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Conserved domains on  [gi|148234941|ref|NP_001087872|]
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ubiquitin specific peptidase 14 S homeolog [Xenopus laevis]

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 ...
106-476 5.97e-178

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: 501.09  E-value: 5.97e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 FAEKGDQGQYLQQDANECWVQVMRVLQQKLEStegdsdmetdsgaaatASKKNSFIDQFFGIEFESTMKCTESE-EEEVT 264
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG----------------AGSKGSFIDQLFGIELETKMKCTESPdEEEVS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 265 KSKETQLQLSCFINQEVKYLFTGLKLRLQEEITKFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYKEKESVNAKVLKD 344
Cdd:cd02657  143 TESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 345 VKFPLMLDIYELCTPdlqekmvpyrskfkqvedkvpeqapkakqmaqrevryepyafpgdvgsinCGYYELQAVLTHQGR 424
Cdd:cd02657  223 VKFPFELDLYELCTP--------------------------------------------------SGYYELVAVITHQGR 252
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148234941 425 SSSSGHYLSWVKRKH-DEWIKFDDDKVSIVSPEDILRLSGGGDWHIAYVLLYG 476
Cdd:cd02657  253 SADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-76 5.00e-46

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: 154.70  E-value: 5.00e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148234941   4 YSVNVKWGKEKFDNVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDDWGN-LKIKSGMTLLMMGSAE 76
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-476 5.97e-178

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: 501.09  E-value: 5.97e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 FAEKGDQGQYLQQDANECWVQVMRVLQQKLEStegdsdmetdsgaaatASKKNSFIDQFFGIEFESTMKCTESE-EEEVT 264
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG----------------AGSKGSFIDQLFGIELETKMKCTESPdEEEVS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 265 KSKETQLQLSCFINQEVKYLFTGLKLRLQEEITKFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYKEKESVNAKVLKD 344
Cdd:cd02657  143 TESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 345 VKFPLMLDIYELCTPdlqekmvpyrskfkqvedkvpeqapkakqmaqrevryepyafpgdvgsinCGYYELQAVLTHQGR 424
Cdd:cd02657  223 VKFPFELDLYELCTP--------------------------------------------------SGYYELVAVITHQGR 252
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148234941 425 SSSSGHYLSWVKRKH-DEWIKFDDDKVSIVSPEDILRLSGGGDWHIAYVLLYG 476
Cdd:cd02657  253 SADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
105-475 2.53e-76

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 241.96  E-value: 2.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  105 CGLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 182
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  183 FPQFAekgdqgQYLQQDANECWVQVMRVLQQKLEStegdsdmetdsgaaATASKKNSFIDQFFGIEFESTMKCTESEEEE 262
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLNG--------------NHSTENESLITDLFRGQLKSRLKCLSCGEVS 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  263 VTKSKETQLQLSCFINQEVK--------YLFTGLKLRLQEEITKFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYkeK 334
Cdd:pfam00443 140 ETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--N 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  335 ESVNAKVLKDVKFPLMLDIYELCTPDLQEKMVPYRSkfkqvedkvpeqapkakqmaqrevryepyafpgdvgsincgyYE 414
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------------------------------------------YR 255
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148234941  415 LQAVLTHQGrSSSSGHYLSWVK-RKHDEWIKFDDDKVSIVSPEDILRLsgggdwHIAYVLLY 475
Cdd:pfam00443 256 LVAVVVHSG-SLSSGHYIAYIKaYENNRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-76 5.00e-46

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: 154.70  E-value: 5.00e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148234941   4 YSVNVKWGKEKFDNVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDDWGN-LKIKSGMTLLMMGSAE 76
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
106-458 6.73e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 92.56  E-value: 6.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIR-SVPELKEALKRYTGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 177
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 178 flhmafpqfaekgdqgQYLQQDANECWVQVMRVLQQKLESTEGDSDMETdsgaaaTASKKNSFIDQFFGIEFESTMKCTE 257
Cdd:COG5533   76 ----------------MGSQEDAHELLGKLLDELKLDLVNSFTIRIFKT------TKDKKKTSTGDWFDIIIELPDQTWV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 258 SEEeevtksKETQlqlsCFINQeVKYLF---TGLKLRLQEEItkfspSLQRNALYnkTSRISRLPAYLTIQMVRFFYkek 334
Cdd:COG5533  134 NNL------KTLQ----EFIDN-MEELVddeTGVKAKENEEL-----EVQAKQEY--EVSFVKLPKILTIQLKRFAN--- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 335 ESVNAKVLKDVKFPLMLDIyelctpdlqekmvpyrsKFKQVEDKVPEqapkakqmaqrevryepyafpgdvgsincGYYE 414
Cdd:COG5533  193 LGGNQKIDTEVDEKFELPV-----------------KHDQILNIVKE-----------------------------TYYD 226
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 148234941 415 LQAVLTHQGrSSSSGHYLSWVKRKhDEWIKFDDDKVSIVSPEDI 458
Cdd:COG5533  227 LVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEA 268
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
5-74 2.26e-11

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: 59.19  E-value: 2.26e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148234941     5 SVNVKWGKEKFDNVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDD-WGNLKIKSGMTLLMMGS 74
Cdd:smart00213   2 ELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRtLADYGIQDGSTIHLVLR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
6-74 1.77e-04

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: 39.85  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148234941    6 VNVK-WGKEKFDnVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDD-WGNLKIKSGMTLLMMGS 74
Cdd:pfam00240   1 ITVKtLDGKKIT-LEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQtLGEYGIEDGSTIHLVLR 70
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-476 5.97e-178

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: 501.09  E-value: 5.97e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 185
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 FAEKGDQGQYLQQDANECWVQVMRVLQQKLEStegdsdmetdsgaaatASKKNSFIDQFFGIEFESTMKCTESE-EEEVT 264
Cdd:cd02657   79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG----------------AGSKGSFIDQLFGIELETKMKCTESPdEEEVS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 265 KSKETQLQLSCFINQEVKYLFTGLKLRLQEEITKFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYKEKESVNAKVLKD 344
Cdd:cd02657  143 TESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 345 VKFPLMLDIYELCTPdlqekmvpyrskfkqvedkvpeqapkakqmaqrevryepyafpgdvgsinCGYYELQAVLTHQGR 424
Cdd:cd02657  223 VKFPFELDLYELCTP--------------------------------------------------SGYYELVAVITHQGR 252
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148234941 425 SSSSGHYLSWVKRKH-DEWIKFDDDKVSIVSPEDILRLSGGGDWHIAYVLLYG 476
Cdd:cd02657  253 SADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
105-475 2.53e-76

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 241.96  E-value: 2.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  105 CGLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 182
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  183 FPQFAekgdqgQYLQQDANECWVQVMRVLQQKLEStegdsdmetdsgaaATASKKNSFIDQFFGIEFESTMKCTESEEEE 262
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLNG--------------NHSTENESLITDLFRGQLKSRLKCLSCGEVS 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  263 VTKSKETQLQLSCFINQEVK--------YLFTGLKLRLQEEITKFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYkeK 334
Cdd:pfam00443 140 ETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--N 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  335 ESVNAKVLKDVKFPLMLDIYELCTPDLQEKMVPYRSkfkqvedkvpeqapkakqmaqrevryepyafpgdvgsincgyYE 414
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------------------------------------------YR 255
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148234941  415 LQAVLTHQGrSSSSGHYLSWVK-RKHDEWIKFDDDKVSIVSPEDILRLsgggdwHIAYVLLY 475
Cdd:pfam00443 256 LVAVVVHSG-SLSSGHYIAYIKaYENNRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
106-475 2.45e-55

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: 185.38  E-value: 2.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVpelkealkrytgalrasgemasaqyitaalrdlfdsmdktsssippiillqflhmafpq 185
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 faekgdqgqylQQDANECWVQVMRVLQQKLESTEGDSDMETdsgaaatasKKNSFIDQFFGIEFESTMKCTESEEEEVTK 265
Cdd:cd02257   22 -----------QQDAHEFLLFLLDKLHEELKKSSKRTSDSS---------SLKSLIHDLFGGKLESTIVCLECGHESVST 81
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 266 SKETQLQLSCFI-NQEVKYLFTGLKLRLQEEIT----KFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYKEKeSVNAK 340
Cdd:cd02257   82 EPELFLSLPLPVkGLPQVSLEDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEK 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 341 VLKDVKFPLMLDIYELCTPDLQEkmvpyrskfkqvedkvpeqapkakqmaqrevryepyafpgDVGSINCGYYELQAVLT 420
Cdd:cd02257  161 LNTKVSFPLELDLSPYLSEGEKD----------------------------------------SDSDNGSYKYELVAVVV 200
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148234941 421 HQGRSSSSGHYLSWVK-RKHDEWIKFDDDKVSIVSPEDILRLsgGGDWHIAYVLLY 475
Cdd:cd02257  201 HSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLEF--GSLSSSAYILFY 254
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-76 5.00e-46

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: 154.70  E-value: 5.00e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148234941   4 YSVNVKWGKEKFDNVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDDWGN-LKIKSGMTLLMMGSAE 76
Cdd:cd16104    2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKDGQTLMLMGSAE 75
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-475 7.46e-25

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 104.76  E-value: 7.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEAL--KRYTgalRASGEMASAQYITAALRDLFDSMDKTSSSIP--PIILLQFLHM 181
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHS---CTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPygPINLLYLSWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 182 AFPQFAekgdqgQYLQQDANECWVQVMRVLQQklestegdsDMETDSGAAATASKKNSFIDQFFGIEFESTMKCTESEEe 261
Cdd:cd02660   79 HSRNLA------GYSQQDAHEFFQFLLDQLHT---------HYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGG- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 262 eVTKSKETQLQLSCFInQEVKYLFTGLKLRLQEEITKFSPSLQR--------NALYN-----------KTSRISRLPAYL 322
Cdd:cd02660  143 -VSTTVDPFLDLSLDI-PNKSTPSWALGESGVSGTPTLSDCLDRftrpeklgDFAYKcsgcgstqeatKQLSIKKLPPVL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 323 TIQMVRFFYKEKESvNAKVLKDVKFPLMLDiyelctpdlqekMVPYRSKFKQVEDKVPEQAPKAKqmaqrevryepyafp 402
Cdd:cd02660  221 CFQLKRFEHSLNKT-SRKIDTYVQFPLELN------------MTPYTSSSIGDTQDSNSLDPDYT--------------- 272
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148234941 403 gdvgsincgyYELQAVLTHQGrSSSSGHYLSWVKRKHDEWIKFDDDKVSIVSPEDILRLSgggdwhiAYVLLY 475
Cdd:cd02660  273 ----------YDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQ-------AYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
104-475 6.53e-24

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: 101.58  E-value: 6.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 104 PCGLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRASGEMASA-----QYITAALRDlfdsmdkTSSSIPPIILLQF 178
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMmcaleAHVERALAS-------SGPGSAPRIFSSN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 179 LHMAFPQFaekgdqGQYLQQDANEcwvqVMRVLQQKLESTEgdSDMETDSGAAATASKKNSFIDQFFGIEFESTMKCT-- 256
Cdd:cd02661   74 LKQISKHF------RIGRQEDAHE----FLRYLLDAMQKAC--LDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLnc 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 257 --ESEeeevtkSKETQLQLSCFINQeVKYLFTGLKLRLQEEItkfspsLQRNALYN-----------KTSRISRLPAYLT 323
Cdd:cd02661  142 khVSN------TYDPFLDLSLDIKG-ADSLEDALEQFTKPEQ------LDGENKYKcerckkkvkasKQLTIHRAPNVLT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 324 IQMVRF--FYKEKESvnakvlKDVKFPLMLDiyelctpdlqekMVPYrskfkqvedkvpeqapkakqMAQrevryepyaf 401
Cdd:cd02661  209 IHLKRFsnFRGGKIN------KQISFPETLD------------LSPY--------------------MSQ---------- 240
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148234941 402 PGDVGSIncgyYELQAVLTHQGRSSSSGHYLSWVKRKHDEWIKFDDDKVSIVSPEDILRLSgggdwhiAYVLLY 475
Cdd:cd02661  241 PNDGPLK----YKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQK-------AYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-475 7.20e-24

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: 102.34  E-value: 7.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 105 CGLTNLGNTCYMNATVQCIRSVPELKEALKRYTGA---------------LRASGEMASAQYITAALRDLFDSMDKTSSS 169
Cdd:cd02659    3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTeddddnksvplalqrLFLFLQLSESPVKTTELTDKTRSFGWDSLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 170 IppiillqflhmafpqfaekgdqgqYLQQDANEcwvqVMRVLQQKLEstegdsdmetdsgaaaTASKKNS---FIDQFFG 246
Cdd:cd02659   83 T------------------------FEQHDVQE----FFRVLFDKLE----------------EKLKGTGqegLIKNLFG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 247 IEFESTMKCTE----SEEEE--------VTKSKETQLQLSCFINQEV-----KYLFTGLKLrlqeeitkfspslQRNAly 309
Cdd:cd02659  119 GKLVNYIICKEcpheSEREEyfldlqvaVKGKKNLEESLDAYVQGETlegdnKYFCEKCGK-------------KVDA-- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 310 NKTSRISRLPAYLTIQMVRFFYK----EKESVNAKVlkdvKFPLMLDiyelctpdlqekMVPYRSKFKQVEDKVPEQapk 385
Cdd:cd02659  184 EKGVCFKKLPPVLTLQLKRFEFDfetmMRIKINDRF----EFPLELD------------MEPYTEKGLAKKEGDSEK--- 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 386 akqmaQREVRYEpyafpgdvgsincgyYELQAVLTHQGrSSSSGHYLSWVK-RKHDEWIKFDDDKVSIVSPEDILRLSGG 464
Cdd:cd02659  245 -----KDSESYI---------------YELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECFG 303
                        410       420
                 ....*....|....*....|....*.
gi 148234941 465 GD---------------WHIAYVLLY 475
Cdd:cd02659  304 GEetqktydsgprafkrTTNAYMLFY 329
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-451 1.80e-21

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: 95.18  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTgalrasgemasaqyITAALRDLFDSMDKTSSSIPPIILLQFLhMAFPQ 185
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECN--------------STEDAELKNMPPDKPHEPQTIIDQLQLI-FAQLQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 FAEKG-------------DQGQylQQDANECWVQVMRVLQQKLESTEGdsdmetdsgaaataSKKNSFIDQFFGIEFEST 252
Cdd:cd02668   66 FGNRSvvdpsgfvkalglDTGQ--QQDAQEFSKLFLSLLEAKLSKSKN--------------PDLKNIVQDLFRGEYSYV 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 253 MKCTESEEEEVTKSKETQLQLSCFINQEVKYLFTGLklrLQEEITK-----FSPSLQRNALYNKTSRISRLPAYLTIQMV 327
Cdd:cd02668  130 TQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEF---LKEEQLTgdnqyFCESCNSKTDATRRIRLTTLPPTLNFQLL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 328 RFFYKEKESVNAKVLKDVKFPLMLDIYELCTPDLQEKMVpyrskfkqvedkvpeqapkakqmaqrevryepyafpgdvgs 407
Cdd:cd02668  207 RFVFDRKTGAKKKLNASISFPEILDMGEYLAESDEGSYV----------------------------------------- 245
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 148234941 408 incgyYELQAVLTHQGRSSSSGHYLSWVKRKH-DEWIKFDDDKVS 451
Cdd:cd02668  246 -----YELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDVE 285
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
106-458 6.73e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 92.56  E-value: 6.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIR-SVPELKEALKRYTGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 177
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 178 flhmafpqfaekgdqgQYLQQDANECWVQVMRVLQQKLESTEGDSDMETdsgaaaTASKKNSFIDQFFGIEFESTMKCTE 257
Cdd:COG5533   76 ----------------MGSQEDAHELLGKLLDELKLDLVNSFTIRIFKT------TKDKKKTSTGDWFDIIIELPDQTWV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 258 SEEeevtksKETQlqlsCFINQeVKYLF---TGLKLRLQEEItkfspSLQRNALYnkTSRISRLPAYLTIQMVRFFYkek 334
Cdd:COG5533  134 NNL------KTLQ----EFIDN-MEELVddeTGVKAKENEEL-----EVQAKQEY--EVSFVKLPKILTIQLKRFAN--- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 335 ESVNAKVLKDVKFPLMLDIyelctpdlqekmvpyrsKFKQVEDKVPEqapkakqmaqrevryepyafpgdvgsincGYYE 414
Cdd:COG5533  193 LGGNQKIDTEVDEKFELPV-----------------KHDQILNIVKE-----------------------------TYYD 226
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 148234941 415 LQAVLTHQGrSSSSGHYLSWVKRKhDEWIKFDDDKVSIVSPEDI 458
Cdd:COG5533  227 LVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEA 268
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-475 3.30e-20

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 90.83  E-value: 3.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIrsvpelkealkrYTGALRASgemasaqyitaaLRDLFDSM---DKTSSSIPPIILLQFLHMA 182
Cdd:cd02663    1 GLENFGNTCYCNSVLQAL------------YFENLLTC------------LKDLFESIseqKKRTGVISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 183 FPQFaekgdqGQYLQQDANECWVQVMRVLQQKLESTEGDSDMETDSGAAATASKKNSFI-DQFFGIEFESTmKCTESEEe 261
Cdd:cd02663   57 NELF------DNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTWVhEIFQGILTNET-RCLTCET- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 262 eVTKSKETQLQLSCFINQEVKyLFTGLKLRLQEEI----TKFS----PSLQRNalyNKTSRISRLPAYLTIQMVRFFYKE 333
Cdd:cd02663  129 -VSSRDETFLDLSIDVEQNTS-ITSCLRQFSATETlcgrNKFYcdecCSLQEA---EKRMKIKKLPKILALHLKRFKYDE 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 334 KESVNAKVLKDVKFPLMLDIYElCTPDlqekmvpyrskfkqvedkvpeqAPKAKQMaqrevryepyafpgdvgsincgyY 413
Cdd:cd02663  204 QLNRYIKLFYRVVFPLELRLFN-TTDD----------------------AENPDRL-----------------------Y 237
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148234941 414 ELQAVLTHQGRSSSSGHYLSWVKrKHDEWIKFDDDKVSIVSPEDILRLSGGGDWHI-AYVLLY 475
Cdd:cd02663  238 ELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEEFFGDSPNQAtAYVLFY 299
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-475 1.06e-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: 86.78  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALRASGE--MASAQYITAALrdlfdsMDKTSSSIPPIIllQFLHMAF 183
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQsvMKKLQLLQAHL------MHTQRRAEAPPD--YFLEASR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 184 PQFAEKGdqgqyLQQDANEcwvqVMRVLQQKLESTegdsdmetdsgaaataskknsfIDQFFGIEFESTMKCTESEEEEV 263
Cdd:cd02664   73 PPWFTPG-----SQQDCSE----YLRYLLDRLHTL----------------------IEKMFGGKLSTTIRCLNCNSTSA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 264 TKSKETQLQLS-CFINQEVKYLFTGLKLrlQEEITKFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYKEKESVNAKVL 342
Cdd:cd02664  122 RTERFRDLDLSfPSVQDLLNYFLSPEKL--TGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIM 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 343 KDVKFPLMLDiyelctpdlqekmVPYRSKFKQVEDKVPEQAPKAKQMAQREVRYEPYafpgdvgsincgyyELQAVLTHQ 422
Cdd:cd02664  200 DNVSINEVLS-------------LPVRVESKSSESPLEKKEEESGDDGELVTRQVHY--------------RLYAVVVHS 252
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148234941 423 GRSSSSGHYLSWV---------------------KRKHDEWIKFDDDKVSIVSPEDILRLSGGGDWHIAYVLLY 475
Cdd:cd02664  253 GYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFY 326
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-475 2.99e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 84.75  E-value: 2.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRytgalrasgemasaqyitaALRDLFDSMDKTSssippiillqflhmafPQ 185
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------TPKELFSQVCRKA----------------PQ 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 FaeKGdqgqYLQQDANEcwvqvmrVLQQKLESTegdsdmetdsgaaataskkNSFIDQFFGIEFESTMKCTESEEeeVTK 265
Cdd:cd02667   46 F--KG----YQQQDSHE-------LLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGT--VSL 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 266 SKETQLQLSC----FINQEV-----KYLFTGlklrlQEEITKFSPSLQRNALYN-KTSRISRLPAYLTIQMVRFFyKEKE 335
Cdd:cd02667   92 VYEPFLDLSLprsdEIKSECsiescLKQFTE-----VEILEGNNKFACENCTKAkKQYLISKLPPVLVIHLKRFQ-QPRS 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 336 SVNAKVLKDVKFPLMLDIYELCTPDLQekmvpyrskfkqvedkVPEqapkakqmAQREVRyepyafpgdvgsincgyYEL 415
Cdd:cd02667  166 ANLRKVSRHVSFPEILDLAPFCDPKCN----------------SSE--------DKSSVL-----------------YRL 204
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 416 QAVLTHQGrSSSSGHYLSWVKRKH----------------------DEWIKFDDDKVSIVSPEDILRLSgggdwhiAYVL 473
Cdd:cd02667  205 YGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVLKSE-------AYLL 276

                 ..
gi 148234941 474 LY 475
Cdd:cd02667  277 FY 278
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-461 2.44e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 79.94  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTGALrasGEMASAQYITAALRDLFDSMDKTSssiPPIILLQFLHMAFPQ 185
Cdd:cd02671   26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI---SSVEQLQSSFLLNPEKYNDELANQ---APRRLLNALREVNPM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 FaekgdQGqYLQQDANECWVQVMRVLQQKLEST-EGDSDMETDSGAAATAS-KKNSFIDQFFGIEFESTMKCTESEE--- 260
Cdd:cd02671  100 Y-----EG-YLQHDAQEVLQCILGNIQELVEKDfQGQLVLRTRCLECETFTeRREDFQDISVPVQESELSKSEESSEisp 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 261 EEVTKSKETQLQLSCF-----INQEVKYLFtglklrlqEEITKFSPSlQRNALYNKtsrisrLPAYLTIQMVRF------ 329
Cdd:cd02671  174 DPKTEMKTLKWAISQFasverIVGEDKYFC--------ENCHHYTEA-ERSLLFDK------LPEVITIHLKCFaangse 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 330 --FYKEKESVNAKVLKdvkfPLMLDIYELCTpdlQEKMvpyrskfkqvedkvpeqapkakqmaqrevryepyafpgDVgs 407
Cdd:cd02671  239 fdCYGGLSKVNTPLLT----PLKLSLEEWST---KPKN--------------------------------------DV-- 271
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148234941 408 incgyYELQAVLTHQGRSSSSGHYLSWVKrkhdeWIKFDDDKVSIVSPEDILRL 461
Cdd:cd02671  272 -----YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEA 315
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-475 1.73e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 75.79  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIrsvpelkealkrytgalrasgemasaqyitaalrdlfdsmdktsssippiillqfLHMafpq 185
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL-------------------------------------------------------SAD---- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 186 faekgdqgqylQQDANECWVQVMRVLqqklestegdsdmetdsgaaataskkNSFIDQFFGIEFESTMKCTESEEEEVTK 265
Cdd:cd02674   22 -----------QQDAQEFLLFLLDGL--------------------------HSIIVDLFQGQLKSRLTCLTCGKTSTTF 64
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 266 SKETQLQLSCFINQEVKY---LFTGLKLRLQEEIT-----KFSPSLQRNALYNKTSRISRLPAYLTIQMVRFFYKEKESV 337
Cdd:cd02674   65 EPFTYLSLPIPSGSGDAPkvtLEDCLRLFTKEETLdgdnaWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 338 naKVLKDVKFPL-MLDiyelctpdlqekMVPYRSKFKQVEDKVpeqapkakqmaqrevryepyafpgdvgsincgyYELQ 416
Cdd:cd02674  145 --KLTTPVTFPLnDLD------------LTPYVDTRSFTGPFK---------------------------------YDLY 177
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 417 AVLTHQGrSSSSGHYLSWVKRKH-DEWIKFDDDKVSIVSPEDILRLSgggdwhiAYVLLY 475
Cdd:cd02674  178 AVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSS-------AYILFY 229
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-475 2.45e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 73.51  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPelkeALKRYTGALRASGE--------------------MASAQYITaaLRDLFDSMDK 165
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIP----SFQWRYDDLENKFPsdvvdpandlncqlikladgLLSGRYSK--PASLKSENDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 166 TSSSIPPIILLQFLHMAFPQFAEKGdqgqylQQDANECWVQVMRVLQQKLESTEGDSdmetdsgaaataskknsFIDQF- 244
Cdd:cd02658   75 YQVGIKPSMFKALIGKGHPEFSTMR------QQDALEFLLHLIDKLDRESFKNLGLN-----------------PNDLFk 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 245 FGIEfeSTMKCTESEEeeVTKSKETQLQLSCFIN---------QEVKYLFTGLKLRLQ-----EEITKFSPSLQRNALYN 310
Cdd:cd02658  132 FMIE--DRLECLSCKK--VKYTSELSEILSLPVPkdeatekeeGELVYEPVPLEDCLKayfapETIEDFCSTCKEKTTAT 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 311 KTSRISRLPAYLTIQMVRFFYKEKESVnakvlkdVKFPLMLDIyelctpdlqekmvpyrskfkqvedkvpeqapkakqma 390
Cdd:cd02658  208 KTTGFKTFPDYLVINMKRFQLLENWVP-------KKLDVPIDV------------------------------------- 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 391 qrevryepyafPGDVGSincGYYELQAVLTHQGRSSSSGHYLSWVKRKHD---EWIKFDDDKVSIV-SPEDILRLsgggd 466
Cdd:cd02658  244 -----------PEELGP---GKYELIAFISHKGTSVHSGHYVAHIKKEIDgegKWVLFNDEKVVASqDPPEMKKL----- 304

                 ....*....
gi 148234941 467 whiAYVLLY 475
Cdd:cd02658  305 ---GYIYFY 310
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
104-472 2.41e-12

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: 67.90  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 104 PCGLTNLGNTCYMNATVQCIRSVPELKEAL-----------------KRYTGALRASGEMASAQYITAALRDLFDSMDKT 166
Cdd:cd02666    1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdeskaelasdypteRRIGGREVSRSELQRSNQFVYELRSLFNDLIHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 167 -SSSIPPIILLQFLHMAfpqfaekgdqgqylQQDANECWVQVMRVLQQKLESTE-GDSDMETDSGAAATASKKNSF---I 241
Cdd:cd02666   81 nTRSVTPSKELAYLALR--------------QQDVTECIDNVLFQLEVALEPISnAFAGPDTEDDKEQSDLIKRLFsgkT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 242 DQffgiefeSTMKCTESEEEEVTKSKETQLQLScfinqeVKYLFTGLKLRLQEEitkfSPSLQrNAL--YNKTSRISRLP 319
Cdd:cd02666  147 KQ-------QLVPESMGNQPSVRTKTERFLSLL------VDVGKKGREIVVLLE----PKDLY-DALdrYFDYDSLTKLP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 320 AYLTIQMVRFFYKEKE---SVNAKVLKDVKfplmlDIYELCTPDLQEKMVPYRSKFKQVEDKVPEqapKAKQMAQrevrY 396
Cdd:cd02666  209 QRSQVQAQLAQPLQRElisMDRYELPSSID-----DIDELIREAIQSESSLVRQAQNELAELKHE---IEKQFDD----L 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 397 EPYAfpgdvgsincgyYELQAVLTHQGrSSSSGHYLSWVKRKHDE-WIKFDDDKVSIVSPEDI-LRLSGGGD--WHIAYV 472
Cdd:cd02666  277 KSYG------------YRLHAVFIHRG-EASSGHYWVYIKDFEENvWRKYNDETVTVVPASEVfLFTLGNTAtpYFLVYV 343
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
5-74 2.26e-11

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: 59.19  E-value: 2.26e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148234941     5 SVNVKWGKEKFDNVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDD-WGNLKIKSGMTLLMMGS 74
Cdd:smart00213   2 ELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRtLADYGIQDGSTIHLVLR 72
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
4-74 2.89e-09

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: 53.35  E-value: 2.89e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148234941   4 YSVNVKWGKEKFDnVELNTDEPPMVFKAQLFALTGVQPDRQKV--MVKGGTLKDDD--WGNLKIKSGMTLLMMGS 74
Cdd:cd01813    1 ITLIVKWSGKEYP-VTVLSSDTVLDLKQRIFELTGVLPKRQKLlgLKVKGKPADDDvkLSSLKLKPNTKIMMMGT 74
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
8-74 8.60e-09

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: 51.86  E-value: 8.60e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148234941   8 VKWGKEKFDnVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDDWGNLKIKSGMTLLMMGS 74
Cdd:cd17047    5 VIWNKEKYD-VKFPLDSTIAELKEHIETLTGVPPAMQKLMYKGLLKDDKTLRELKVTKGAKVMVVGS 70
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
6-72 1.11e-08

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: 51.44  E-value: 1.11e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148234941   6 VNVKWGKEKFDNVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDDW-GNLKIKSGMTLLMM 72
Cdd:cd17039    1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTlSDYGIKDGSTIHLV 68
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
89-264 2.94e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.96  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  89 VEDMTEEQLASAMEL--PCGLTNLGNTCYMNATVQCIRSVPELKEAL--KRYTGALRASGEMASAQYITAALRDLFDSM- 163
Cdd:COG5560  248 VDSIVDDHNRSINKEagTCGLRNLGNTCYMNSALQCLMHTWELRDYFlsDEYEESINEENPLGMHGSVASAYADLIKQLy 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 164 DKTSSSIPPI----ILLQFLHMAfpqfaeKGdqgqYLQQDANECWVQVMRVL-------QQKLESTEGDSDMETDSGAAA 232
Cdd:COG5560  328 DGNLHAFTPSgfkkTIGSFNEEF------SG----YDQQDSQEFIAFLLDGLhedlnriIKKPYTSKPDLSPGDDVVVKK 397
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 148234941 233 TASKK--------NSFIDQFFGIEFESTMKCTESEEEEVT 264
Cdd:COG5560  398 KAKECwwehlkrnDSIITDLFQGMYKSTLTCPGCGSVSIT 437
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
401-475 5.71e-07

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 50.63  E-value: 5.71e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148234941 401 FPGDVGSINcgyYELQAVLTHQGRsSSSGHYLSWV-KRKHDEWIKFDDDKVSIVSPEDILRLS-GGGDWHIAYVLLY 475
Cdd:cd02665  155 FPQIIQQVP---YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfGGGRNPSAYCLMY 227
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
106-466 1.23e-05

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 47.94  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  106 GLTNLGNTCYMNATVQCIRSVpelkEALKRYTGALRASGEmASAQYITAALRDLFDSMDKTSSsipPIILLQFLHmafpQ 185
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHP-RGRDSVALALQRLFYNLQTGEE---PVDTTELTR----S 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  186 FAEKGDQgQYLQQDANEcwvqVMRVLQQKLESTEGDSDMEtdsgaaataskkNSFIDQFFGiEFESTMKCTESEEEEVTK 265
Cdd:COG5077   263 FGWDSDD-SFMQHDIQE----FNRVLQDNLEKSMRGTVVE------------NALNGIFVG-KMKSYIKCVNVNYESARV 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  266 SKETQLQLScfiNQEVKYLFTGLKLRLQEEItkfspsLQRNALYN----------KTSRISRLPAYLTIQMVRFFYKEKE 335
Cdd:COG5077   325 EDFWDIQLN---VKGMKNLQESFRRYIQVET------LDGDNRYNaekhglqdakKGVIFESLPPVLHLQLKRFEYDFER 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941  336 SVNAKVLKDVKFPLMLDIYELCTPDlqekmvpyrSKFKQVEDKVpeqapkakqmaqrevryepyafpgdvgsincgyYEL 415
Cdd:COG5077   396 DMMVKINDRYEFPLEIDLLPFLDRD---------ADKSENSDAV---------------------------------YVL 433
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148234941  416 QAVLTHQGrSSSSGHYLSWVK-RKHDEWIKFDDDKVSIVSPEDILRLSGGGD 466
Cdd:COG5077   434 YGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEENFGGD 484
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
413-475 1.92e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 47.19  E-value: 1.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148234941 413 YELQAVLTHQGrSSSSGHYLSWVKRKHDE-WIKFDDDKVSIVSPEDILRLSgggdwhiAYVLLY 475
Cdd:COG5560  764 YDLYAVDNHYG-GLSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSS-------AYVLFY 819
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
4-74 6.69e-05

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 41.11  E-value: 6.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148234941   4 YSVNVKWGKEKFD-NVELNTDEPPMV--FKAQLFALTGVQPDRQKVMVKGGTLKDDD--WGNLKIKSGMTLLMMGS 74
Cdd:cd01812    1 LTVTVIHGSNKHTiELPSQDEDEPTLqdLAEAIEEVTGVPVENQKLIFKGKSLKDPEqpLSALGVKNGSKIMLIGK 76
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
6-74 1.77e-04

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: 39.85  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148234941    6 VNVK-WGKEKFDnVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDD-WGNLKIKSGMTLLMMGS 74
Cdd:pfam00240   1 ITVKtLDGKKIT-LEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQtLGEYGIEDGSTIHLVLR 70
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
106-138 2.68e-04

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 42.35  E-value: 2.68e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 148234941 106 GLTNLGNTCYMNATVQCIRSVPELKEALKRYTG 138
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE 33
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-447 3.67e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 42.13  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 309 YNKTSRISRLPAYLTIQMVRFFYKEkeSVNAKVLKDVKFPLMLDIyelctPDLqekmvpyrskfkqVEDKVPEQApkaKQ 388
Cdd:cd02670   89 YFNNSVFAKAPSCLIICLKRYGKTE--GKAQKMFKKILIPDEIDI-----PDF-------------VADDPRACS---KC 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148234941 389 MAQREVRYEPYAFPGDVGSINCgyyELQAVLTHQGRSSSSGHYLSWVKRKHDE------------WIKFDD 447
Cdd:cd02670  146 QLECRVCYDDKDFSPTCGKFKL---SLCSAVCHRGTSLETGHYVAFVRYGSYSltetdneaynaqWVFFDD 213
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
29-72 6.72e-04

ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain.


Pssm-ID: 340573  Cd Length: 71  Bit Score: 38.10  E-value: 6.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148234941  29 FKAQLFALTGVQPDRQKVMVKGGTLKDDD--WGNLKIKSGMTLLMM 72
Cdd:cd17053   26 VKAMIEDQSGVPPNEQILVYNGKRLEDGDktLGEYGIKTGDTLYLL 71
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
413-464 9.52e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 40.98  E-value: 9.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148234941 413 YELQAVLTHQGRSSSSGHYLSWVKR--KHDEWIKFDDDKVSIVSPEDIL---RLSGG 464
Cdd:cd02673  184 YSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGY 240
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
413-475 1.41e-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: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148234941 413 YELQAVLTHQGrSSSSGHYLSWvKRK----------------------HDEWIKFDDDKVSIVSPEDILrLSGGgdwhiA 470
Cdd:cd02662  163 YRLRAVVVHYG-SHSSGHYVCY-RRKplfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVL-EQKS-----A 234

                 ....*
gi 148234941 471 YVLLY 475
Cdd:cd02662  235 YMLFY 239
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
5-75 7.58e-03

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 35.31  E-value: 7.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148234941   5 SVNVKW-GKEKFDnVELNTDEPPMVFKAQLFALTGVQPDRQKVMVKGGTLKDDDWGNL-KIKSGMTLLMMGSA 75
Cdd:cd16106    2 KVTVKCsNGKKFT-VEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSyKIQDGHTVHLVKGA 73
 
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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