33  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 569004274     1 MVFKAQLFALTGVQPARQKVMVKGGTLKDDD-WGNIKMKNGMTVLMMGS 48
Cdd:smart00213  24 SELKEKIAELTGIPPEQQRLIYKGKVLEDDRtLADYGIQDGSTIHLVLR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
3-48 9.00e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 34.84  E-value: 9.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 569004274    3 FKAQLFALTGVQPARQKVMVKGGTLKDDD-WGNIKMKNGMTVLMMGS 48
Cdd:pfam00240  24 LKEKIAEKEGVPPEQQRLIYSGKVLEDDQtLGEYGIEDGSTIHLVLR 70
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-454 1.75e-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: 493.77  E-value: 1.75e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 159
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsgretdsssapavtPSKKKSLIDQYFGVEFETTMKCTESE-EEE 238
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 239 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 318
Cdd:cd02657  141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 319 KDVKFPLMLDVYELCTPelqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 398
Cdd:cd02657  221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569004274 399 HQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 454
Cdd:cd02657  249 HQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
79-453 2.60e-77

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 243.89  E-value: 2.60e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274   79 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 156
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  157 FPQFAekgeqgQYLQQDANECWIQMMRVLQQKLEaieddsgretdsssapAVTPSKKKSLIDQYFGVEFETTMKCTESEE 236
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLN----------------GNHSTENESLITDLFRGQLKSRLKCLSCGE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  237 EEVTKGKENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYk 308
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  309 eKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVSFRSkfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnc 388
Cdd:pfam00443 217 -NRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------------------------------------------ 253
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004274  389 gyYDLQAVLTHQGrSSSSGHYVSWVRRKQD-EWIKFDDDKVSIVTPEDILRLsgggdwHIAYVLLY 453
Cdd:pfam00443 254 --YRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
80-453 2.92e-54

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: 181.91  E-value: 2.92e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVpelkdalkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqflhmafpq 159
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 faekgeqgqylQQDANECWIQMmrvlqqkLEAIEDdsgrETDSSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEEEEV 239
Cdd:cd02257   22 -----------QQDAHEFLLFL-------LDKLHE----ELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 240 TKGKENQLQLSCFI-NQEVKYLFTGLKLRLQEEIT----KQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKeSVN 314
Cdd:cd02257   80 STEPELFLSLPLPVkGLPQVSLEDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTK 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 315 AKVLKDVKFPLMLDVYELCTPElqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsFADDIGSNNCGYYDLQ 394
Cdd:cd02257  159 EKLNTKVSFPLELDLSPYLSEG------------------------------------------EKDSDSDNGSYKYELV 196
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 395 AVLTHQGRSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDILRLsgGGDWHIAYVLLY 453
Cdd:cd02257  197 AVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLEF--GSLSSSAYILFY 254
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
1-50 7.29e-27

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: 102.70  E-value: 7.29e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569004274   1 MVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKNGMTVLMMGSAD 50
Cdd:cd16104   25 LVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
78-453 1.55e-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: 100.43  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  78 PCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASA-----QYITAALRDlfdsmdkTSSSIPPIILLQF 152
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMmcaleAHVERALAS-------SGPGSAPRIFSSN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 153 LHMAFPQFaekgeqGQYLQQDANEcwiqMMRVLQQKLEAIEDDSGRETDSSSapavTPSKKKSLIDQYFGVEFETTMKCT 232
Cdd:cd02661   74 LKQISKHF------RIGRQEDAHE----FLRYLLDAMQKACLDRFKKLKAVD----PSSQETTLVQQIFGGYLRSQVKCL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 233 ESEEEEVTKgkENQLQLSCFINQeVKYLFTGLKLRLQEEITKQSPTLQ--RNALYIKSSK---ISRLPAYLTIQMVRF-- 305
Cdd:cd02661  140 NCKHVSNTY--DPFLDLSLDIKG-ADSLEDALEQFTKPEQLDGENKYKceRCKKKVKASKqltIHRAPNVLTIHLKRFsn 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 306 FYKEKESvnakvlKDVKFPLMLDvyelctpeLQEKMvsfrskfkdledkkvnqqpnANDKNSPPKeikyepfsfaddigs 385
Cdd:cd02661  217 FRGGKIN------KQISFPETLD--------LSPYM--------------------SQPNDGPLK--------------- 247
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004274 386 nncgyYDLQAVLTHQGRSSSSGHYVSWVRRKQDEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 453
Cdd:cd02661  248 -----YKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQK-------AYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-453 3.40e-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: 3.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDAL---KRYAGALRASgemaSAQYITAALRDLFDSMDkTSSSIPPIILLQFLHMA 156
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFlsdRHSCTCLSCS----PNSCLSCAMDEIFQEFY-YSGDRSPYGPINLLYLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 157 FpqFAEKgEQGQYLQQDANECWIQMMRVLQQkleaiedDSGRetdsSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEE 236
Cdd:cd02660   77 W--KHSR-NLAGYSQQDAHEFFQFLLDQLHT-------HYGG----DKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 237 eeVTKGKENQLQLSCFInQEVKYLFTGLKLRLQEEITKQSPTLQR--------NALY-----------IKSSKISRLPAY 297
Cdd:cd02660  143 --VSTTVDPFLDLSLDI-PNKSTPSWALGESGVSGTPTLSDCLDRftrpeklgDFAYkcsgcgstqeaTKQLSIKKLPPV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 298 LTIQMVRFFYKEKESvNAKVLKDVKFPLMLDVYELCTPELQEKMvsfrskfkdledkkvnqqpnanDKNSPPKEIKYepf 377
Cdd:cd02660  220 LCFQLKRFEHSLNKT-SRKIDTYVQFPLELNMTPYTSSSIGDTQ----------------------DSNSLDPDYTY--- 273
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004274 378 sfaddigsnncgyyDLQAVLTHQGrSSSSGHYVSWVRRKQDEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 453
Cdd:cd02660  274 --------------DLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQ-------AYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
79-453 9.48e-23

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 98.87  E-value: 9.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  79 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGA---------------LRASGEMASAQYITAALRDLFDSMDKTSSS 143
Cdd:cd02659    3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTeddddnksvplalqrLFLFLQLSESPVKTTELTDKTRSFGWDSLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 144 IppiillqflhmafpqfaekgeqgqYLQQDANEcwiqMMRVLQQKLEaieddsgreTDSSSAPAvtpskkKSLIDQYFGV 223
Cdd:cd02659   83 T------------------------FEQHDVQE----FFRVLFDKLE---------EKLKGTGQ------EGLIKNLFGG 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 224 EFETTMKCTE----SEEEEVTkgkenqLQLSCFInQEVKYLFTGLKLRLQEEI-------TKQSPTLQRNAlyIKSSKIS 292
Cdd:cd02659  120 KLVNYIICKEcpheSEREEYF------LDLQVAV-KGKKNLEESLDAYVQGETlegdnkyFCEKCGKKVDA--EKGVCFK 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 293 RLPAYLTIQMVRFFYK----EKESVNAKVlkdvKFPLMLDVYELCTPELqekmvsfrsKFKDLEDKKVNQQPnandknsp 368
Cdd:cd02659  191 KLPPVLTLQLKRFEFDfetmMRIKINDRF----EFPLELDMEPYTEKGL---------AKKEGDSEKKDSES-------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 369 pkeikYEpfsfaddigsnncgyYDLQAVLTHQGrSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDILRLSGGGD--- 444
Cdd:cd02659  250 -----YI---------------YELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECFGGEetq 308
                        410       420
                 ....*....|....*....|.
gi 569004274 445 ------------WHIAYVLLY 453
Cdd:cd02659  309 ktydsgprafkrTTNAYMLFY 329
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
80-436 2.25e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 93.71  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIR-SVPELKDALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 151
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 152 flhmafpqfaekgeqgQYLQQDANEcwiqmmrVLQQKLEAIE-DDSGRETDSSSAPavTPSKKKSLIDQYFGVEFETTMK 230
Cdd:COG5533   76 ----------------MGSQEDAHE-------LLGKLLDELKlDLVNSFTIRIFKT--TKDKKKTSTGDWFDIIIELPDQ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 231 cteseeeevtKGKENQLQLSCFINQeVKYLF---TGLKLRLQEEITKQSPTLQRNAlyiksskISRLPAYLTIQMVRFFY 307
Cdd:COG5533  131 ----------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEELEVQAKQEYEVS-------FVKLPKILTIQLKRFAN 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 308 kekESVNAKVLKDVkfplmldvyelctpelqekmvsfrskfkdleDKKVNQqpnandknsppkeikyePFSFADDIGSNN 387
Cdd:COG5533  193 ---LGGNQKIDTEV-------------------------------DEKFEL-----------------PVKHDQILNIVK 221
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 569004274 388 CGYYDLQAVLTHQGrSSSSGHYVSWVRRKqDEWIKFDDDKVSIVTPEDI 436
Cdd:COG5533  222 ETYYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEA 268
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-453 1.23e-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: 89.40  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALkrYAGALRASGEMASAQyitaalrdlfdsMDKTSSSIPPIILLQ--FLHMAF 157
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAV--YECNSTEDAELKNMP------------PDKPHEPQTIIDQLQliFAQLQF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 158 PQ--------FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDdsgretdsssapavtpSKKKSLIDQYFGVEFETTM 229
Cdd:cd02668   67 GNrsvvdpsgFVKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN----------------PDLKNIVQDLFRGEYSYVT 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 230 KCTESEEEEVTKGKENQLQLSCFINQEVKYLFTG-LKlrlQEEITKQS----PTLQRNALYIKSSKISRLPAYLTIQMVR 304
Cdd:cd02668  131 QCSKCGRESSLPSKFYELELQLKGHKTLEECIDEfLK---EEQLTGDNqyfcESCNSKTDATRRIRLTTLPPTLNFQLLR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 305 FFYKEKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddig 384
Cdd:cd02668  208 FVFDRKTGAKKKLNASISFPEILDMGEYLAESDEGSYV------------------------------------------ 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 385 snncgyYDLQAVLTHQGRSSSSGHYVSWVRRKQ-DEWIKFDDDKVS-----------IVTPEDILRLSGGGDWHI---AY 449
Cdd:cd02668  246 ------YELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDVEempgkplklgnSEDPAKPRKSEIKKGTHSsrtAY 319

                 ....
gi 569004274 450 VLLY 453
Cdd:cd02668  320 MLVY 323
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-453 2.49e-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: 2.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQcirsvpelkdalkryagALrasgemASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAfpq 159
Cdd:cd02664    1 GLINLGNTCYMNSVLQ-----------------AL------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLM--- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 faekgeqgqyLQQDANECWIQmmRVLQQKLEAIEDDsGRETDSSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEEEEV 239
Cdd:cd02664   55 ----------HTQRRAEAPPD--YFLEASRPPWFTP-GSQQDCSEYLRYLLDRLHTLIEKMFGGKLSTTIRCLNCNSTSA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 240 TKGKENQLQLS-CFINQEVKYLFTGLKLRLQEEITKQSPTLQRNAlyIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 318
Cdd:cd02664  122 RTERFRDLDLSfPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDA--EKEMKVTGAPEYLILTLLRFSYDQKTHVREKIM 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 319 KDVKFPLMLDVyelctPELQEKMVSFRSKFKDLEDkkvnqqpnandknsppkeikyepfSFADDIGSNNCGYYDLQAVLT 398
Cdd:cd02664  200 DNVSINEVLSL-----PVRVESKSSESPLEKKEEE------------------------SGDDGELVTRQVHYRLYAVVV 250
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004274 399 HQGRSSSSGHYVSWVR---------------------RKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLY 453
Cdd:cd02664  251 HSGYSSESGHYFTYARdqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFY 326
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-453 6.25e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 79.64  E-value: 6.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIrsvpelkdalkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqfLHMafpq 159
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL-------------------------------------------------------SAD---- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 faekgeqgqylQQDANECWIQMMRVLQqkleaieddsgretdsssapavtpskkkSLIDQYFGVEFETTMKCTESEEEEV 239
Cdd:cd02674   22 -----------QQDAQEFLLFLLDGLH----------------------------SIIVDLFQGQLKSRLTCLTCGKTST 62
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 240 T----------------KGKENQLQlSCFInqevkyLFTGlKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMV 303
Cdd:cd02674   63 TfepftylslpipsgsgDAPKVTLE-DCLR------LFTK-EETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLK 134
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 304 RFFYKEKESVnaKVLKDVKFPLmldvyelctpelqekmvsfrskfKDLEDKKVnqqPNANDKNSPPKeikyepfsfaddi 383
Cdd:cd02674  135 RFSFSRGSTR--KLTTPVTFPL-----------------------NDLDLTPY---VDTRSFTGPFK------------- 173
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569004274 384 gsnncgyYDLQAVLTHQGrSSSSGHYVSWVRRKQ-DEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 453
Cdd:cd02674  174 -------YDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSS-------AYILFY 229
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-453 8.90e-17

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 80.82  E-value: 8.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIrsvpelkdalkrYAGALRASgemasaqyitaaLRDLFDSM---DKTSSSIPPIILLQFLHMA 156
Cdd:cd02663    1 GLENFGNTCYCNSVLQAL------------YFENLLTC------------LKDLFESIseqKKRTGVISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 157 FPQFaekgeqGQYLQQDANECwiqMMRVLQQKLEAIEDDSGRE-TDSSSAPAVTPSKKKSLIDQYF-GVEFETTmKCTES 234
Cdd:cd02663   57 NELF------DNYMHQDAHEF---LNFLLNEIAEILDAERKAEkANRKLNNNNNAEPQPTWVHEIFqGILTNET-RCLTC 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 235 EEeeVTKGKENQLQLSCFINQEVKyLFTGLKLRLQEEitkqspTL-QRNALYI----------KSSKISRLPAYLTIQMV 303
Cdd:cd02663  127 ET--VSSRDETFLDLSIDVEQNTS-ITSCLRQFSATE------TLcGRNKFYCdeccslqeaeKRMKIKKLPKILALHLK 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 304 RFFYKEKESVNAKVLKDVKFPLMLdvyelctpelqekmvsfrskfkdledkkvnqqpnandknsppkeikyEPFSFADDi 383
Cdd:cd02663  198 RFKYDEQLNRYIKLFYRVVFPLEL-----------------------------------------------RLFNTTDD- 229
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569004274 384 GSNNCGYYDLQAVLTHQGRSSSSGHYVSWVrRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHI-AYVLLY 453
Cdd:cd02663  230 AENPDRLYELVAVVVHIGGGPNHGHYVSIV-KSHGGWLLFDDETVEKIDENAVEEFFGDSPNQAtAYVLFY 299
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-414 2.71e-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: 78.97  E-value: 2.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALKRyagalrasgemasaqyitaALRDLFDSMDKTSssippiillqflhmafPQ 159
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------TPKELFSQVCRKA----------------PQ 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 FaeKGeqgqYLQQDANEcwiqMMRVLQQKLEaieddsgretdsssapavtpskkkSLIDQYFGVEFETTMKCTESEEeeV 239
Cdd:cd02667   46 F--KG----YQQQDSHE----LLRYLLDGLR------------------------TFIDSIFGGELTSTIMCESCGT--V 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 240 TKGKENQLQLSC----FINQEV-----KYLFTGlklrlQEEITKQSPTLQRNALY-IKSSKISRLPAYLTIQMVRFFyKE 309
Cdd:cd02667   90 SLVYEPFLDLSLprsdEIKSECsiescLKQFTE-----VEILEGNNKFACENCTKaKKQYLISKLPPVLVIHLKRFQ-QP 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 310 KESVNAKVLKDVKFPLMLDVYELCTPelqeKMVSFRSKFKDLedkkvnqqpnandknsppkeikyepfsfaddigsnncg 389
Cdd:cd02667  164 RSANLRKVSRHVSFPEILDLAPFCDP----KCNSSEDKSSVL-------------------------------------- 201
                        330       340
                 ....*....|....*....|....*
gi 569004274 390 yYDLQAVLTHQGrSSSSGHYVSWVR 414
Cdd:cd02667  202 -YRLYGVVEHSG-TMRSGHYVAYVK 224
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-439 1.27e-14

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 74.54  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALrasGEMASAQYITAALRDLFDSMDKTSssiPPIILLQFLHMAFPQ 159
Cdd:cd02671   26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI---SSVEQLQSSFLLNPEKYNDELANQ---APRRLLNALREVNPM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 160 FaekgeQGqYLQQDANEcwiqmmrVLQQKLEAIEDdsgretdsssapavtpskkksLIDQYFGVEFETTMKCTESeeEEV 239
Cdd:cd02671  100 Y-----EG-YLQHDAQE-------VLQCILGNIQE---------------------LVEKDFQGQLVLRTRCLEC--ETF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 240 TKGKENQLQLSCFInQEVKYLFTGLKLRLQEEITKQSPTLQRN-ALYIKSSKI-----------------------SRLP 295
Cdd:cd02671  144 TERREDFQDISVPV-QESELSKSEESSEISPDPKTEMKTLKWAiSQFASVERIvgedkyfcenchhyteaersllfDKLP 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 296 AYLTIQMVRF--------FYKEKESVNAKVLKdvkfPLMLDVYELCTpelqekmvsfrskfkdledkkvnqqpnandknS 367
Cdd:cd02671  223 EVITIHLKCFaangsefdCYGGLSKVNTPLLT----PLKLSLEEWST--------------------------------K 266
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569004274 368 PPKEIkyepfsfaddigsnncgyYDLQAVLTHQGRSSSSGHYVSWVRrkqdeWIKFDDDKVSIVTPEDILRL 439
Cdd:cd02671  267 PKNDV------------------YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEA 315
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
78-450 1.43e-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: 74.84  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  78 PCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRAS-----------------GEMASAQYITAALRDLFDSMDKT 140
Cdd:cd02666    1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELasdypterriggrevsrSELQRSNQFVYELRSLFNDLIHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 141 -SSSIPPIILLQFLHMAfpqfaekgeqgqylQQDANECWIQMMRVLQQKLEAIED-DSGRETDSSSApavtpskKKSLID 218
Cdd:cd02666   81 nTRSVTPSKELAYLALR--------------QQDVTECIDNVLFQLEVALEPISNaFAGPDTEDDKE-------QSDLIK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 219 QYFGVEF-ETTMKCTESEEEEVTKGKENQLQLScfinqeVKYLFTGlklrlQEEITKQSPTLQRNAL--YIKSSKISRLP 295
Cdd:cd02666  140 RLFSGKTkQQLVPESMGNQPSVRTKTERFLSLL------VDVGKKG-----REIVVLLEPKDLYDALdrYFDYDSLTKLP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 296 AYLTIQMVRFFYKEKESvnakvlkdvkfpLMLDVYELctPELQEKMVSFRSkfKDLEDKKVNQQPNANDKNSPPKEIKYE 375
Cdd:cd02666  209 QRSQVQAQLAQPLQREL------------ISMDRYEL--PSSIDDIDELIR--EAIQSESSLVRQAQNELAELKHEIEKQ 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 376 pfsFAD--DIGsnncgyYDLQAVLTHQGrSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDI-LRLSGGGD--WHIAY 449
Cdd:cd02666  273 ---FDDlkSYG------YRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYNDETVTVVPASEVfLFTLGNTAtpYFLVY 342

                 .
gi 569004274 450 V 450
Cdd:cd02666  343 V 343
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-453 2.10e-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: 70.81  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPelkdALKRYAGALRASGE--------------------MASAQYITaaLRDLFDSMDK 139
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIP----SFQWRYDDLENKFPsdvvdpandlncqlikladgLLSGRYSK--PASLKSENDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 140 TSSSIPPIILLQFLHMAFPQFAEKGeqgqylQQDANECWiqmmRVLQQKLEaieddsgRETDSSSAPAVTPSkkkslidq 219
Cdd:cd02658   75 YQVGIKPSMFKALIGKGHPEFSTMR------QQDALEFL----LHLIDKLD-------RESFKNLGLNPNDL-------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 220 yFGVEFETTMKCTESEEEEVTKGKENQLQL-------SCFINQEVKYLFTGLKLRLQ-----EEITKQSPTLQRNALYIK 287
Cdd:cd02658  130 -FKFMIEDRLECLSCKKVKYTSELSEILSLpvpkdeaTEKEEGELVYEPVPLEDCLKayfapETIEDFCSTCKEKTTATK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 288 SSKISRLPAYLTIQMVRFFYKEKESvnakvlkdvkfPLMLDVyelctpelqekmvsfrskfkdledkkvnqqpnandkns 367
Cdd:cd02658  209 TTGFKTFPDYLVINMKRFQLLENWV-----------PKKLDV-------------------------------------- 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 368 ppkeikyePFSFADDIGSnncGYYDLQAVLTHQGRSSSSGHYVSWVRRKQD---EWIKFDDDKVSIVT-PEDILRLsggg 443
Cdd:cd02658  240 --------PIDVPEELGP---GKYELIAFISHKGTSVHSGHYVAHIKKEIDgegKWVLFNDEKVVASQdPPEMKKL---- 304
                        410
                 ....*....|
gi 569004274 444 dwhiAYVLLY 453
Cdd:cd02658  305 ----GYIYFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
79-240 3.82e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 56.04  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  79 CGLTNLGNTCYMNATVQCIRSVPELKDAL--KRYAGALRASGEMASAQYITAALRDLFDSM-DKTSSSIPPI----ILLQ 151
Cdd:COG5560  266 CGLRNLGNTCYMNSALQCLMHTWELRDYFlsDEYEESINEENPLGMHGSVASAYADLIKQLyDGNLHAFTPSgfkkTIGS 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 152 FLHMAfpqfaeKGeqgqYLQQDANECWIQMMRVLQQKLEAIEDDSGRETDSSSAPAVTPSKKK-------------SLID 218
Cdd:COG5560  346 FNEEF------SG----YDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKakecwwehlkrndSIIT 415
                        170       180
                 ....*....|....*....|..
gi 569004274 219 QYFGVEFETTMKCTESEEEEVT 240
Cdd:COG5560  416 DLFQGMYKSTLTCPGCGSVSIT 437
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
363-444 6.49e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 55.26  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  363 NDKNSPPKEIKYEPFSFADDIGSNNCGY-YDLQAVLTHQGrSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDILRLS 440
Cdd:COG5077   402 NDRYEFPLEIDLLPFLDRDADKSENSDAvYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEN 480

                  ....
gi 569004274  441 GGGD 444
Cdd:COG5077   481 FGGD 484
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
1-48 1.77e-06

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: 45.33  E-value: 1.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 569004274     1 MVFKAQLFALTGVQPARQKVMVKGGTLKDDD-WGNIKMKNGMTVLMMGS 48
Cdd:smart00213  24 SELKEKIAELTGIPPEQQRLIYKGKVLEDDRtLADYGIQDGSTIHLVLR 72
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
391-453 2.75e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 49.88  E-value: 2.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569004274 391 YDLQAVLTHQGrSSSSGHYVSWVRRKQDE-WIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 453
Cdd:COG5560  764 YDLYAVDNHYG-GLSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSS-------AYVLFY 819
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
4-48 3.20e-06

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: 44.87  E-value: 3.20e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 569004274   4 KAQLFALTGVQPARQKV--MVKGGTLKDDD--WGNIKMKNGMTVLMMGS 48
Cdd:cd01813   26 KQRIFELTGVLPKRQKLlgLKVKGKPADDDvkLSSLKLKPNTKIMMMGT 74
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
364-453 3.64e-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: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 364 DKNSPPKEIKYEPfsfaddigsnncgyYDLQAVLTHQGRsSSSGHYVSWV-RRKQDEWIKFDDDKVSIVTPEDILRLS-G 441
Cdd:cd02665  151 DKLEFPQIIQQVP--------------YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfG 215
                         90
                 ....*....|..
gi 569004274 442 GGDWHIAYVLLY 453
Cdd:cd02665  216 GGRNPSAYCLMY 227
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
3-46 6.56e-05

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: 41.04  E-value: 6.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569004274   3 FKAQLFALTGVQPARQKVMVKGGTLKDDDW-GNIKMKNGMTVLMM 46
Cdd:cd17039   24 LKEKIEEKTGIPVEQQRLIYNGKELKDDKTlSDYGIKDGSTIHLV 68
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
4-48 6.87e-05

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: 40.69  E-value: 6.87e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569004274   4 KAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKMKNGMTVLMMGS 48
Cdd:cd17047   26 KEHIETLTGVPPAMQKLMYKGLLKDDKTLRELKVTKGAKVMVVGS 70
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
212-437 7.36e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 45.00  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 212 KKKSLIDQYF-GVEFETTMKCTESEEEEVTKGKENQLQLScFINQEVKYLFTGLKL--------RLQEEITKQSP----- 277
Cdd:cd02669  231 PNSSIIHDCFqGKVQIETQKIKPHAEEEGSKDKFFKDSRV-KKTSVSPFLLLTLDLpppplfkdGNEENIIPQVPlkqll 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 278 ------TLQRNALYIKSSKISRLPAYLTIQMVRF----FYKEKesvNAKVlkdVKFPLmldvyelctpelqekmvsfrsk 347
Cdd:cd02669  310 kkydgkTETELKDSLKRYLISRLPKYLIFHIKRFsknnFFKEK---NPTI---VNFPI---------------------- 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 348 fKDLEDKKVnqqpNANDKNSPPKEIKyepfsfaddigsnncgyYDLQAVLTHQGRSSSSGHYVSWVRRK-QDEWIKFDDD 426
Cdd:cd02669  362 -KNLDLSDY----VHFDKPSLNLSTK-----------------YNLVANIVHEGTPQEDGTWRVQLRHKsTNKWFEIQDL 419
                        250
                 ....*....|.
gi 569004274 427 KVSIVTPEDIL 437
Cdd:cd02669  420 NVKEVLPQLIF 430
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
80-425 7.67e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274   80 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGalrasgemasaqyiTAALRD---------LFDSMDKTSSSIppiilL 150
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLA--------------TECLKEhcllcelgfLFDMLEKAKGKN-----C 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  151 Q---FLHmAFPQFAEKGEQG--QYLQQDANECWIQMM-----RVLqqkLEAIEDDsGRETDSSSAPAVTPskkkslIDQY 220
Cdd:pfam13423  63 QasnFLR-ALSSIPEASALGllDEDRETNSAISLSSLiqsfnRFL---LDQLSSE-ENSTPPNPSPAESP------LEQL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  221 FGVEFETTMKCT----ESEEEEVT-----------KGKENQLQLSCFINqevkYLFTGLKlrlQEEITK--------QSP 277
Cdd:pfam13423 132 FGIDAETTIRCSncghESVRESSThvldliyprkpSSNNKKPPNQTFSS----ILKSSLE---RETTTKawcekckrYQP 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274  278 TLQRnalyiksSKISRLPAYLtiqmvrffykekeSVNAKVLKDvkfplmldvyelctpelqekmvsfrskfkdlEDKKVN 357
Cdd:pfam13423 205 LESR-------RTVRNLPPVL-------------SLNAALTNE-------------------------------EWRQLW 233
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004274  358 QQPNandknSPPKEIKyePFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVR--------RKQDEWIKFDD 425
Cdd:pfam13423 234 KTPG-----WLPPEIG--LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQWYLFND 302
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
391-453 1.01e-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: 40.81  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004274 391 YDLQAVLTHQGrSSSSGHYVSWvRRK----------------------QDEWIKFDDDKVSIVTPEDILrLSGGgdwhiA 448
Cdd:cd02662  163 YRLRAVVVHYG-SHSSGHYVCY-RRKplfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVL-EQKS-----A 234

                 ....*
gi 569004274 449 YVLLY 453
Cdd:cd02662  235 YMLFY 239
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
391-442 1.05e-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: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569004274 391 YDLQAVLTHQGRSSSSGHYVSWVRR--KQDEWIKFDDDKVSIVTPEDIL---RLSGG 442
Cdd:cd02673  184 YSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGY 240
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-110 1.27e-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: 1.27e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 569004274  80 GLTNLGNTCYMNATVQCIRSVPELKDALKRY 110
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF 31
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
3-48 9.00e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 34.84  E-value: 9.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 569004274    3 FKAQLFALTGVQPARQKVMVKGGTLKDDD-WGNIKMKNGMTVLMMGS 48
Cdd:pfam00240  24 LKEKIAEKEGVPPEQQRLIYSGKVLEDDQtLGEYGIEDGSTIHLVLR 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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