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Conserved domains on  [gi|564392594|ref|XP_006254460|]
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ubiquitin carboxyl-terminal hydrolase 14 isoform X2 [Rattus norvegicus]

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 ...
71-445 7.31e-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: 491.85  E-value: 7.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsaretesssasavtPSKKKSLIDQFFGVEFETTMKCTESE-EEE 229
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 230 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02657  141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 310 KDVKFPLMLDVYELCTPelqekmisfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 389
Cdd:cd02657  221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564392594 390 HQGRSSSSGHYVSWVKRKE-DEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 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 1.89e-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: 123.11  E-value: 1.89e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564392594   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 7.31e-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: 491.85  E-value: 7.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsaretesssasavtPSKKKSLIDQFFGVEFETTMKCTESE-EEE 229
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 230 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02657  141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 310 KDVKFPLMLDVYELCTPelqekmisfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 389
Cdd:cd02657  221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564392594 390 HQGRSSSSGHYVSWVKRKE-DEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 445
Cdd:cd02657  249 HQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-444 1.28e-77

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 244.27  E-value: 1.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594   70 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 147
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  148 FPQFAekgeqgQYLQQDANECWIQMMRVLQQKLEaieddsaretesssasAVTPSKKKSLIDQFFGVEFETTMKCTESEE 227
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLN----------------GNHSTENESLITDLFRGQLKSRLKCLSCGE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  228 EEVTKGKENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYk 299
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  300 eKESVNAKVLKDVKFPLMLDVYELCTPELQEKMisfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsNNC 379
Cdd:pfam00443 217 -NRSTWEKLNTEVEFPLELDLSRYLAEELKPKT--------------------------------------------NNL 251
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564392594  380 GYYDLQAVLTHQGrSSSSGHYVSWVKRKED-EWIKFDDDKVSIVTPEDILRLsgggdwHIAYVLLY 444
Cdd:pfam00443 252 QDYRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-65 1.89e-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: 123.11  E-value: 1.89e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564392594   4 YSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKN 65
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKD 64
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
71-427 4.10e-22

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 95.64  E-value: 4.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIR-SVPELKDALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 142
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 143 flhmafpqfaekgeqgQYLQQDANEcwiqmmrVLQQKLEAIEDDSAReTESSSASAVTPSKKKSLIDQFFGVEFETTMKc 222
Cdd:COG5533   76 ----------------MGSQEDAHE-------LLGKLLDELKLDLVN-SFTIRIFKTTKDKKKTSTGDWFDIIIELPDQ- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 223 teseeeevtKGKENQLQLSCFINQeVKYLF---TGLKLRLQEEITKQSPTLQRNAlyiksskISRLPAYLTIQMVRFFYk 299
Cdd:COG5533  131 ---------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEELEVQAKQEYEVS-------FVKLPKILTIQLKRFAN- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 300 ekESVNAKVLKDVkfplmldvyelctpelqekmisfrskfkdleDKKVNQqpnandknsppkeikyePFSFADDIGSNNC 379
Cdd:COG5533  193 --LGGNQKIDTEV-------------------------------DEKFEL-----------------PVKHDQILNIVKE 222
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 564392594 380 GYYDLQAVLTHQGrSSSSGHYVSWVKRKEDeWIKFDDDKVSIVTPEDI 427
Cdd:COG5533  223 TYYDLVGFVLHQG-SLEGGHYIAYVKKGGK-WEKANDSDVTPVSEEEA 268
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
5-57 6.78e-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: 6.78e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564392594     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 7.31e-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: 491.85  E-value: 7.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsaretesssasavtPSKKKSLIDQFFGVEFETTMKCTESE-EEE 229
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 230 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02657  141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 310 KDVKFPLMLDVYELCTPelqekmisfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 389
Cdd:cd02657  221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564392594 390 HQGRSSSSGHYVSWVKRKE-DEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 445
Cdd:cd02657  249 HQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-444 1.28e-77

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 244.27  E-value: 1.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594   70 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 147
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  148 FPQFAekgeqgQYLQQDANECWIQMMRVLQQKLEaieddsaretesssasAVTPSKKKSLIDQFFGVEFETTMKCTESEE 227
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLN----------------GNHSTENESLITDLFRGQLKSRLKCLSCGE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  228 EEVTKGKENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYk 299
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  300 eKESVNAKVLKDVKFPLMLDVYELCTPELQEKMisfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsNNC 379
Cdd:pfam00443 217 -NRSTWEKLNTEVEFPLELDLSRYLAEELKPKT--------------------------------------------NNL 251
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564392594  380 GYYDLQAVLTHQGrSSSSGHYVSWVKRKED-EWIKFDDDKVSIVTPEDILRLsgggdwHIAYVLLY 444
Cdd:pfam00443 252 QDYRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
71-444 2.45e-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: 179.60  E-value: 2.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVpelkdalkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqflhmafpq 150
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 faekgeqgqylQQDANECWIQMMRVLQqkleaieddsaRETESSSASAVTPSKKKSLIDQFFGVEFETTMKCTESEEEEV 230
Cdd:cd02257   22 -----------QQDAHEFLLFLLDKLH-----------EELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 231 TKGKENQLQLSCFI-NQEVKYLFTGLKLRLQEEIT----KQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKeSVN 305
Cdd:cd02257   80 STEPELFLSLPLPVkGLPQVSLEDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTK 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 306 AKVLKDVKFPLMLDVYELCTPElqekmisfrskfkdledkkvnqqpnandknsppkeikyepfsFADDIGSNNCGYYDLQ 385
Cdd:cd02257  159 EKLNTKVSFPLELDLSPYLSEG------------------------------------------EKDSDSDNGSYKYELV 196
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 386 AVLTHQGRSSSSGHYVSWVK-RKEDEWIKFDDDKVSIVTPEDILRLsgGGDWHIAYVLLY 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 1.89e-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: 123.11  E-value: 1.89e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564392594   4 YSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKN 65
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKD 64
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
70-444 1.23e-23

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 101.18  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  70 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGA---------------LRASGEMASAQYITAALRDLFDSMDKTSSS 134
Cdd:cd02659    3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTeddddnksvplalqrLFLFLQLSESPVKTTELTDKTRSFGWDSLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 135 IppiillqflhmafpqfaekgeqgqYLQQDANEcwiqMMRVLQQKLEaieddsaretESSSASAVtpskkKSLIDQFFGV 214
Cdd:cd02659   83 T------------------------FEQHDVQE----FFRVLFDKLE----------EKLKGTGQ-----EGLIKNLFGG 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 215 EFETTMKCTE----SEEEEVTkgkenqLQLSCFInQEVKYLFTGLKLRLQEEI-------TKQSPTLQRNAlyIKSSKIS 283
Cdd:cd02659  120 KLVNYIICKEcpheSEREEYF------LDLQVAV-KGKKNLEESLDAYVQGETlegdnkyFCEKCGKKVDA--EKGVCFK 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 284 RLPAYLTIQMVRFFYK----EKESVNAKVlkdvKFPLMLDVYELCTPELqekmisfrsKFKDLEDKKVNQQPnandknsp 359
Cdd:cd02659  191 KLPPVLTLQLKRFEFDfetmMRIKINDRF----EFPLELDMEPYTEKGL---------AKKEGDSEKKDSES-------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 360 pkeikYEpfsfaddigsnncgyYDLQAVLTHQGrSSSSGHYVSWVK-RKEDEWIKFDDDKVSIVTPEDILRLSGGGD--- 435
Cdd:cd02659  250 -----YI---------------YELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECFGGEetq 308
                        410       420
                 ....*....|....*....|.
gi 564392594 436 ------------WHIAYVLLY 444
Cdd:cd02659  309 ktydsgprafkrTTNAYMLFY 329
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
69-444 2.14e-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: 2.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  69 PCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASA-----QYITAALRDlfdsmdkTSSSIPPIILLQF 143
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMmcaleAHVERALAS-------SGPGSAPRIFSSN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 144 LHMAFPQFaekgeqGQYLQQDANEcwiqMMRVLqqkLEAIEDDSARETESSSAsAVTPSKKKSLIDQFFGVEFETTMKCT 223
Cdd:cd02661   74 LKQISKHF------RIGRQEDAHE----FLRYL---LDAMQKACLDRFKKLKA-VDPSSQETTLVQQIFGGYLRSQVKCL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 224 ESEEEEVTKgkENQLQLSCFINQeVKYLFTGLKLRLQEEITKQSPTLQ--RNALYIKSSK---ISRLPAYLTIQMVRF-- 296
Cdd:cd02661  140 NCKHVSNTY--DPFLDLSLDIKG-ADSLEDALEQFTKPEQLDGENKYKceRCKKKVKASKqltIHRAPNVLTIHLKRFsn 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 297 FYKEKESvnakvlKDVKFPLMLDvyelctpeLQEKMisfrskfkdledkkvnqqpnANDKNSPPKeikyepfsfaddigs 376
Cdd:cd02661  217 FRGGKIN------KQISFPETLD--------LSPYM--------------------SQPNDGPLK--------------- 247
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564392594 377 nncgyYDLQAVLTHQGRSSSSGHYVSWVKRKEDEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:cd02661  248 -----YKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQK-------AYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 2.43e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 97.44  E-value: 2.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDAL---KRYAGALRASgemaSAQYITAALRDLFDSMDkTSSSIPPIILLQFLHMA 147
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFlsdRHSCTCLSCS----PNSCLSCAMDEIFQEFY-YSGDRSPYGPINLLYLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 148 FpqFAEKgEQGQYLQQDANECWIQMMRVLQQkleaiedDSARETESSSasavTPSKKKSLIDQFFGVEFETTMKCTESEE 227
Cdd:cd02660   77 W--KHSR-NLAGYSQQDAHEFFQFLLDQLHT-------HYGGDKNEAN----DESHCNCIIHQTFSGSLQSSVTCQRCGG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 228 eeVTKGKENQLQLSCFInQEVKYLFTGLKLRLQEEITKQSPTLQR--------NALY-----------IKSSKISRLPAY 288
Cdd:cd02660  143 --VSTTVDPFLDLSLDI-PNKSTPSWALGESGVSGTPTLSDCLDRftrpeklgDFAYkcsgcgstqeaTKQLSIKKLPPV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 289 LTIQMVRFFYKEKESvNAKVLKDVKFPLMLDVYELCTPELQEKMisfrskfkdledkkvnqqpnanDKNSPPKEIKYepf 368
Cdd:cd02660  220 LCFQLKRFEHSLNKT-SRKIDTYVQFPLELNMTPYTSSSIGDTQ----------------------DSNSLDPDYTY--- 273
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564392594 369 sfaddigsnncgyyDLQAVLTHQGrSSSSGHYVSWVKRKEDEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:cd02660  274 --------------DLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQ-------AYLLFY 327
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
71-427 4.10e-22

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 95.64  E-value: 4.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIR-SVPELKDALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 142
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 143 flhmafpqfaekgeqgQYLQQDANEcwiqmmrVLQQKLEAIEDDSAReTESSSASAVTPSKKKSLIDQFFGVEFETTMKc 222
Cdd:COG5533   76 ----------------MGSQEDAHE-------LLGKLLDELKLDLVN-SFTIRIFKTTKDKKKTSTGDWFDIIIELPDQ- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 223 teseeeevtKGKENQLQLSCFINQeVKYLF---TGLKLRLQEEITKQSPTLQRNAlyiksskISRLPAYLTIQMVRFFYk 299
Cdd:COG5533  131 ---------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEELEVQAKQEYEVS-------FVKLPKILTIQLKRFAN- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 300 ekESVNAKVLKDVkfplmldvyelctpelqekmisfrskfkdleDKKVNQqpnandknsppkeikyePFSFADDIGSNNC 379
Cdd:COG5533  193 --LGGNQKIDTEV-------------------------------DEKFEL-----------------PVKHDQILNIVKE 222
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 564392594 380 GYYDLQAVLTHQGrSSSSGHYVSWVKRKEDeWIKFDDDKVSIVTPEDI 427
Cdd:COG5533  223 TYYDLVGFVLHQG-SLEGGHYIAYVKKGGK-WEKANDSDVTPVSEEEA 268
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 2.62e-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: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDALkrYAGALRASGEMASAQyitaalrdlfdsMDKTSSSIPPIILLQ--FLHMAF 148
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAV--YECNSTEDAELKNMP------------PDKPHEPQTIIDQLQliFAQLQF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 149 PQ--------FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDdsaretesssasavtpSKKKSLIDQFFGVEFETTM 220
Cdd:cd02668   67 GNrsvvdpsgFVKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN----------------PDLKNIVQDLFRGEYSYVT 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 221 KCTESEEEEVTKGKENQLQLSCFINQEVKYLFTG-LKlrlQEEITKQS----PTLQRNALYIKSSKISRLPAYLTIQMVR 295
Cdd:cd02668  131 QCSKCGRESSLPSKFYELELQLKGHKTLEECIDEfLK---EEQLTGDNqyfcESCNSKTDATRRIRLTTLPPTLNFQLLR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 296 FFYKEKESVNAKVLKDVKFPLMLDVYELCTPElqekmisfrskfkdledkkvnqqpnandknsppKEIKYEpfsfaddig 375
Cdd:cd02668  208 FVFDRKTGAKKKLNASISFPEILDMGEYLAES---------------------------------DEGSYV--------- 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 376 snncgyYDLQAVLTHQGRSSSSGHYVSWVK-RKEDEWIKFDDDKVS-----------IVTPEDILRLSGGGDWHI---AY 440
Cdd:cd02668  246 ------YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEempgkplklgnSEDPAKPRKSEIKKGTHSsrtAY 319

                 ....
gi 564392594 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 6.61e-18

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 84.47  E-value: 6.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQcirsvpelkdalkryagALrasgemASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02664    1 GLINLGNTCYMNSVLQ-----------------AL------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQ 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 FAEKGEQGQYL------------QQDANEcwiqMMRVLQQKLEaieddsaretesssasavtpskkkSLIDQFFGVEFET 218
Cdd:cd02664   58 RRAEAPPDYFLeasrppwftpgsQQDCSE----YLRYLLDRLH------------------------TLIEKMFGGKLST 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 219 TMKCTESEEEEVTKGKENQLQLS-CFINQEVKYLFTGLKLRLQEEITKQSPTLQRNAlyIKSSKISRLPAYLTIQMVRFF 297
Cdd:cd02664  110 TIRCLNCNSTSARTERFRDLDLSfPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDA--EKEMKVTGAPEYLILTLLRFS 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 298 YKEKESVNAKVLKDVKFPLMLDVyelctPELQEKMISFRSKFKDLEDkkvnqqpnandknsppkeikyepfSFADDIGSN 377
Cdd:cd02664  188 YDQKTHVREKIMDNVSINEVLSL-----PVRVESKSSESPLEKKEEE------------------------SGDDGELVT 238
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 378 NCGYYDLQAVLTHQGRSSSSGHYVSWV---------------------KRKEDEWIKFDDDKVSIVTPEDILRLSGGGDW 436
Cdd:cd02664  239 RQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNVTSRFPK 318

                 ....*...
gi 564392594 437 HIAYVLLY 444
Cdd:cd02664  319 DTPYILFY 326
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 7.92e-18

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 83.90  E-value: 7.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIrsvpelkdalkrYAGALRASgemasaqyitaaLRDLFDSM---DKTSSSIPPIILLQFLHMA 147
Cdd:cd02663    1 GLENFGNTCYCNSVLQAL------------YFENLLTC------------LKDLFESIseqKKRTGVISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 148 FPQFaekgeqGQYLQQDANECwiqMMRVLQQKLEAIEDDSARETESSSASA-VTPSKKKSLI-DQFFGVEFETTmKCTES 225
Cdd:cd02663   57 NELF------DNYMHQDAHEF---LNFLLNEIAEILDAERKAEKANRKLNNnNNAEPQPTWVhEIFQGILTNET-RCLTC 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 226 EEeeVTKGKENQLQLSCFINQEVKyLFTGLKLRLQEEitkqspTL-QRNALYI----------KSSKISRLPAYLTIQMV 294
Cdd:cd02663  127 ET--VSSRDETFLDLSIDVEQNTS-ITSCLRQFSATE------TLcGRNKFYCdeccslqeaeKRMKIKKLPKILALHLK 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 295 RFFYKEKESVNAKVLKDVKFPLMLdvyelctpelqekmisfrskfkdledkkvnqqpnandknsppkeikyEPFSFADDi 374
Cdd:cd02663  198 RFKYDEQLNRYIKLFYRVVFPLEL-----------------------------------------------RLFNTTDD- 229
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564392594 375 GSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKeDEWIKFDDDKVSIVTPEDILRLSGGGDWHI-AYVLLY 444
Cdd:cd02663  230 AENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKIDENAVEEFFGDSPNQAtAYVLFY 299
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 7.63e-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: 79.25  E-value: 7.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIrsvpelkdalkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqfLHMafpq 150
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL-------------------------------------------------------SAD---- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 faekgeqgqylQQDANECWIQMMRVLQqkleaieddsaretesssasavtpskkkSLIDQFFGVEFETTMKCTESEEEEV 230
Cdd:cd02674   22 -----------QQDAQEFLLFLLDGLH----------------------------SIIVDLFQGQLKSRLTCLTCGKTST 62
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 231 T----------------KGKENQLQlSCFInqevkyLFTGlKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMV 294
Cdd:cd02674   63 TfepftylslpipsgsgDAPKVTLE-DCLR------LFTK-EETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLK 134
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 295 RFFYKEKESVnaKVLKDVKFPLmldvyelctpelqekmisfrskfKDLEDKKVnqqPNANDKNSPPKeikyepfsfaddi 374
Cdd:cd02674  135 RFSFSRGSTR--KLTTPVTFPL-----------------------NDLDLTPY---VDTRSFTGPFK------------- 173
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564392594 375 gsnncgyYDLQAVLTHQGrSSSSGHYVSWVKRKE-DEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:cd02674  174 -------YDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSS-------AYILFY 229
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-405 3.17e-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: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRyagalrasgemasaqyitaALRDLFDSMDKTSssippiillqflhmafPQ 150
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------TPKELFSQVCRKA----------------PQ 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 151 FaeKGeqgqYLQQDANEcwiqMMRVLQQKLEaieddsaretesssasavtpskkkSLIDQFFGVEFETTMKCTESEEeeV 230
Cdd:cd02667   46 F--KG----YQQQDSHE----LLRYLLDGLR------------------------TFIDSIFGGELTSTIMCESCGT--V 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 231 TKGKENQLQLSC----FINQEV-----KYLFTGlklrlQEEITKQSPTLQRNALY-IKSSKISRLPAYLTIQMVRFFyKE 300
Cdd:cd02667   90 SLVYEPFLDLSLprsdEIKSECsiescLKQFTE-----VEILEGNNKFACENCTKaKKQYLISKLPPVLVIHLKRFQ-QP 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 301 KESVNAKVLKDVKFPLMLDVYELCTPelqeKMISFRSKFKDLedkkvnqqpnandknsppkeikyepfsfaddigsnncg 380
Cdd:cd02667  164 RSANLRKVSRHVSFPEILDLAPFCDP----KCNSSEDKSSVL-------------------------------------- 201
                        330       340
                 ....*....|....*....|....*
gi 564392594 381 yYDLQAVLTHQGrSSSSGHYVSWVK 405
Cdd:cd02667  202 -YRLYGVVEHSG-TMRSGHYVAYVK 224
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
64-430 6.41e-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: 6.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  64 KNMELP-CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALrasGEMASAQYITAALRDLFDSMDKTSssiPPIILLQ 142
Cdd:cd02671   18 RENLLPfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI---SSVEQLQSSFLLNPEKYNDELANQ---APRRLLN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 143 FLHMAFPQFaekgeQGqYLQQDANE---CWIQMMRVLQQKLeaIEDDSARETESSSASAVTpSKKKSLIDQFFGVEFETT 219
Cdd:cd02671   92 ALREVNPMY-----EG-YLQHDAQEvlqCILGNIQELVEKD--FQGQLVLRTRCLECETFT-ERREDFQDISVPVQESEL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 220 MKCTESEE---EEVTKGKENQLQLSCFINQEvkylftglKLRLQEEITKQSPTLQRNAlyIKSSKISRLPAYLTIQMVRF 296
Cdd:cd02671  163 SKSEESSEispDPKTEMKTLKWAISQFASVE--------RIVGEDKYFCENCHHYTEA--ERSLLFDKLPEVITIHLKCF 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 297 --------FYKEKESVNAKVLKdvkfPLMLDVYELCTpelqekmisfrskfkdledkkvnqqpnandknSPPKEIkyepf 368
Cdd:cd02671  233 aangsefdCYGGLSKVNTPLLT----PLKLSLEEWST--------------------------------KPKNDV----- 271
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564392594 369 sfaddigsnncgyYDLQAVLTHQGRSSSSGHYVSWVKrkedeWIKFDDDKVSIVTPEDILRL 430
Cdd:cd02671  272 -------------YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEA 315
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
69-441 7.46e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 75.61  E-value: 7.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  69 PCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRAS-----------------GEMASAQYITAALRDLFDSMDKT 131
Cdd:cd02666    1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELasdypterriggrevsrSELQRSNQFVYELRSLFNDLIHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 132 -SSSIPPIILLQFLHMAfpqfaekgeqgqylQQDANECWIQMMRVLQQKLEAIEDDSARETESSSASAVTpskkksLIDQ 210
Cdd:cd02666   81 nTRSVTPSKELAYLALR--------------QQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSD------LIKR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 211 FFGVEF-ETTMKCTESEEEEVTKGKENQLQLScfinqeVKYLFTGlklrlQEEITKQSPTLQRNAL--YIKSSKISRLPA 287
Cdd:cd02666  141 LFSGKTkQQLVPESMGNQPSVRTKTERFLSLL------VDVGKKG-----REIVVLLEPKDLYDALdrYFDYDSLTKLPQ 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 288 YLTIQMVRFFYKEKESvnakvlkdvkfpLMLDVYELctPELQEKMISFRSkfKDLEDKKVNQQPNANDKNSPPKEIKYEp 367
Cdd:cd02666  210 RSQVQAQLAQPLQREL------------ISMDRYEL--PSSIDDIDELIR--EAIQSESSLVRQAQNELAELKHEIEKQ- 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 368 fsFAD--DIGsnncgyYDLQAVLTHQGrSSSSGHYVSWVK-RKEDEWIKFDDDKVSIVTPEDI-LRLSGGGD--WHIAYV 441
Cdd:cd02666  273 --FDDlkSYG------YRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYNDETVTVVPASEVfLFTLGNTAtpYFLVYV 343
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 2.77e-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: 70.43  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  71 GLTNLGNTCYMNATVQCIRSVPelkdALKRYAGALRASGE--------------------MASAQYITaaLRDLFDSMDK 130
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIP----SFQWRYDDLENKFPsdvvdpandlncqlikladgLLSGRYSK--PASLKSENDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 131 TSSSIPPIILLQFLHMAFPQFAEKGeqgqylQQDANECWiqmmRVLQQKLEaieddsaRETESSSASAVTPSkkkslidq 210
Cdd:cd02658   75 YQVGIKPSMFKALIGKGHPEFSTMR------QQDALEFL----LHLIDKLD-------RESFKNLGLNPNDL-------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 211 fFGVEFETTMKCTESEEEEVTKGKENQLQLScfinqevkylftglkLRLQEEITKQSPTLqrnaLYIKSSKISRLPAYLT 290
Cdd:cd02658  130 -FKFMIEDRLECLSCKKVKYTSELSEILSLP---------------VPKDEATEKEEGEL----VYEPVPLEDCLKAYFA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 291 IQMVRFFYKE-KESVNAkvLKDVKFPLMLDVyelctpeLQEKMIsfrsKFKDLED---KKVNqqpnandknsppkeikyE 366
Cdd:cd02658  190 PETIEDFCSTcKEKTTA--TKTTGFKTFPDY-------LVINMK----RFQLLENwvpKKLD-----------------V 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 367 PFSFADDIGSnncGYYDLQAVLTHQGRSSSSGHYVSWVKRK---EDEWIKFDDDKVSIVT-PEDILRLsgggdwhiAYVL 442
Cdd:cd02658  240 PIDVPEELGP---GKYELIAFISHKGTSVHSGHYVAHIKKEidgEGKWVLFNDEKVVASQdPPEMKKL--------GYIY 308

                 ..
gi 564392594 443 LY 444
Cdd:cd02658  309 FY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
354-435 9.14e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 57.96  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  354 NDKNSPPKEIKYEPFSFADDIGSNNCGY-YDLQAVLTHQGrSSSSGHYVSWVK-RKEDEWIKFDDDKVSIVTPEDILRLS 431
Cdd:COG5077   402 NDRYEFPLEIDLLPFLDRDADKSENSDAvYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEN 480

                  ....
gi 564392594  432 GGGD 435
Cdd:COG5077   481 FGGD 484
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
70-231 1.92e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 56.82  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  70 CGLTNLGNTCYMNATVQCIRSVPELKDAL--KRYAGALRASGEMASAQYITAALRDLFDSM-DKTSSSIPPI----ILLQ 142
Cdd:COG5560  266 CGLRNLGNTCYMNSALQCLMHTWELRDYFlsDEYEESINEENPLGMHGSVASAYADLIKQLyDGNLHAFTPSgfkkTIGS 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 143 FLHMAfpqfaeKGeqgqYLQQDANECWIQMMRVLQQKLEAIEDDSARETESSSASAVTPSKKK-------------SLID 209
Cdd:COG5560  346 FNEEF------SG----YDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKakecwwehlkrndSIIT 415
                        170       180
                 ....*....|....*....|..
gi 564392594 210 QFFGVEFETTMKCTESEEEEVT 231
Cdd:COG5560  416 DLFQGMYKSTLTCPGCGSVSIT 437
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
5-57 6.78e-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: 6.78e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564392594     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 3.19e-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: 3.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564392594   6 VTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDD 57
Cdd:cd17039    1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK 52
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
382-444 3.70e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 49.50  E-value: 3.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564392594 382 YDLQAVLTHQGrSSSSGHYVSWVKRKEDE-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 6.52e-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: 6.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564392594   5 SVTVKWGKEKFEgVELNTDEPPMVFKAQLFALTGVQPARQKVMVKgGTLKDD 56
Cdd:cd17047    2 DFKVIWNKEKYD-VKFPLDSTIAELKEHIETLTGVPPAMQKLMYK-GLLKDD 51
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
355-444 8.69e-06

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 46.78  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 355 DKNSPPKEIKYEPfsfaddigsnncgyYDLQAVLTHQGRsSSSGHYVSWV-KRKEDEWIKFDDDKVSIVTPEDILRLS-G 432
Cdd:cd02665  151 DKLEFPQIIQQVP--------------YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfG 215
                         90
                 ....*....|..
gi 564392594 433 GGDWHIAYVLLY 444
Cdd:cd02665  216 GGRNPSAYCLMY 227
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
4-57 2.79e-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: 2.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564392594   4 YSVTVKWGKEKFEgVELNTDEPPMVFKAQLFALTGVQPARQKV--MVKGGTLKDDD 57
Cdd:cd01813    1 ITLIVKWSGKEYP-VTVLSSDTVLDLKQRIFELTGVLPKRQKLlgLKVKGKPADDD 55
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
71-416 7.07e-05

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 44.57  E-value: 7.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594   71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGalrasgemasaqyiTAALRD---------LFDSMDKTSSSIppiilL 141
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLA--------------TECLKEhcllcelgfLFDMLEKAKGKN-----C 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  142 Q---FLHmAFPQFAEKGEQG--QYLQQDANECWIQMM-----RVLqqkLEAIEDDSARETESSSASAvtpskkkSLIDQF 211
Cdd:pfam13423  63 QasnFLR-ALSSIPEASALGllDEDRETNSAISLSSLiqsfnRFL---LDQLSSEENSTPPNPSPAE-------SPLEQL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  212 FGVEFETTMKCT----ESEEEEVT-----------KGKENQLQLSCFINqevkYLFTGLKlrlQEEITK--------QSP 268
Cdd:pfam13423 132 FGIDAETTIRCSncghESVRESSThvldliyprkpSSNNKKPPNQTFSS----ILKSSLE---RETTTKawcekckrYQP 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594  269 TLQRnalyiksSKISRLPAYLtiqmvrffykekeSVNAKVLKDvkfplmldvyelctpelqekmisfrskfkdlEDKKVN 348
Cdd:pfam13423 205 LESR-------RTVRNLPPVL-------------SLNAALTNE-------------------------------EWRQLW 233
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564392594  349 QQPNandknSPPKEIKyePFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVK--------RKEDEWIKFDD 416
Cdd:pfam13423 234 KTPG-----WLPPEIG--LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQWYLFND 302
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
382-433 4.27e-04

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 41.75  E-value: 4.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564392594 382 YDLQAVLTHQGRSSSSGHYVSWVKR--KEDEWIKFDDDKVSIVTPEDIL---RLSGG 433
Cdd:cd02673  184 YSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGY 240
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
203-428 8.52e-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: 41.54  E-value: 8.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 203 KKKSLI-DQFFGVEFETTMKCTESEEEEVTKGKENQLQLScFINQEVKYLFTGLKL--------RLQEEITKQSP----- 268
Cdd:cd02669  231 PNSSIIhDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRV-KKTSVSPFLLLTLDLpppplfkdGNEENIIPQVPlkqll 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 269 ------TLQRNALYIKSSKISRLPAYLTIQMVRF----FYKEKesvNAKVlkdVKFPLmldvyelctpelqekmisfrsk 338
Cdd:cd02669  310 kkydgkTETELKDSLKRYLISRLPKYLIFHIKRFsknnFFKEK---NPTI---VNFPI---------------------- 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 339 fKDLEDKKVNQQpnanDKNSPPKEIKyepfsfaddigsnncgyYDLQAVLTHQGRSSSSGHY-VSWVKRKEDEWIKFDDD 417
Cdd:cd02669  362 -KNLDLSDYVHF----DKPSLNLSTK-----------------YNLVANIVHEGTPQEDGTWrVQLRHKSTNKWFEIQDL 419
                        250
                 ....*....|.
gi 564392594 418 KVSIVTPEDIL 428
Cdd:cd02669  420 NVKEVLPQLIF 430
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 564392594  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRY 101
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF 31
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
382-444 2.94e-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: 39.27  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564392594 382 YDLQAVLTHQGrSSSSGHYVSW------VKRKE---------------DEWIKFDDDKVSIVTPEDILrLSGGgdwhiAY 440
Cdd:cd02662  163 YRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEpgsfvrmregpsstsHPWWRISDTTVKEVSESEVL-EQKS-----AY 235

                 ....
gi 564392594 441 VLLY 444
Cdd:cd02662  236 MLFY 239
 
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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