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Conserved domains on  [gi|42565077|ref|NP_566680|]
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ubiquitin carboxyl-terminal hydrolase [Arabidopsis thaliana]

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 ...
160-526 8.00e-150

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: 431.37  E-value: 8.00e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTkDVDQTSHMLTVATRELFSELDKSVKAVAPMPFWMVLQKKYPQF 239
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR-GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 AQLHN-GNHMQQDAEECWTQMLYTLSQslKLPSPSEDPDAVKALFGLNLLNRLHCQ-ESSEESSETESVFSLKCHISH-- 315
Cdd:cd02657  80 AEKQNqGGYAQQDAEECWSQLLSVLSQ--KLPGAGSKGSFIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQCHISItt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 316 EVNHLHEGLKHGLKGELEKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRESNQKAKILRKVDYPLELDIYDLCSe 395
Cdd:cd02657 158 EVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLYELCT- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 396 dlrkkleaprqklrdiegqklglqasakssskgddvkmtdaegssnqsgesstgdqqegasphMTGIYDLVSVLTHKGRS 475
Cdd:cd02657 237 ---------------------------------------------------------------PSGYYELVAVITHQGRS 253
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 42565077 476 ADSGHYVAWVKQES-GKWVQYDDANTSLQRGEDIIKLSGGGDWHMAYIVMYK 526
Cdd:cd02657 254 ADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
56-130 5.28e-43

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: 147.38  E-value: 5.28e-43
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565077  56 MLTVSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGTAD 130
Cdd:cd16104   1 TYKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSKLKLKDGQTLMLMGSAE 75
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 8.00e-150

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: 431.37  E-value: 8.00e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTkDVDQTSHMLTVATRELFSELDKSVKAVAPMPFWMVLQKKYPQF 239
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR-GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 AQLHN-GNHMQQDAEECWTQMLYTLSQslKLPSPSEDPDAVKALFGLNLLNRLHCQ-ESSEESSETESVFSLKCHISH-- 315
Cdd:cd02657  80 AEKQNqGGYAQQDAEECWSQLLSVLSQ--KLPGAGSKGSFIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQCHISItt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 316 EVNHLHEGLKHGLKGELEKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRESNQKAKILRKVDYPLELDIYDLCSe 395
Cdd:cd02657 158 EVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLYELCT- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 396 dlrkkleaprqklrdiegqklglqasakssskgddvkmtdaegssnqsgesstgdqqegasphMTGIYDLVSVLTHKGRS 475
Cdd:cd02657 237 ---------------------------------------------------------------PSGYYELVAVITHQGRS 253
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 42565077 476 ADSGHYVAWVKQES-GKWVQYDDANTSLQRGEDIIKLSGGGDWHMAYIVMYK 526
Cdd:cd02657 254 ADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
159-525 1.74e-60

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 201.90  E-value: 1.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   159 AGLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTKDVDQTSHMLTVATRELFSELDKSVK--AVAPMPFWMVLQKKY 236
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKssSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   237 PQFAqlhngNHMQQDAEECWTQMLYTLSQSLKLPSPSEDPDAVKALFGLNLLNRLHCQESSEESSETESVFSL------- 309
Cdd:pfam00443  81 PDFS-----GYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgd 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   310 ---KCHISHEVNHLHEGLKHGLKGELEKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRESnqKAKILRKVDYPLE 386
Cdd:pfam00443 156 saeLKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   387 LDIYDLCSEDLRKKLEAPRQklrdiegqklglqasakssskgddvkmtdaegssnqsgesstgdqqegasphmtgiYDLV 466
Cdd:pfam00443 234 LDLSRYLAEELKPKTNNLQD--------------------------------------------------------YRLV 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   467 SVLTHKGrSADSGHYVAWVKQ-ESGKWVQYDDANTSLQRGEDIIKLSGggdwhmAYIVMY 525
Cdd:pfam00443 258 AVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETAVLSSS------AYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
56-130 5.28e-43

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: 147.38  E-value: 5.28e-43
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565077  56 MLTVSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGTAD 130
Cdd:cd16104   1 TYKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSKLKLKDGQTLMLMGSAE 75
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
57-128 4.38e-13

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: 64.20  E-value: 4.38e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42565077     57 LTVSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGT 128
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
160-526 1.26e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 62.51  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLI----SVPELKSELS-NYQSarTKDVDQTSHmlTVATRElfsELDKSVKAVAPmpfwmvlqK 234
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlylpKLDELLDDLSkELKV--LKNVIRKPE--PDLNQE---EALKLFTALWS--------S 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 235 KYPQFAQLHNGNHmQQDAEECWTQML--------YTLSQSLKLPSPSEdpdavkalfglnllnrlhcqesseessetesv 306
Cdd:COG5533  66 KEHKVGWIPPMGS-QEDAHELLGKLLdelkldlvNSFTIRIFKTTKDK-------------------------------- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 307 fslKCHISHEVNHLHEGLKHGLKGELEKT-------SPSLGRTAVYVKES---------------LIDSLPRYLTVQFVR 364
Cdd:COG5533 113 ---KKTSTGDWFDIIIELPDQTWVNNLKTlqefidnMEELVDDETGVKAKeneelevqakqeyevSFVKLPKILTIQLKR 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 365 FfwkRESNQKAKILRKVDYPLELdiydlcsedlrkkleaprqklrdiegqklglqaSAKSSSKGDDVkmtdaegssnqsg 444
Cdd:COG5533 190 F---ANLGGNQKIDTEVDEKFEL---------------------------------PVKHDQILNIV------------- 220
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 445 esstgdqqegasphMTGIYDLVSVLTHKGrSADSGHYVAWVKQeSGKWVQYDDANTSLQRGEDIIKLsgggDWHMAYIVM 524
Cdd:COG5533 221 --------------KETYYDLVGFVLHQG-SLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINE----KAKNAYLYF 280

                ..
gi 42565077 525 YK 526
Cdd:COG5533 281 YE 282
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
57-128 9.40e-06

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: 43.70  E-value: 9.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42565077    57 LTVSVkWQKKVFEsIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGT 128
Cdd:pfam00240   1 ITVKT-LDGKKIT-LEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLR 70
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 8.00e-150

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: 431.37  E-value: 8.00e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTkDVDQTSHMLTVATRELFSELDKSVKAVAPMPFWMVLQKKYPQF 239
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR-GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 AQLHN-GNHMQQDAEECWTQMLYTLSQslKLPSPSEDPDAVKALFGLNLLNRLHCQ-ESSEESSETESVFSLKCHISH-- 315
Cdd:cd02657  80 AEKQNqGGYAQQDAEECWSQLLSVLSQ--KLPGAGSKGSFIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQCHISItt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 316 EVNHLHEGLKHGLKGELEKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRESNQKAKILRKVDYPLELDIYDLCSe 395
Cdd:cd02657 158 EVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLYELCT- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 396 dlrkkleaprqklrdiegqklglqasakssskgddvkmtdaegssnqsgesstgdqqegasphMTGIYDLVSVLTHKGRS 475
Cdd:cd02657 237 ---------------------------------------------------------------PSGYYELVAVITHQGRS 253
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 42565077 476 ADSGHYVAWVKQES-GKWVQYDDANTSLQRGEDIIKLSGGGDWHMAYIVMYK 526
Cdd:cd02657 254 ADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
159-525 1.74e-60

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 201.90  E-value: 1.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   159 AGLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTKDVDQTSHMLTVATRELFSELDKSVK--AVAPMPFWMVLQKKY 236
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKssSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   237 PQFAqlhngNHMQQDAEECWTQMLYTLSQSLKLPSPSEDPDAVKALFGLNLLNRLHCQESSEESSETESVFSL------- 309
Cdd:pfam00443  81 PDFS-----GYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgd 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   310 ---KCHISHEVNHLHEGLKHGLKGELEKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRESnqKAKILRKVDYPLE 386
Cdd:pfam00443 156 saeLKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   387 LDIYDLCSEDLRKKLEAPRQklrdiegqklglqasakssskgddvkmtdaegssnqsgesstgdqqegasphmtgiYDLV 466
Cdd:pfam00443 234 LDLSRYLAEELKPKTNNLQD--------------------------------------------------------YRLV 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077   467 SVLTHKGrSADSGHYVAWVKQ-ESGKWVQYDDANTSLQRGEDIIKLSGggdwhmAYIVMY 525
Cdd:pfam00443 258 AVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETAVLSSS------AYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
160-526 1.36e-43

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: 155.33  E-value: 1.36e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLIsvpelkselsnyqsartkdvdqtshmltvatrelfseldksvkavapmpfwmvlqkkypqf 239
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 aqlhngnHMQQDAEECWTQMLYTLSQSLKLPSPSEDPDA-----VKALFGLNLLNRLHCQESSEESSETESVFSLKCHI- 313
Cdd:cd02257  20 -------SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSslkslIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLp 92
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 314 --SHEVNHLHEGLKHGLKGEL----EKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKrESNQKAKILRKVDYPLEL 387
Cdd:cd02257  93 vkGLPQVSLEDCLEKFFKEEIlegdNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLEL 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 388 DIYDLCSEdlrkkleaprqklrdiegqklglqasakssskgddvkmtdaegssnqsgesstgDQQEGASPHMTGIYDLVS 467
Cdd:cd02257 172 DLSPYLSE------------------------------------------------------GEKDSDSDNGSYKYELVA 197
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 468 VLTHKGRSADSGHYVAWVK-QESGKWVQYDDANTSLQRGEDIIKLsgGGDWHMAYIVMYK 526
Cdd:cd02257 198 VVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLEF--GSLSSSAYILFYE 255
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
56-130 5.28e-43

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: 147.38  E-value: 5.28e-43
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565077  56 MLTVSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGTAD 130
Cdd:cd16104   1 TYKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSKLKLKDGQTLMLMGSAE 75
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
156-526 2.15e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 106.96  E-value: 2.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 156 GYSaGLVNLGNTCYMNSTMQCLISVPELKSELsnYQSARTKDVDQTSHMLTVATReLFSELDKSVKAV-APMPFWmvLQK 234
Cdd:cd02659   1 GYV-GLKNQGATCYMNSLLQQLYMTPEFRNAV--YSIPPTEDDDDNKSVPLALQR-LFLFLQLSESPVkTTELTD--KTR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 235 KYpqfaqlhNGN----HMQQDAEECWTQMLYTLSQSLKlpsPSEDPDAVKALFGLNLLNRLHCQESSEESSETESVFSLK 310
Cdd:cd02659  75 SF-------GWDslntFEQHDVQEFFRVLFDKLEEKLK---GTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 311 CHISHEVNhLHEGLKHGLKGEL---------EKTspSLGRTAvyVKESLIDSLPRYLTVQFVRFFWKRESNQKAKILRKV 381
Cdd:cd02659 145 VAVKGKKN-LEESLDAYVQGETlegdnkyfcEKC--GKKVDA--EKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRF 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 382 DYPLELDIYDLCSEDLRKKLEAPRQKlrdiegqklglqasakssskgddvkmtdaegssnQSGESstgdqqegasphmtg 461
Cdd:cd02659 220 EFPLELDMEPYTEKGLAKKEGDSEKK----------------------------------DSESY--------------- 250
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 462 IYDLVSVLTHKGrSADSGHYVAWVKQ-ESGKWVQYDDANTSLQRGEDIIKLSGGGD---------------WHMAYIVMY 525
Cdd:cd02659 251 IYELHGVLVHSG-DAHGGHYYSYIKDrDDGKWYKFNDDVVTPFDPNDAEEECFGGEetqktydsgprafkrTTNAYMLFY 329

                .
gi 42565077 526 K 526
Cdd:cd02659 330 E 330
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
159-525 2.41e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 88.49  E-value: 2.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 159 AGLVNLGNTCYMNSTMQCLISVPelksELSNYqsARTKDVDQTSH---------MLTVATRELFSeldkSVKAVAPMPFW 229
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTP----PLANY--LLSREHSKDCCnegfcmmcaLEAHVERALAS----SGPGSAPRIFS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 230 MVLQKKYPQFaqlhnGNHMQQDAEE--------CWTQMLYTLSQSLKLPSPSEDPDAVKALFGLNLLNRLHCqesseess 301
Cdd:cd02661  72 SNLKQISKHF-----RIGRQEDAHEflrylldaMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKC-------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 302 etesvfsLKC-HIS-------------HEVNHLHEGLKH-----GLKGEL--------EKTSPSlgrtavyvKESLIDSL 354
Cdd:cd02661 139 -------LNCkHVSntydpfldlsldiKGADSLEDALEQftkpeQLDGENkykcerckKKVKAS--------KQLTIHRA 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 355 PRYLTVQFVRFfwkrESNQKAKILRKVDYPLELDIYDLCSedlrkkleaprqklrdiegqklglqasakssskgddvkmt 434
Cdd:cd02661 204 PNVLTIHLKRF----SNFRGGKINKQISFPETLDLSPYMS---------------------------------------- 239
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 435 daegssnQSGESSTgdqqegasphmtgIYDLVSVLTHKGRSADSGHYVAWVKQESGKWVQYDDANTSLQRGEDIikLSGG 514
Cdd:cd02661 240 -------QPNDGPL-------------KYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETV--LSQK 297
                       410
                ....*....|.
gi 42565077 515 gdwhmAYIVMY 525
Cdd:cd02661 298 -----AYILFY 303
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 7.67e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 87.38  E-value: 7.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTKDV-----DQTSHMLTVAT----------RELFSELDKSVKAVA 224
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVvdpanDLNCQLIKLADgllsgryskpASLKSENDPYQVGIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 225 PMPFWMVLQKKYPQFAQLHngnhmQQDAEECWTQMLYTLSQSLKlPSPSEDPDavkALFGLNLLNRLHCQESSEESSETE 304
Cdd:cd02658  81 PSMFKALIGKGHPEFSTMR-----QQDALEFLLHLIDKLDRESF-KNLGLNPN---DLFKFMIEDRLECLSCKKVKYTSE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 305 SVFSLKCHISHEVN-------------HLHEGLKHGLKGE-LEKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRE 370
Cdd:cd02658 152 LSEILSLPVPKDEAtekeegelvyepvPLEDCLKAYFAPEtIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 371 SNQKakilrKVDYPLELDiydlcsEDLRkkleaprqklrdiegqklglqaSAKssskgddvkmtdaegssnqsgesstgd 450
Cdd:cd02658 232 WVPK-----KLDVPIDVP------EELG----------------------PGK--------------------------- 251
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42565077 451 qqegasphmtgiYDLVSVLTHKGRSADSGHYVAWVKQE---SGKWVQYDDANTSLQRGEDIIKlsgggdwHMAYIVMYK 526
Cdd:cd02658 252 ------------YELIAFISHKGTSVHSGHYVAHIKKEidgEGKWVLFNDEKVVASQDPPEMK-------KLGYIYFYQ 311
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 6.70e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 81.70  E-value: 6.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLI-------SVPELKSELSNYQSARTKDVDQTSHMLTVATRELFSELDKS-VKAVAPMPFWMV 231
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFmnlefrkAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGnRSVVDPSGFVKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 232 LQkkypqfaqLHNGNhmQQDAEEcWTQMLYTLSQSlKLpSPSEDPDA---VKALFGLNLLNRLHCQESSEESSETESVFS 308
Cdd:cd02668  81 LG--------LDTGQ--QQDAQE-FSKLFLSLLEA-KL-SKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 309 LKCHIShevnhLHEGLKHGLKGEL--EKTS-------PSLGRTAVYVKESLIDSLPRYLTVQFVRFFWKRESNQKAKILR 379
Cdd:cd02668 148 LELQLK-----GHKTLEECIDEFLkeEQLTgdnqyfcESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNA 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 380 KVDYPLELDIYDLCSEdlrkkleaprqklrdiegqklglqasakssskgddvkmtdaegSSNQSGEsstgdqqegasphm 459
Cdd:cd02668 223 SISFPEILDMGEYLAE-------------------------------------------SDEGSYV-------------- 245
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 460 tgiYDLVSVLTHKGRSADSGHYVAWVKQES-GKWVQYDD-------------ANTSLQRGEDIIKLSGGgdWHM---AYI 522
Cdd:cd02668 246 ---YELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDedveempgkplklGNSEDPAKPRKSEIKKG--THSsrtAYM 320

                ....
gi 42565077 523 VMYK 526
Cdd:cd02668 321 LVYK 324
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-498 1.61e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 80.88  E-value: 1.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTKDVDQTSHMLTVATRELFSELDKSVKAVAPMP------FWmvlq 233
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPinllylSW---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 234 kkypqFAQLHNGNHMQQDAEECWTQMLYTLSQSLKLPS-PSEDPDA----VKALFGLNLLNRLHCQesseessetesvfs 308
Cdd:cd02660  78 -----KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKnEANDESHcnciIHQTFSGSLQSSVTCQ-------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 309 lKCH-----------ISHEVNHL-----HEGLKHG-----LKGELEK-TSP-----------SLGRTAVYVKESLIDSLP 355
Cdd:cd02660 139 -RCGgvsttvdpfldLSLDIPNKstpswALGESGVsgtptLSDCLDRfTRPeklgdfaykcsGCGSTQEATKQLSIKKLP 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 356 RYLTVQFVRFfwKRESN-QKAKILRKVDYPLELDIYDLCSedlrkkleaprqklrdiegqklglqasakssskgddvkmt 434
Cdd:cd02660 218 PVLCFQLKRF--EHSLNkTSRKIDTYVQFPLELNMTPYTS---------------------------------------- 255
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42565077 435 daegssnqsgeSSTGDQQEGASPHMTGIYDLVSVLTHKGrSADSGHYVAWVKQESGKWVQYDDA 498
Cdd:cd02660 256 -----------SSIGDTQDSNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDA 307
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
57-128 4.38e-13

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: 64.20  E-value: 4.38e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42565077     57 LTVSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGT 128
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 6.08e-13

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 69.83  E-value: 6.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQSARTKDvdqtSHMLTVATRELFSELDKSVKAVAPMPFWMVLQKKYPQF 239
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGD----SQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRPPWF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 AqlhngNHMQQDAEEcWTQMLYTLSQSLklpspsedpdaVKALFGLNLLNRLHCqesseessetesvfsLKCHISHEvnh 319
Cdd:cd02664  77 T-----PGSQQDCSE-YLRYLLDRLHTL-----------IEKMFGGKLSTTIRC---------------LNCNSTSA--- 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 320 lheglKHGLKGELEKTSPSLGRTAVY------------------------VKESLIDSLPRYLTVQFVRFFWKRESNQKA 375
Cdd:cd02664 122 -----RTERFRDLDLSFPSVQDLLNYflspekltgdnqyycekcaslqdaEKEMKVTGAPEYLILTLLRFSYDQKTHVRE 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 376 KILRKVDYPLELDiydlcsedlrkkleaprqklrdiegqklglqasakssskgddVKMTDAEGSSNQSGESSTGDQQE-G 454
Cdd:cd02664 197 KIMDNVSINEVLS------------------------------------------LPVRVESKSSESPLEKKEEESGDdG 234
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 455 ASPHMTGIYDLVSVLTHKGRSADSGHY---------------------VAWVKQESGKWVQYDDANTSLQRGEDIIKLSG 513
Cdd:cd02664 235 ELVTRQVHYRLYAVVVHSGYSSESGHYftyardqtdadstgqecpepkDAEENDESKNWYLFNDSRVTFSSFESVQNVTS 314
                       410
                ....*....|...
gi 42565077 514 GGDWHMAYIVMYK 526
Cdd:cd02664 315 RFPKDTPYILFYE 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 2.47e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 66.54  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLIsvpelkselsnyqsartkdvdqtshmltvatrelfseldksvkavapmpfwmvlqkkypqf 239
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLS------------------------------------------------------------- 19
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 aqlhngnHMQQDAEECWTQMLYTLsQSLklpspsedpdaVKALF-GLnLLNRLHCqesseessetesvfsLKCHIS---- 314
Cdd:cd02674  20 -------ADQQDAQEFLLFLLDGL-HSI-----------IVDLFqGQ-LKSRLTC---------------LTCGKTsttf 64
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 315 -----------------HEVNhLHEGLKHGLKGEL-----EKTSPSLGRTAVYVKESLIDSLPRYLTVQFVRFfwKRESN 372
Cdd:cd02674  65 epftylslpipsgsgdaPKVT-LEDCLRLFTKEETldgdnAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF--SFSRG 141
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 373 QKAKILRKVDYPLEldiydlcsedlrkkleaprqklrdiegqKLGLQASAKSSSKGDDVKmtdaegssnqsgesstgdqq 452
Cdd:cd02674 142 STRKLTTPVTFPLN----------------------------DLDLTPYVDTRSFTGPFK-------------------- 173
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565077 453 egasphmtgiYDLVSVLTHKGrSADSGHYVAWVK-QESGKWVQYDDANTSLQRGEDIIKLSgggdwhmAYIVMYK 526
Cdd:cd02674 174 ----------YDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSS-------AYILFYE 230
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-486 3.26e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 67.03  E-value: 3.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSelsnyqsartkdvdqtshMLTVATRELFSEldksvkavapmpfwmvLQKKYPQF 239
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRE------------------LLSETPKELFSQ----------------VCRKAPQF 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 240 aqlhNGNHmQQDAEEcwtqMLYTLSQSLKLpspsedpdAVKALFGLNLLNRLHCQesseessetesvfslKChisHEVNH 319
Cdd:cd02667  47 ----KGYQ-QQDSHE----LLRYLLDGLRT--------FIDSIFGGELTSTIMCE---------------SC---GTVSL 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 320 LHE-----------------GLKHGLKG-----ELEKTSPSLGRTAVY-VKESLIDSLPRYLTVQFVRFFWKRESNQKaK 376
Cdd:cd02667  92 VYEpfldlslprsdeiksecSIESCLKQfteveILEGNNKFACENCTKaKKQYLISKLPPVLVIHLKRFQQPRSANLR-K 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 377 ILRKVDYPLELDIYDLCsedlrkkleaprqklrdiegqklglqasakssskgdDVKMTDAEGSSNQSgesstgdqqegas 456
Cdd:cd02667 171 VSRHVSFPEILDLAPFC------------------------------------DPKCNSSEDKSSVL------------- 201
                       330       340       350
                ....*....|....*....|....*....|
gi 42565077 457 phmtgiYDLVSVLTHKGrSADSGHYVAWVK 486
Cdd:cd02667 202 ------YRLYGVVEHSG-TMRSGHYVAYVK 224
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
57-128 1.11e-11

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: 60.28  E-value: 1.11e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565077  57 LTVSVKWQKKVFeSIEIDTSQPPFVFKAQLYDLSGVPPERQKIM---VKGGLLKDDADWSTLGLKNGQKLMMMGT 128
Cdd:cd01813   1 ITLIVKWSGKEY-PVTVLSSDTVLDLKQRIFELTGVLPKRQKLLglkVKGKPADDDVKLSSLKLKPNTKIMMMGT 74
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-526 1.28e-11

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: 65.41  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLisvpelkselsnYQSArtkdvdqtshMLTvATRELF---SELDKSVKAVAPMPFWMVLQKKY 236
Cdd:cd02663   1 GLENFGNTCYCNSVLQAL------------YFEN----------LLT-CLKDLFesiSEQKKRTGVISPKKFITRLKREN 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 237 PQFaqlhnGNHMQQDAEECWTQMLYTLSQSLK--------------LPSPSEDPDAVKALFGLNLLNRLHCqesseesse 302
Cdd:cd02663  58 ELF-----DNYMHQDAHEFLNFLLNEIAEILDaerkaekanrklnnNNNAEPQPTWVHEIFQGILTNETRC--------- 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 303 tesvfsLKCHI--SHEVNHL--------HEGLKHGLKGeLEKTSPSLGRTAVYV----------KESLIDSLPRYLTVQF 362
Cdd:cd02663 124 ------LTCETvsSRDETFLdlsidveqNTSITSCLRQ-FSATETLCGRNKFYCdeccslqeaeKRMKIKKLPKILALHL 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 363 VRFFWKRESNQKAKILRKVDYPLELDIYdlcsedlrkkleaprqklrdiegqklglqasakssskgddvkmtdaegssNQ 442
Cdd:cd02663 197 KRFKYDEQLNRYIKLFYRVVFPLELRLF--------------------------------------------------NT 226
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 443 SGESSTGDQqegasphmtgIYDLVSVLTHKGRSADSGHYVAWVKQeSGKWVQYDDANTSLQRGEDIIKLSGGG-DWHMAY 521
Cdd:cd02663 227 TDDAENPDR----------LYELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENAVEEFFGDSpNQATAY 295

                ....*
gi 42565077 522 IVMYK 526
Cdd:cd02663 296 VLFYQ 300
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
160-526 1.26e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 62.51  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 160 GLVNLGNTCYMNSTMQCLI----SVPELKSELS-NYQSarTKDVDQTSHmlTVATRElfsELDKSVKAVAPmpfwmvlqK 234
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlylpKLDELLDDLSkELKV--LKNVIRKPE--PDLNQE---EALKLFTALWS--------S 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 235 KYPQFAQLHNGNHmQQDAEECWTQML--------YTLSQSLKLPSPSEdpdavkalfglnllnrlhcqesseessetesv 306
Cdd:COG5533  66 KEHKVGWIPPMGS-QEDAHELLGKLLdelkldlvNSFTIRIFKTTKDK-------------------------------- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 307 fslKCHISHEVNHLHEGLKHGLKGELEKT-------SPSLGRTAVYVKES---------------LIDSLPRYLTVQFVR 364
Cdd:COG5533 113 ---KKTSTGDWFDIIIELPDQTWVNNLKTlqefidnMEELVDDETGVKAKeneelevqakqeyevSFVKLPKILTIQLKR 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 365 FfwkRESNQKAKILRKVDYPLELdiydlcsedlrkkleaprqklrdiegqklglqaSAKSSSKGDDVkmtdaegssnqsg 444
Cdd:COG5533 190 F---ANLGGNQKIDTEVDEKFEL---------------------------------PVKHDQILNIV------------- 220
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 445 esstgdqqegasphMTGIYDLVSVLTHKGrSADSGHYVAWVKQeSGKWVQYDDANTSLQRGEDIIKLsgggDWHMAYIVM 524
Cdd:COG5533 221 --------------KETYYDLVGFVLHQG-SLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINE----KAKNAYLYF 280

                ..
gi 42565077 525 YK 526
Cdd:COG5533 281 YE 282
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
130-267 1.70e-10

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 63.75  E-value: 1.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 130 DEIVKAPEkGPVFMEDLPEEQQAANLGYSAGLVNLGNTCYMNSTMQCLISVPelksELSNYQSART--KDVDQTSH---M 204
Cdd:COG5560 238 SKITRNPD-WLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTW----ELRDYFLSDEyeESINEENPlgmH 312
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42565077 205 LTVATreLFSELDKSV-----KAVAPMPFWMVLQKKYPQFAqlhngNHMQQDAEECWTQMLYTLSQSL 267
Cdd:COG5560 313 GSVAS--AYADLIKQLydgnlHAFTPSGFKKTIGSFNEEFS-----GYDQQDSQEFIAFLLDGLHEDL 373
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
59-126 4.80e-10

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: 55.68  E-value: 4.80e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42565077  59 VSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMM 126
Cdd:cd17039   1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
83-128 1.19e-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: 51.86  E-value: 1.19e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 42565077  83 KAQLYDLSGVPPERQKIMVKgGLLKDDADWSTLGLKNGQKLMMMGT 128
Cdd:cd17047  26 KEHIETLTGVPPAMQKLMYK-GLLKDDKTLRELKVTKGAKVMVVGS 70
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
159-508 2.23e-08

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: 55.96  E-value: 2.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 159 AGLVNLGNTCYMNSTMQCLISVPELKSELSNYQ---SARTKDVDQT---------------SHMLTVATRELFSELDKS- 219
Cdd:cd02666   2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDeskAELASDYPTErriggrevsrselqrSNQFVYELRSLFNDLIHSn 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 220 VKAVAPMpfwmvlqkkypqfAQLHNGNHMQQDAEECWTQMLYTLSQSLKLPSPSE-DPDAVKALFGLNLLNRLHCQESSE 298
Cdd:cd02666  82 TRSVTPS-------------KELAYLALRQQDVTECIDNVLFQLEVALEPISNAFaGPDTEDDKEQSDLIKRLFSGKTKQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 299 ESSETESVFSLKCHISHE------VNHLHEGLKHGLKGELEKTSPSLGRtavYVKESLIDSLPRYLTVQFvrffwKRESN 372
Cdd:cd02666 149 QLVPESMGNQPSVRTKTErflsllVDVGKKGREIVVLLEPKDLYDALDR---YFDYDSLTKLPQRSQVQA-----QLAQP 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 373 QKAKILRKVDYPLELDIyDLCSEDLRKKLEAPRQKLRDIEGQKLGLQasAKSSSKGDDVKMTDaegssnqsgesstgdqq 452
Cdd:cd02666 221 LQRELISMDRYELPSSI-DDIDELIREAIQSESSLVRQAQNELAELK--HEIEKQFDDLKSYG----------------- 280
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42565077 453 egasphmtgiYDLVSVLTHKGrSADSGHYVAWVKQ-ESGKWVQYDDANTSLQRGEDI 508
Cdd:cd02666 281 ----------YRLHAVFIHRG-EASSGHYWVYIKDfEENVWRKYNDETVTVVPASEV 326
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
88-127 8.48e-07

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: 46.50  E-value: 8.48e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 42565077  88 DLSGVPPERQKIMVKGGLLKD-DADWSTLGLKNGQKLMMMG 127
Cdd:cd01812  35 EVTGVPVENQKLIFKGKSLKDpEQPLSALGVKNGSKIMLIG 75
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
57-128 9.40e-06

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: 43.70  E-value: 9.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42565077    57 LTVSVkWQKKVFEsIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMMGT 128
Cdd:pfam00240   1 ITVKT-LDGKKIT-LEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLR 70
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
160-192 1.80e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 46.21  E-value: 1.80e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 42565077 160 GLVNLGNTCYMNSTMQCLISVPELKSELSNYQS 192
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE 33
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
156-497 5.78e-05

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 46.02  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077  156 GYsAGLVNLGNTCYMNSTMQCLISVPELKSELSNYQSartkDVDQTSHMLTVATRELFSELDKSVKAVAPMPFWMvlqkk 235
Cdd:COG5077  192 GY-VGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPT----DHPRGRDSVALALQRLFYNLQTGEEPVDTTELTR----- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077  236 ypQFAQLHNGNHMQQDAEECWTQMLYTLSQSLKlPSPSEDpdAVKALFGLNLLNRLHCQESSEESSETESVFSLKCHISH 315
Cdd:COG5077  262 --SFGWDSDDSFMQHDIQEFNRVLQDNLEKSMR-GTVVEN--ALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077  316 EVNhLHEGLKHGLKGEL---EKTSPSLGRTAVYVKESLI-DSLPRYLTVQFVRFFWKRESNQKAKILRKVDYPLELDIYD 391
Cdd:COG5077  337 MKN-LQESFRRYIQVETldgDNRYNAEKHGLQDAKKGVIfESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLP 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077  392 LCSEDLRKKLEaprqklrdiegqklglqasakssskgddvkmTDAEgssnqsgesstgdqqegasphmtgiYDLVSVLTH 471
Cdd:COG5077  416 FLDRDADKSEN-------------------------------SDAV-------------------------YVLYGVLVH 439
                        330       340
                 ....*....|....*....|....*..
gi 42565077  472 KGrSADSGHYVAWVKQE-SGKWVQYDD 497
Cdd:COG5077  440 SG-DLHEGHYYALLKPEkDGRWYKFDD 465
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
57-126 1.60e-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: 40.02  E-value: 1.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565077  57 LTVSVKWQKKVFESIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLL-KDDADWSTLGLKNGQKLMMM 126
Cdd:cd17053   1 LTVNSKLLTGTVHTLQVSRSTTVAQVKAMIEDQSGVPPNEQILVYNGKRLeDGDKTLGEYGIKTGDTLYLL 71
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
161-189 1.73e-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: 43.29  E-value: 1.73e-04
                        10        20
                ....*....|....*....|....*....
gi 42565077 161 LVNLGNTCYMNSTMQCLISVPELKSELSN 189
Cdd:cd02673   2 LVNTGNSCYFNSTMQALSSIGKINTEFDN 30
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
345-526 2.19e-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: 42.90  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 345 YVKESLIDSLPRYLTVQFVRFFWKRESNQKakILRKVDYPLELDIYDLcsedlrkkleaprqklrdIEGQKLGLQASAKS 424
Cdd:cd02670  89 YFNNSVFAKAPSCLIICLKRYGKTEGKAQK--MFKKILIPDEIDIPDF------------------VADDPRACSKCQLE 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 425 SSKGDDVKMTDAEGssnqsgesstGDQQegasphmtgiYDLVSVLTHKGRSADSGHYVAWVKQESG------------KW 492
Cdd:cd02670 149 CRVCYDDKDFSPTC----------GKFK----------LSLCSAVCHRGTSLETGHYVAFVRYGSYsltetdneaynaQW 208
                       170       180       190
                ....*....|....*....|....*....|....
gi 42565077 493 VQYDDANTSlQRGEDIIKLSGGGDWHMAYIVMYK 526
Cdd:cd02670 209 VFFDDMADR-DGVSNGFNIPAARLLEDPYMLFYQ 241
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
130-254 5.70e-04

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 42.19  E-value: 5.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565077 130 DEIVKAPEKGPvfmedLPEEQQAANLGYSAGLVNLGNTCYMNSTMQCLISVPELKSELSN-YQSARTKDVDQTSHMLtva 208
Cdd:cd02671   1 DQVVPAPQPSS-----ATSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHlVSLISSVEQLQSSFLL--- 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42565077 209 TRELFSELdksVKAVAPMPFWMVLQKKYPQFaqlhNGNhMQQDAEE 254
Cdd:cd02671  73 NPEKYNDE---LANQAPRRLLNALREVNPMY----EGY-LQHDAQE 110
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
70-121 1.02e-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: 38.00  E-value: 1.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 42565077  70 SIEIDTSQPPFVFKAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQ 121
Cdd:cd16106  14 TVEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSYKIQDGH 65
Ubl_NUB1 cd17062
ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, ...
83-126 5.49e-03

ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also termed negative regulator of ubiquitin-like proteins 1, or renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1), which may function in the regulation of cell cycle progression. NUB1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif.


Pssm-ID: 340582  Cd Length: 78  Bit Score: 35.96  E-value: 5.49e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 42565077  83 KAQLYDLSGVPPERQKIMVKGGLLKDDADWSTLGLKNGQKLMMM 126
Cdd:cd17062  33 REKIAEELGVPEDRIKLISNGKVLKDEKTLAEQGVKNNSQVMVL 76
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
463-499 6.73e-03

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 38.28  E-value: 6.73e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 42565077 463 YDLVSVLTHKGRSADSGHYVAWVKQESG--KWVQYDDAN 499
Cdd:cd02673 184 YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDE 222
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
463-525 7.55e-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: 38.31  E-value: 7.55e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565077 463 YDLVSVLTHKGRsADSGHYVAWV-KQESGKWVQYDDANTSLQRGEDIIKLS-GGGDWHMAYIVMY 525
Cdd:cd02665 164 YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfGGGRNPSAYCLMY 227
 
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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