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Conserved domains on  [gi|24583343|ref|NP_609377|]
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ubiquitin specific protease 14, isoform A [Drosophila melanogaster]

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 ...
105-467 1.18e-156

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: 446.39  E-value: 1.18e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFSISSAMKSIFAQMEKGTT-VTPIVLLQALHRASPQFA 183
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIEFLQLLRMAFPQFA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 184 QTGENGTYRQQDANECWAEILKMLQQKLRPKnqepsntvqKRHSSFIDQFFGGTFEVKMSSEEDP-DEPSTVTSENFLQL 262
Cdd:cd02657  81 EKQNQGGYAQQDAEECWSQLLSVLSQKLPGA---------GSKGSFIDQLFGIELETKMKCTESPdEEEVSTESEYKLQC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 263 SCFISMDVKYMQSGLKSKMKEQLVKKSETLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKEGINAKVLKDIKFPIDFDA 342
Cdd:cd02657 152 HISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 343 FELCTPelqnklcpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgsnnSGYYTLQAVLTHKGRSSSSGH 422
Cdd:cd02657 232 YELCTP-----------------------------------------------------SGYYELVAVITHQGRSADSGH 258
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 24583343 423 YVAWVRSSG-DVWFKFDDDEVSAVATDEILRLSGGGDWHCAYVLLY 467
Cdd:cd02657 259 YVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLY 304
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-75 1.04e-35

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: 126.96  E-value: 1.04e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583343   4 FKVKVKWGRELYTDIVVNTDEEPILFKAQLFALTGVQPDRQKVMCKGGILKDDQWN--LQIKDGAVVLLLGSKE 75
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 ...
105-467 1.18e-156

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: 446.39  E-value: 1.18e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFSISSAMKSIFAQMEKGTT-VTPIVLLQALHRASPQFA 183
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIEFLQLLRMAFPQFA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 184 QTGENGTYRQQDANECWAEILKMLQQKLRPKnqepsntvqKRHSSFIDQFFGGTFEVKMSSEEDP-DEPSTVTSENFLQL 262
Cdd:cd02657  81 EKQNQGGYAQQDAEECWSQLLSVLSQKLPGA---------GSKGSFIDQLFGIELETKMKCTESPdEEEVSTESEYKLQC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 263 SCFISMDVKYMQSGLKSKMKEQLVKKSETLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKEGINAKVLKDIKFPIDFDA 342
Cdd:cd02657 152 HISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 343 FELCTPelqnklcpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgsnnSGYYTLQAVLTHKGRSSSSGH 422
Cdd:cd02657 232 YELCTP-----------------------------------------------------SGYYELVAVITHQGRSADSGH 258
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 24583343 423 YVAWVRSSG-DVWFKFDDDEVSAVATDEILRLSGGGDWHCAYVLLY 467
Cdd:cd02657 259 YVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLY 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
104-467 1.09e-55

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 187.65  E-value: 1.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   104 AGLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFS-ISSAMKSIFAQMEKGTT---VTPIVLLQALHRAS 179
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInLLCALRDLFKALQKNSKsssVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   180 PQFAqtgengTYRQQDANECWAEILKMLQQKLRPKNqepsntvQKRHSSFIDQFFGGTFE-----VKMSSEEDPDEPSTV 254
Cdd:pfam00443  81 PDFS------GYKQQDAQEFLLFLLDGLHEDLNGNH-------STENESLITDLFRGQLKsrlkcLSCGEVSETFEPFSD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   255 TS---ENFLQLSCFISMDVKYMQSGLKSKMKEQLVKKSETLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKegINAKVL 331
Cdd:pfam00443 148 LSlpiPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRS--TWEKLN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   332 KDIKFPIDFDAFELCTPELQNKLcpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgsNNSGYYTLQAVL 411
Cdd:pfam00443 226 TEVEFPLELDLSRYLAEELKPKT---------------------------------------------NNLQDYRLVAVV 260
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24583343   412 THKGrSSSSGHYVAWVRSSGDV-WFKFDDDEVSAVATDEILRLSGggdwhcAYVLLY 467
Cdd:pfam00443 261 VHSG-SLSSGHYIAYIKAYENNrWYKFDDEKVTEVDEETAVLSSS------AYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-75 1.04e-35

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: 126.96  E-value: 1.04e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583343   4 FKVKVKWGRELYTDIVVNTDEEPILFKAQLFALTGVQPDRQKVMCKGGILKDDQWN--LQIKDGAVVLLLGSKE 75
Cdd:cd16104   2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLskLKLKDGQTLMLMGSAE 75
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
105-450 2.03e-15

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 76.38  E-value: 2.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCL----NAVPELRTALSTFSNDGTDTMSTAFSISSamksiFAQMEKGTTVTPIVLLQALHRASP 180
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILalylPKLDELLDDLSKELKVLKNVIRKPEPDLN-----QEEALKLFTALWSSKEHKVGWIPP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 181 QfaqtgengtYRQQDANEC------WAEILKMLQQKLRPKNQEPSNTvqkrhSSFIDQFFGGTFEVKMSSEEDPDEpstv 254
Cdd:COG5533  76 M---------GSQEDAHELlgklldELKLDLVNSFTIRIFKTTKDKK-----KTSTGDWFDIIIELPDQTWVNNLK---- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 255 TSENFLQLSCFISMDVKymqsGLKSKMKEQlvkksetLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKegiNAKVLKDI 334
Cdd:COG5533 138 TLQEFIDNMEELVDDET----GVKAKENEE-------LEVQAKQEYEVSFVKLPKILTIQLKRFANLGG---NQKIDTEV 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 335 kfpidfdafelctpelqnklcpmrskfkdleDKKMEVDVVkrnepneekkdvkyeqfwFDDDLGSNNSGYYTLQAVLTHK 414
Cdd:COG5533 204 -------------------------------DEKFELPVK------------------HDQILNIVKETYYDLVGFVLHQ 234
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 24583343 415 GrSSSSGHYVAWVRsSGDVWFKFDDDEVSAVATDEI 450
Cdd:COG5533 235 G-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEA 268
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
4-73 1.21e-06

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


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.10  E-value: 1.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24583343      4 FKVKVKWGRELYTDIVVNTDEePIL-FKAQLFALTGVQPDRQKVMCKGGILKDDQW--NLQIKDGAVVLLLGS 73
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSD-TVSeLKEKIAELTGIPPEQQRLIYKGKVLEDDRTlaDYGIQDGSTIHLVLR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
29-74 2.13e-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: 39.46  E-value: 2.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 24583343    29 FKAQLFALTGVQPDRQKVMCKGGILKDDQwNLQ---IKDGAVVLLLGSK 74
Cdd:pfam00240  24 LKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGeygIEDGSTIHLVLRQ 71
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 1.18e-156

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: 446.39  E-value: 1.18e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFSISSAMKSIFAQMEKGTT-VTPIVLLQALHRASPQFA 183
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIEFLQLLRMAFPQFA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 184 QTGENGTYRQQDANECWAEILKMLQQKLRPKnqepsntvqKRHSSFIDQFFGGTFEVKMSSEEDP-DEPSTVTSENFLQL 262
Cdd:cd02657  81 EKQNQGGYAQQDAEECWSQLLSVLSQKLPGA---------GSKGSFIDQLFGIELETKMKCTESPdEEEVSTESEYKLQC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 263 SCFISMDVKYMQSGLKSKMKEQLVKKSETLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKEGINAKVLKDIKFPIDFDA 342
Cdd:cd02657 152 HISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 343 FELCTPelqnklcpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgsnnSGYYTLQAVLTHKGRSSSSGH 422
Cdd:cd02657 232 YELCTP-----------------------------------------------------SGYYELVAVITHQGRSADSGH 258
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 24583343 423 YVAWVRSSG-DVWFKFDDDEVSAVATDEILRLSGGGDWHCAYVLLY 467
Cdd:cd02657 259 YVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLY 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
104-467 1.09e-55

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 187.65  E-value: 1.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   104 AGLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFS-ISSAMKSIFAQMEKGTT---VTPIVLLQALHRAS 179
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInLLCALRDLFKALQKNSKsssVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   180 PQFAqtgengTYRQQDANECWAEILKMLQQKLRPKNqepsntvQKRHSSFIDQFFGGTFE-----VKMSSEEDPDEPSTV 254
Cdd:pfam00443  81 PDFS------GYKQQDAQEFLLFLLDGLHEDLNGNH-------STENESLITDLFRGQLKsrlkcLSCGEVSETFEPFSD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   255 TS---ENFLQLSCFISMDVKYMQSGLKSKMKEQLVKKSETLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKegINAKVL 331
Cdd:pfam00443 148 LSlpiPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRS--TWEKLN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343   332 KDIKFPIDFDAFELCTPELQNKLcpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgsNNSGYYTLQAVL 411
Cdd:pfam00443 226 TEVEFPLELDLSRYLAEELKPKT---------------------------------------------NNLQDYRLVAVV 260
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24583343   412 THKGrSSSSGHYVAWVRSSGDV-WFKFDDDEVSAVATDEILRLSGggdwhcAYVLLY 467
Cdd:pfam00443 261 VHSG-SLSSGHYIAYIKAYENNrWYKFDDEKVTEVDEETAVLSSS------AYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
105-467 4.27e-51

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: 173.82  E-value: 4.27e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLnavpelrtalstfsndgtdtmstafsissamksifaqmekgttvtpivllqalhraspqfaq 184
Cdd:cd02257   1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 185 tgengTYRQQDANECWAEILKMLQQKLRPKNQEPSNtvQKRHSSFIDQFFGGTFEVKMSSEEDPDEPSTVTSENFLQLSC 264
Cdd:cd02257  19 -----FSEQQDAHEFLLFLLDKLHEELKKSSKRTSD--SSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 265 FI-SMDVKYMQSGLKSKMKEQLVKKSETLGRDAK----YIRTYLVSRLPAYLTVQFVRFQYKGKeGINAKVLKDIKFPID 339
Cdd:cd02257  92 PVkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKkkqeATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 340 FDAFELCTPElqnklcpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwFDDDLGSNNSGYYTLQAVLTHKGRSSS 419
Cdd:cd02257 171 LDLSPYLSEG-------------------------------------------EKDSDSDNGSYKYELVAVVVHSGTSAD 207
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 24583343 420 SGHYVAWVRSSG-DVWFKFDDDEVSAVATDEILRLsgGGDWHCAYVLLY 467
Cdd:cd02257 208 SGHYVAYVKDPSdGKWYKFNDDKVTEVSEEEVLEF--GSLSSSAYILFY 254
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-75 1.04e-35

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: 126.96  E-value: 1.04e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583343   4 FKVKVKWGRELYTDIVVNTDEEPILFKAQLFALTGVQPDRQKVMCKGGILKDDQWN--LQIKDGAVVLLLGSKE 75
Cdd:cd16104   2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLskLKLKDGQTLMLMGSAE 75
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
103-468 2.23e-33

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: 128.16  E-value: 2.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 103 PAGLTNLGNTCYMNATVQCLNAVPELRTALSTFsNDGTDTMSTAFSISSAMKSIFAQM--EKGTTVTPIVLLQALHRASP 180
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSR-EHSKDCCNEGFCMMCALEAHVERAlaSSGPGSAPRIFSSNLKQISK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 181 QFaqtgenGTYRQQDANECWAEILKMLQQ-KLRPKNQEPSNTVQKRHSSFIDQFFGGTF--EVKMSSEEDPDEpstvTSE 257
Cdd:cd02661  80 HF------RIGRQEDAHEFLRYLLDAMQKaCLDRFKKLKAVDPSSQETTLVQQIFGGYLrsQVKCLNCKHVSN----TYD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 258 NFLQLSCFIsMDVKYMQSGLkskmkEQLVkKSETLGRDAKYI-----------RTYLVSRLPAYLTVQFVRFQYKGKEGI 326
Cdd:cd02661 150 PFLDLSLDI-KGADSLEDAL-----EQFT-KPEQLDGENKYKcerckkkvkasKQLTIHRAPNVLTIHLKRFSNFRGGKI 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 327 NakvlKDIKFPIDFDafelctpelqnkLCP-MRSKfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgSNNSGYY 405
Cdd:cd02661 223 N----KQISFPETLD------------LSPyMSQP--------------------------------------NDGPLKY 248
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24583343 406 TLQAVLTHKGRSSSSGHYVAWVRSSGDVWFKFDDDEVSAVATDEILRLSgggdwhcAYVLLYA 468
Cdd:cd02661 249 KLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQK-------AYILFYI 304
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 8.00e-28

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 113.24  E-value: 8.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRT-ALSTFSNDGTDTMSTAFSISSAMKSIFAQME-KGTTV--TPIVLLQALHRASP 180
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYySGDRSpyGPINLLYLSWKHSR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 181 QFAqtgengTYRQQDANECWAEILKMLQQKLRPKNQEPSNTvqKRHSSFIDQFFGGTFEV--------KMSSEEDPdeps 252
Cdd:cd02660  82 NLA------GYSQQDAHEFFQFLLDQLHTHYGGDKNEANDE--SHCNCIIHQTFSGSLQSsvtcqrcgGVSTTVDP---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 253 tvtsenFLQLScfISMDVKYMQSGLKSKMKEQLVK----------KSETLGRDA----------KYIRTYLVSRLPAYLT 312
Cdd:cd02660 150 ------FLDLS--LDIPNKSTPSWALGESGVSGTPtlsdcldrftRPEKLGDFAykcsgcgstqEATKQLSIKKLPPVLC 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 313 VQFVRFQYKGkEGINAKVLKDIKFPIDFDAFELCTPELQnklcpmrskfkdleDKKMEvdvvkrnepNEEKKDVKYEqfw 392
Cdd:cd02660 222 FQLKRFEHSL-NKTSRKIDTYVQFPLELNMTPYTSSSIG--------------DTQDS---------NSLDPDYTYD--- 274
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24583343 393 fdddlgsnnsgyytLQAVLTHKGrSSSSGHYVAWVRSSGDVWFKFDDDEVSAVATDEILRLSgggdwhcAYVLLY 467
Cdd:cd02660 275 --------------LFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQ-------AYLLFY 327
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 1.61e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 106.74  E-value: 1.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTFS--------NDGTDTMSTAFSISSAMKSIFAQMEKG--TTVTPIVLLQA 174
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNstedaelkNMPPDKPHEPQTIIDQLQLIFAQLQFGnrSVVDPSGFVKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 175 LhraspqfaqtgENGTYRQQDANECWAEILKMLQQKLrpknQEPSNTVQKrhsSFIDQFFGGTFEVKMSSEEDPDEPSTV 254
Cdd:cd02668  81 L-----------GLDTGQQQDAQEFSKLFLSLLEAKL----SKSKNPDLK---NIVQDLFRGEYSYVTQCSKCGRESSLP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 255 TSenFLQLSCFISmdvkyMQSGLKSKMKEQLvkKSETLGRDAKY-----------IRTYLVSRLPAYLTVQFVRFQYKGK 323
Cdd:cd02668 143 SK--FYELELQLK-----GHKTLEECIDEFL--KEEQLTGDNQYfcescnsktdaTRRIRLTTLPPTLNFQLLRFVFDRK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 324 EGINAKVLKDIKFPIDFDAFELCTPELQNKLCpmrskfkdledkkmevdvvkrnepneekkdvkyeqfwfdddlgsnnsg 403
Cdd:cd02668 214 TGAKKKLNASISFPEILDMGEYLAESDEGSYV------------------------------------------------ 245
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24583343 404 yYTLQAVLTHKGRSSSSGHYVAWVR-SSGDVWFKFDDDEVSAV-----------ATDEILRLSGGGDWHC---AYVLLY 467
Cdd:cd02668 246 -YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMpgkplklgnseDPAKPRKSEIKKGTHSsrtAYMLVY 323
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 1.93e-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: 103.49  E-value: 1.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALstFSNDGTDTMSTAFSISSAMKSIFAQM-----EKGTTVTpivllqalhras 179
Cdd:cd02659   4 GLKNQGATCYMNSLLQQLYMTPEFRNAV--YSIPPTEDDDDNKSVPLALQRLFLFLqlsesPVKTTEL------------ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 180 pqFAQTGENG-----TYRQQDANECWAEILKMLQQKLRPKNQEPSntvqkrhssfIDQFFGGTF-------EVKMSSEED 247
Cdd:cd02659  70 --TDKTRSFGwdslnTFEQHDVQEFFRVLFDKLEEKLKGTGQEGL----------IKNLFGGKLvnyiickECPHESERE 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 248 pdepstvtsENFLQlscfISMDVKYMQSGLKSkmKEQLVKKsETLGRDAKY-----------IRTYLVSRLPAYLTVQFV 316
Cdd:cd02659 138 ---------EYFLD----LQVAVKGKKNLEES--LDAYVQG-ETLEGDNKYfcekcgkkvdaEKGVCFKKLPPVLTLQLK 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 317 RFQYKGKEGINAKVLKDIKFPIDFDafelctpelqnkLCPMrskfkdledkkMEVDVVKRNEPNEEKKDVKYEqfwfddd 396
Cdd:cd02659 202 RFEFDFETMMRIKINDRFEFPLELD------------MEPY-----------TEKGLAKKEGDSEKKDSESYI------- 251
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 397 lgsnnsgyYTLQAVLTHKGrSSSSGHYVAWVRS-SGDVWFKFDDDEVSAVATDEILRLSGGGD---------------WH 460
Cdd:cd02659 252 --------YELHGVLVHSG-DAHGGHYYSYIKDrDDGKWYKFNDDVVTPFDPNDAEEECFGGEetqktydsgprafkrTT 322

                ....*..
gi 24583343 461 CAYVLLY 467
Cdd:cd02659 323 NAYMLFY 329
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 1.97e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 99.77  E-value: 1.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTfsndgtdtmstafsissamksifaqmekgttvTPIVLLQALHRASPQFaq 184
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------------------------------TPKELFSQVCRKAPQF-- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 185 tgeNGtYRQQDANEcwaeILKMLQQKLRPknqepsntvqkrhssFIDQFFGGTFEVKMSSEedpdEPSTVTS--ENFLQL 262
Cdd:cd02667  47 ---KG-YQQQDSHE----LLRYLLDGLRT---------------FIDSIFGGELTSTIMCE----SCGTVSLvyEPFLDL 99
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 263 SCFISMDVKYMQSgLKSKMKeQLVKKSETLGRDA-------KYIRTYLVSRLPAYLTVQFVRFQyKGKEGINAKVLKDIK 335
Cdd:cd02667 100 SLPRSDEIKSECS-IESCLK-QFTEVEILEGNNKfacenctKAKKQYLISKLPPVLVIHLKRFQ-QPRSANLRKVSRHVS 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 336 FPIDFDAFELCTPELQNklcpmrskfkdledkkmevdvvkrnepNEEKKDVKyeqfwfdddlgsnnsgyYTLQAVLTHKG 415
Cdd:cd02667 177 FPEILDLAPFCDPKCNS---------------------------SEDKSSVL-----------------YRLYGVVEHSG 212
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583343 416 rSSSSGHYVAWVR----------------------SSGDVWFKFDDDEVSAVATDEILRLSgggdwhcAYVLLY 467
Cdd:cd02667 213 -TMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSE-------AYLLFY 278
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 1.71e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 88.52  E-value: 1.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAvpelrtalstfsndgtDTMSTAFsiSSAMKSIFAQMEKGTTVTPIVLLQALHRASPQFaq 184
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF----------------ENLLTCL--KDLFESISEQKKRTGVISPKKFITRLKRENELF-- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 185 tgenGTYRQQDA--------NECwAEILKMLQQKLRPKNQEPSNTVQKRHSSFIDQFFGG--TFEVKMSSEEdpdepsTV 254
Cdd:cd02663  61 ----DNYMHQDAheflnfllNEI-AEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGilTNETRCLTCE------TV 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 255 TS--ENFLQLScfISMDVKY-MQSGLKSkmkeqlVKKSETLGRDAKYI-----------RTYLVSRLPAYLTVQFVRFQY 320
Cdd:cd02663 130 SSrdETFLDLS--IDVEQNTsITSCLRQ------FSATETLCGRNKFYcdeccslqeaeKRMKIKKLPKILALHLKRFKY 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 321 KGKEGINAKVLKDIKFPidfdafelctpeLQNKLCPMRSkfkdledkkmevdvvkrnepNEEKKDVKYEqfwfdddlgsn 400
Cdd:cd02663 202 DEQLNRYIKLFYRVVFP------------LELRLFNTTD--------------------DAENPDRLYE----------- 238
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24583343 401 nsgyytLQAVLTHKGRSSSSGHYVAWVRSSGdVWFKFDDDEVSAVATDEILRLSGGG-DWHCAYVLLY 467
Cdd:cd02663 239 ------LVAVVVHIGGGPNHGHYVSIVKSHG-GWLLFDDETVEKIDENAVEEFFGDSpNQATAYVLFY 299
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
94-468 6.93e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 84.56  E-value: 6.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343  94 AEAATAMRLP-AGLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTdtmstafSISSAMKSIFAQMEKGT----TVTP 168
Cdd:cd02671  14 SCEKRENLLPfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS-------SVEQLQSSFLLNPEKYNdelaNQAP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 169 IVLLQALHRASPQFAqtgengTYRQQDANECWAEIL--------KMLQQK--LRPKNQEpSNTVQKRHSSFIDqffggtf 238
Cdd:cd02671  87 RRLLNALREVNPMYE------GYLQHDAQEVLQCILgniqelveKDFQGQlvLRTRCLE-CETFTERREDFQD------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 239 evkMSSEEDPDEPSTVTSenflqlSCFISMDVKYMQSGLKSKMkEQLVKKSETLGRDaKY-----------IRTYLVSRL 307
Cdd:cd02671 153 ---ISVPVQESELSKSEE------SSEISPDPKTEMKTLKWAI-SQFASVERIVGED-KYfcenchhyteaERSLLFDKL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 308 PAYLTVQFVRFQYKGKE----GINAKVLKDIKFPIDFDAFELCTpelqnklcpmrskfkdledkkmevdvvkrnepnEEK 383
Cdd:cd02671 222 PEVITIHLKCFAANGSEfdcyGGLSKVNTPLLTPLKLSLEEWST---------------------------------KPK 268
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 384 KDVkyeqfwfdddlgsnnsgyYTLQAVLTHKGRSSSSGHYVAWVRssgdvWFKFDDDEVSAVATDEILRLSGGGDWHCA- 462
Cdd:cd02671 269 NDV------------------YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEALSPNTSSTSt 325

                ....*..
gi 24583343 463 -YVLLYA 468
Cdd:cd02671 326 pYLLFYK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 2.24e-17

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 82.76  E-value: 2.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVP-------ELRTALSTFSNDGTDTMSTAFS-ISSAMKS-------IFAQMEKGTTV--T 167
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPsfqwrydDLENKFPSDVVDPANDLNCQLIkLADGLLSgryskpaSLKSENDPYQVgiK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 168 PIVLLQALHRASPQFaqtgenGTYRQQDANECWAEILKMLQQKLRPKNQEPSNTVqkrhssfidqffggtFEVKMSSEED 247
Cdd:cd02658  81 PSMFKALIGKGHPEF------STMRQQDALEFLLHLIDKLDRESFKNLGLNPNDL---------------FKFMIEDRLE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 248 PDEPSTVTSENflQLSCFISMDVKYMQSGLKSKMKEqlvkksetlgrdaKYIRTYLVSRLPAYLTVQFVRFQYKG-KEGI 326
Cdd:cd02658 140 CLSCKKVKYTS--ELSEILSLPVPKDEATEKEEGEL-------------VYEPVPLEDCLKAYFAPETIEDFCSTcKEKT 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 327 NAKVLKDIK-FPiDFDAFELctpelqnklcpmrSKFKDLED---KKMEVDVvkrnepneekkDVkyeqfwfDDDLGSnns 402
Cdd:cd02658 205 TATKTTGFKtFP-DYLVINM-------------KRFQLLENwvpKKLDVPI-----------DV-------PEELGP--- 249
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24583343 403 GYYTLQAVLTHKGRSSSSGHYVAWVR---SSGDVWFKFDDDEVSAVATDEILRLSGggdwhcaYVLLY 467
Cdd:cd02658 250 GKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLG-------YIYFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 2.43e-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: 80.79  E-value: 2.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAvpelrtalstfsndgtdtmstafsissamksifaqmekgttvtpivllqalhraspqfaq 184
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 185 tgengtyRQQDANECWAEILKMLqqklrpknqepsntvqkrHSsFIDQFFGG----------------TFEVKMS-SEED 247
Cdd:cd02674  21 -------DQQDAQEFLLFLLDGL------------------HS-IIVDLFQGqlksrltcltcgktstTFEPFTYlSLPI 74
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 248 PDEpSTVTSENFLQlSCFI------SMDVKYMQSGLKSKMKEQLVKKSEtlgrdakyirtylVSRLPAYLTVQFVRFQYK 321
Cdd:cd02674  75 PSG-SGDAPKVTLE-DCLRlftkeeTLDGDNAWKCPKCKKKRKATKKLT-------------ISRLPKVLIIHLKRFSFS 139
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 322 GKEG--INAKVlkdiKFPIDfdafelctpelqnklcpmrskfkDLEDKKmevdvvkrnepneekkdvkyeqfwFDDDLGS 399
Cdd:cd02674 140 RGSTrkLTTPV----TFPLN-----------------------DLDLTP------------------------YVDTRSF 168
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24583343 400 NNSGYYTLQAVLTHKGrSSSSGHYVAWVRSS-GDVWFKFDDDEVSAVATDEILRLSgggdwhcAYVLLY 467
Cdd:cd02674 169 TGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNeTNDWYKFDDSRVTKVSESSVVSSS-------AYILFY 229
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-467 1.08e-16

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 81.00  E-value: 1.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELR-TALSTFSNDGTDTMSTAFSIssAMKSIFAQMEKGTTVTPI--VLLQALhraSPQ 181
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRrQVLSLNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEAPPdyFLEASR---PPW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 182 FAQTgengtyRQQDAnecwAEILKMLQQKLrpknqepsntvqkrhSSFIDQFFGGTFEVKMSSEEDPDEPSTVTSENFLQ 261
Cdd:cd02664  76 FTPG------SQQDC----SEYLRYLLDRL---------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 262 LS-CFISMDVKYMQSGlkskmkeqlvkksETLGRDAKY-----------IRTYLVSRLPAYLTVQFVRFQYKGKEGINAK 329
Cdd:cd02664 131 LSfPSVQDLLNYFLSP-------------EKLTGDNQYycekcaslqdaEKEMKVTGAPEYLILTLLRFSYDQKTHVREK 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 330 VLKDIKFPIDFDAfelctpelqnklcPMRSKFKDLEDkkmeVDVVKRNEPNeekkdvkyeqfwfDDDLGSNNSGYYTLQA 409
Cdd:cd02664 198 IMDNVSINEVLSL-------------PVRVESKSSES----PLEKKEEESG-------------DDGELVTRQVHYRLYA 247
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24583343 410 VLTHKGRSSSSGHYVAWVRSSGDV---------------------WFKFDDDEVSAVATDEILRLSGGGDWHCAYVLLY 467
Cdd:cd02664 248 VVVHSGYSSESGHYFTYARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
105-450 2.03e-15

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 76.38  E-value: 2.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCL----NAVPELRTALSTFSNDGTDTMSTAFSISSamksiFAQMEKGTTVTPIVLLQALHRASP 180
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILalylPKLDELLDDLSKELKVLKNVIRKPEPDLN-----QEEALKLFTALWSSKEHKVGWIPP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 181 QfaqtgengtYRQQDANEC------WAEILKMLQQKLRPKNQEPSNTvqkrhSSFIDQFFGGTFEVKMSSEEDPDEpstv 254
Cdd:COG5533  76 M---------GSQEDAHELlgklldELKLDLVNSFTIRIFKTTKDKK-----KTSTGDWFDIIIELPDQTWVNNLK---- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 255 TSENFLQLSCFISMDVKymqsGLKSKMKEQlvkksetLGRDAKYIRTYLVSRLPAYLTVQFVRFQYKGKegiNAKVLKDI 334
Cdd:COG5533 138 TLQEFIDNMEELVDDET----GVKAKENEE-------LEVQAKQEYEVSFVKLPKILTIQLKRFANLGG---NQKIDTEV 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 335 kfpidfdafelctpelqnklcpmrskfkdleDKKMEVDVVkrnepneekkdvkyeqfwFDDDLGSNNSGYYTLQAVLTHK 414
Cdd:COG5533 204 -------------------------------DEKFELPVK------------------HDQILNIVKETYYDLVGFVLHQ 234
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 24583343 415 GrSSSSGHYVAWVRsSGDVWFKFDDDEVSAVATDEI 450
Cdd:COG5533 235 G-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEA 268
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
103-468 6.49e-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: 66.75  E-value: 6.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 103 PAGLTNLGNTCYMNATVQCLNAVPELRTALSTFSndgtdtmstAFSISSAMKSIFAQMEKGTTVTPIVLLQALhraspQF 182
Cdd:cd02666   1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFD---------ESKAELASDYPTERRIGGREVSRSELQRSN-----QF 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 183 AQ-----------TGE----------NGTYRQQDANECwaeILKMLQQ-----KLRPKNQEPSNTV-QKRHSSFIDQFFG 235
Cdd:cd02666  67 VYelrslfndlihSNTrsvtpskelaYLALRQQDVTEC---IDNVLFQlevalEPISNAFAGPDTEdDKEQSDLIKRLFS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 236 GTFEVKMSSEEDPDEPSTVT-SENFLQLScfismdVKYMQSGLKSKMKEQLVKKSETLGRdakYIRTYLVSRLPAYLTVQ 314
Cdd:cd02666 144 GKTKQQLVPESMGNQPSVRTkTERFLSLL------VDVGKKGREIVVLLEPKDLYDALDR---YFDYDSLTKLPQRSQVQ 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 315 FVRFQYKGKEGI---NAKVLKDIKfpiDFDAFELCTPELQNKLCPMRSKFKDLEDKKMEvdvvkrnepneekkdvkyEQF 391
Cdd:cd02666 215 AQLAQPLQRELIsmdRYELPSSID---DIDELIREAIQSESSLVRQAQNELAELKHEIE------------------KQF 273
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24583343 392 wfdDDLGSNNsgyYTLQAVLTHKGrSSSSGHYVAWVRS-SGDVWFKFDDDEVSAV-ATDEILRLSGGGDwhCAYVLLYA 468
Cdd:cd02666 274 ---DDLKSYG---YRLHAVFIHRG-EASSGHYWVYIKDfEENVWRKYNDETVTVVpASEVFLFTLGNTA--TPYFLVYV 343
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
7-73 6.91e-08

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: 49.55  E-value: 6.91e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24583343   7 KVKWGRELYtDIVVNTDEEPILFKAQLFALTGVQPDRQKVMCKgGILKDDQW--NLQIKDGAVVLLLGS 73
Cdd:cd17047   4 KVIWNKEKY-DVKFPLDSTIAELKEHIETLTGVPPAMQKLMYK-GLLKDDKTlrELKVTKGAKVMVVGS 70
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
6-71 9.75e-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: 48.75  E-value: 9.75e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24583343   6 VKVKWGRELYTDIVVNTDEePIL-FKAQLFALTGVQPDRQKVMCKGGILKDDQW--NLQIKDGAVVLLL 71
Cdd:cd17039   1 ITVKTLDGKTYTVEVDPDD-TVAdLKEKIEEKTGIPVEQQRLIYNGKELKDDKTlsDYGIKDGSTIHLV 68
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
105-246 1.41e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 54.12  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTFSNDGTDTMSTAFSISSAMKSIFAQMEKgttvtpIVLLQALHRASP-QFA 183
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIK------QLYDGNLHAFTPsGFK 340
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24583343 184 QT-GENGT----YRQQDANECWAEILKMLQQKLrpknqepSNTVQKRHSSFIDQFFGGTFEVKMSSEE 246
Cdd:COG5560 341 KTiGSFNEefsgYDQQDSQEFIAFLLDGLHEDL-------NRIIKKPYTSKPDLSPGDDVVVKKKAKE 401
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
105-458 2.49e-07

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 53.34  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343  105 GLTNLGNTCYMNATVQCLNAVPELRT---ALSTFSNDGTDtmstafSISSAMKSIFAQMEKGTTvtPIVLLQAlhraspq 181
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFRKdvyGIPTDHPRGRD------SVALALQRLFYNLQTGEE--PVDTTEL------- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343  182 faqTGENG-----TYRQQDANEcwaeILKMLQQKLRpknqepsntvQKRHSSFIDQFFGGTFEVKMSSE---EDPDEPST 253
Cdd:COG5077  260 ---TRSFGwdsddSFMQHDIQE----FNRVLQDNLE----------KSMRGTVVENALNGIFVGKMKSYikcVNVNYESA 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343  254 vTSENFLQlscfISMDVKYMqSGLKSKMKEQLvkKSETLGRDAKYI----------RTYLVSRLPAYLTVQFVRFQYKGK 323
Cdd:COG5077  323 -RVEDFWD----IQLNVKGM-KNLQESFRRYI--QVETLDGDNRYNaekhglqdakKGVIFESLPPVLHLQLKRFEYDFE 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343  324 EGINAKVLKDIKFPIDFDAfelctpelqnklcpmrSKFKDLEDKKMEvdvvkrnepneekkdvkyeqfwfdddlgsNNSG 403
Cdd:COG5077  395 RDMMVKINDRYEFPLEIDL----------------LPFLDRDADKSE-----------------------------NSDA 429
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24583343  404 YYTLQAVLTHKGrSSSSGHYVAWVRSSGD-VWFKFDDDEVSAVATDEILRLSGGGD 458
Cdd:COG5077  430 VYVLYGVLVHSG-DLHEGHYYALLKPEKDgRWYKFDDTRVTRATEKEVLEENFGGD 484
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
4-73 1.21e-06

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


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.10  E-value: 1.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24583343      4 FKVKVKWGRELYTDIVVNTDEePIL-FKAQLFALTGVQPDRQKVMCKGGILKDDQW--NLQIKDGAVVLLLGS 73
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSD-TVSeLKEKIAELTGIPPEQQRLIYKGKVLEDDRTlaDYGIQDGSTIHLVLR 72
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
4-74 6.81e-06

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: 43.80  E-value: 6.81e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24583343   4 FKVKVKWGRELYT-DIVVNTDEEPIL--FKAQLFALTGVQPDRQKVMCKGGILKDDQWNLQ---IKDGAVVLLLGSK 74
Cdd:cd01812   1 LTVTVIHGSNKHTiELPSQDEDEPTLqdLAEAIEEVTGVPVENQKLIFKGKSLKDPEQPLSalgVKNGSKIMLIGKK 77
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
405-456 1.71e-05

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 45.98  E-value: 1.71e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24583343 405 YTLQAVLTHKGRSSSSGHYVAWVRSS--GDVWFKFDDDEVSAVATDEIL---RLSGG 456
Cdd:cd02673 184 YSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRPVSKNDVStnaRSSGY 240
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
5-73 1.18e-04

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: 40.25  E-value: 1.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24583343   5 KVKVKWGRELYTdiVVNTDEEPIL-FKAQLFALTGVQPDRQKVM---CKGGILKDDQW--NLQIKDGAVVLLLGS 73
Cdd:cd01813   2 TLIVKWSGKEYP--VTVLSSDTVLdLKQRIFELTGVLPKRQKLLglkVKGKPADDDVKlsSLKLKPNTKIMMMGT 74
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
405-467 1.85e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 44.10  E-value: 1.85e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583343 405 YTLQAVLTHKGrSSSSGHYVAWVRSSGDV-WFKFDDDEVSAVATDEILRLSgggdwhcAYVLLY 467
Cdd:COG5560 764 YDLYAVDNHYG-GLSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSS-------AYVLFY 819
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
29-74 2.13e-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: 39.46  E-value: 2.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 24583343    29 FKAQLFALTGVQPDRQKVMCKGGILKDDQwNLQ---IKDGAVVLLLGSK 74
Cdd:pfam00240  24 LKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGeygIEDGSTIHLVLRQ 71
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
405-467 8.02e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 41.00  E-value: 8.02e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24583343 405 YTLQAVLTHKGRsSSSGHYVAWV-RSSGDVWFKFDDDEVSAVATDEILRLS-GGGDWHCAYVLLY 467
Cdd:cd02665 164 YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfGGGRNPSAYCLMY 227
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
405-467 2.11e-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: 39.66  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 405 YTLQAVLTHKGrSSSSGHYVAWVRSS---------------------GDVWFKFDDDEVSAVATDEILrLSGGgdwhcAY 463
Cdd:cd02662 163 YRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVL-EQKS-----AY 235

                ....
gi 24583343 464 VLLY 467
Cdd:cd02662 236 MLFY 239
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-184 2.66e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.46  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583343 105 GLTNLGNTCYMNATVQCL----NAVPELRTALSTFSNDGTDTMSTAFSISSAMKSIFAQMEKGTTVTPIVLLQALHRASP 180
Cdd:cd02665   1 GLKNVGNTCWFSAVIQSLfsqqQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCE 80

                ....
gi 24583343 181 QFAQ 184
Cdd:cd02665  81 TFGQ 84
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-137 2.72e-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: 2.72e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 24583343 105 GLTNLGNTCYMNATVQCLNAVPELRTALSTFSN 137
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE 33
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
393-439 2.82e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 39.43  E-value: 2.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24583343 393 FDDDLGSNNSGYYT--LQAVLTHKGRSSSSGHYVAWVRSSGDV------------WFKFDD 439
Cdd:cd02670 153 YDDKDFSPTCGKFKlsLCSAVCHRGTSLETGHYVAFVRYGSYSltetdneaynaqWVFFDD 213
 
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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