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Conserved domains on  [gi|1972232041|ref|NP_001380262|]
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Ubiquitin carboxyl-terminal hydrolase usp-48 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
108-393 1.02e-53

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 190.35  E-value: 1.02e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  108 AGLINGGNFCYVNSFLQVWFNVPEFRQLIYDfRPSENFVPPEAPRMNVqatMLALQDIFYTLQTTPFNETDKTSNLGKLL 187
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR-ISPLSEDSRYNKDINL---LCALRDLFKALQKNSKSSSVSPKMFKKSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  188 RLNSE------QQDSQEFGLKFFNALERCL-PDHPNGKETLkrLKDLFTGETCTRIVCK-CGQRSEREETAISLTLNIEG 259
Cdd:pfam00443   77 GKLNPdfsgykQQDAQEFLLFLLDGLHEDLnGNHSTENESL--ITDLFRGQLKSRLKCLsCGEVSETFEPFSDLSLPIPG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  260 YCTLL-------DALDAYFGEEHLDDFK--CSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREI 330
Cdd:pfam00443  155 DSAELktaslqiCFLQFSKLEELDDEEKyyCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEL 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972232041  331 PAKAFQ-RTNNSIPPPAEMYDLFAVTIHEGnNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKP 393
Cdd:pfam00443  235 DLSRYLaEELKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEE 297
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
1159-1262 1.25e-09

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd01795:

Pssm-ID: 475130 [Multi-domain]  Cd Length: 99  Bit Score: 56.52  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041 1159 RRGRAKNLyAIKMSSTNKLMELKVQLYDKTHQLPNDQLLYrTAGGEqfdVSNNQKTLFDLRLSPNNNdnpLILIAQQF-- 1236
Cdd:cd01795      1 RRVRGERK-SLTVSSTTTLKELKLQIMEKFSVAPFDQHLY-FNGRE---LTDDSATLADLGILPGDV---LYLKVDEPpd 72
                           90       100
                   ....*....|....*....|....*..
gi 1972232041 1237 -SPSASQADETGDRAPERGFVDTALAH 1262
Cdd:cd01795     73 dPDDADEADVSRARVPEEGFKGTALLG 99
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
108-393 1.02e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 190.35  E-value: 1.02e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  108 AGLINGGNFCYVNSFLQVWFNVPEFRQLIYDfRPSENFVPPEAPRMNVqatMLALQDIFYTLQTTPFNETDKTSNLGKLL 187
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR-ISPLSEDSRYNKDINL---LCALRDLFKALQKNSKSSSVSPKMFKKSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  188 RLNSE------QQDSQEFGLKFFNALERCL-PDHPNGKETLkrLKDLFTGETCTRIVCK-CGQRSEREETAISLTLNIEG 259
Cdd:pfam00443   77 GKLNPdfsgykQQDAQEFLLFLLDGLHEDLnGNHSTENESL--ITDLFRGQLKSRLKCLsCGEVSETFEPFSDLSLPIPG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  260 YCTLL-------DALDAYFGEEHLDDFK--CSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREI 330
Cdd:pfam00443  155 DSAELktaslqiCFLQFSKLEELDDEEKyyCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEL 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972232041  331 PAKAFQ-RTNNSIPPPAEMYDLFAVTIHEGnNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKP 393
Cdd:pfam00443  235 DLSRYLaEELKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEE 297
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-416 1.15e-51

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: 184.93  E-value: 1.15e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVPPEAPRMNV---QATMLALQDIFYTLQTTPFNETDkTSNLGK 185
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPhepQTIIDQLQLIFAQLQFGNRSVVD-PSGFVK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  186 LLRL-NSEQQDSQEFGLKFFNALERCLpDHPNGKETLKRLKDLFTGETCTRIVC-KCGQRSEREETAISLTLNIEGYCTL 263
Cdd:cd02668     80 ALGLdTGQQQDAQEFSKLFLSLLEAKL-SKSKNPDLKNIVQDLFRGEYSYVTQCsKCGRESSLPSKFYELELQLKGHKTL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  264 LDALDAYFGEEHLDD---FKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQ--KLKTPMAYPREI---PAKAF 335
Cdd:cd02668    159 EECIDEFLKEEQLTGdnqYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkkKLNASISFPEILdmgEYLAE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  336 QRTNNSIpppaemYDLFAVTIHEGNNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKPPGTEkpttAKTEKSRKKDKEKY 415
Cdd:cd02668    239 SDEGSYV------YELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKL----GNSEDPAKPRKSEI 308

                   .
gi 1972232041  416 P 416
Cdd:cd02668    309 K 309
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
109-485 1.64e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 127.68  E-value: 1.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDfrpsenfVPPEAPRMNvQATMLALQDIFYTLQTT--PFNETDKTSNLGKL 186
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYG-------IPTDHPRGR-DSVALALQRLFYNLQTGeePVDTTELTRSFGWD 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  187 LRLNSEQQDSQEFGLKFFNALERCLpdhpNGKETLKRLKDLFTGETCTRIVC-KCGQRSEREETAISLTLNIEGYCTLLD 265
Cdd:COG5077    267 SDDSFMQHDIQEFNRVLQDNLEKSM----RGTVVENALNGIFVGKMKSYIKCvNVNYESARVEDFWDIQLNVKGMKNLQE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  266 ALDAYFGEEHLDDFKCSKCNKTG--DVSKQSDYVKLPPVIVIQLNRYKYTSKGRQ--KLKTPMAYPREIPAKAF-QRTNN 340
Cdd:COG5077    343 SFRRYIQVETLDGDNRYNAEKHGlqDAKKGVIFESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLEIDLLPFlDRDAD 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  341 SIPPPAEMYDLFAVTIHEGNNAEcGHYYDLIKSPLNQKWYRYNDEAI------EAIPKPPGTEKPTtakTEKSRKKDKEK 414
Cdd:COG5077    423 KSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEKDGRWYKFDDTRVtratekEVLEENFGGDHPY---KDKIRDHSGIK 498
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972232041  415 YPTdqkACYGLLYRRRDafkplphpkLPPEELIIDSKTEIEELFEGLTKKKIEKSEKRLYDLERRINKVKI 485
Cdd:COG5077    499 RFM---SAYMLVYLRKS---------MLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGV 557
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
1159-1262 1.25e-09

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 56.52  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041 1159 RRGRAKNLyAIKMSSTNKLMELKVQLYDKTHQLPNDQLLYrTAGGEqfdVSNNQKTLFDLRLSPNNNdnpLILIAQQF-- 1236
Cdd:cd01795      1 RRVRGERK-SLTVSSTTTLKELKLQIMEKFSVAPFDQHLY-FNGRE---LTDDSATLADLGILPGDV---LYLKVDEPpd 72
                           90       100
                   ....*....|....*....|....*..
gi 1972232041 1237 -SPSASQADETGDRAPERGFVDTALAH 1262
Cdd:cd01795     73 dPDDADEADVSRARVPEEGFKGTALLG 99
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
108-393 1.02e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 190.35  E-value: 1.02e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  108 AGLINGGNFCYVNSFLQVWFNVPEFRQLIYDfRPSENFVPPEAPRMNVqatMLALQDIFYTLQTTPFNETDKTSNLGKLL 187
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR-ISPLSEDSRYNKDINL---LCALRDLFKALQKNSKSSSVSPKMFKKSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  188 RLNSE------QQDSQEFGLKFFNALERCL-PDHPNGKETLkrLKDLFTGETCTRIVCK-CGQRSEREETAISLTLNIEG 259
Cdd:pfam00443   77 GKLNPdfsgykQQDAQEFLLFLLDGLHEDLnGNHSTENESL--ITDLFRGQLKSRLKCLsCGEVSETFEPFSDLSLPIPG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  260 YCTLL-------DALDAYFGEEHLDDFK--CSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREI 330
Cdd:pfam00443  155 DSAELktaslqiCFLQFSKLEELDDEEKyyCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEL 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972232041  331 PAKAFQ-RTNNSIPPPAEMYDLFAVTIHEGnNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKP 393
Cdd:pfam00443  235 DLSRYLaEELKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEE 297
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-416 1.15e-51

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: 184.93  E-value: 1.15e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVPPEAPRMNV---QATMLALQDIFYTLQTTPFNETDkTSNLGK 185
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPhepQTIIDQLQLIFAQLQFGNRSVVD-PSGFVK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  186 LLRL-NSEQQDSQEFGLKFFNALERCLpDHPNGKETLKRLKDLFTGETCTRIVC-KCGQRSEREETAISLTLNIEGYCTL 263
Cdd:cd02668     80 ALGLdTGQQQDAQEFSKLFLSLLEAKL-SKSKNPDLKNIVQDLFRGEYSYVTQCsKCGRESSLPSKFYELELQLKGHKTL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  264 LDALDAYFGEEHLDD---FKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQ--KLKTPMAYPREI---PAKAF 335
Cdd:cd02668    159 EECIDEFLKEEQLTGdnqYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkkKLNASISFPEILdmgEYLAE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  336 QRTNNSIpppaemYDLFAVTIHEGNNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKPPGTEkpttAKTEKSRKKDKEKY 415
Cdd:cd02668    239 SDEGSYV------YELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKL----GNSEDPAKPRKSEI 308

                   .
gi 1972232041  416 P 416
Cdd:cd02668    309 K 309
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
109-392 6.42e-49

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: 174.59  E-value: 6.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFnvpefrqliydfrpsenfvppeaprmnvqatmlalqdifytlqttpfnetdktsnlgkllr 188
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  189 lnSEQQDSQEFGLKFFNALERCLPDHPNGKETLKRLK----DLFTGETCTRIVCK-CGQRSEREETAISLTLNI----EG 259
Cdd:cd02257     20 --SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKslihDLFGGKLESTIVCLeCGHESVSTEPELFLSLPLpvkgLP 97
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  260 YCTLLDALDAYFGEEHLDDFKCSKCNKTG--DVSKQSDYVKLPPVIVIQLNRYKYTSKGR-QKLKTPMAYPREIPAKAF- 335
Cdd:cd02257     98 QVSLEDCLEKFFKEEILEGDNCYKCEKKKkqEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSFPLELDLSPYl 177
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972232041  336 --QRTNNSIPPPAEMYDLFAVTIHEGNNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPK 392
Cdd:cd02257    178 seGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSE 236
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-431 3.47e-48

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: 175.52  E-value: 3.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDFrPSENFVPPEAPRmnvqatMLALQDIFYTLQTTP-----FNETDKTSNL 183
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSV------PLALQRLFLFLQLSEspvktTELTDKTRSF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  184 GKlLRLNS-EQQDSQEFGLKFFNALERCLPdhpnGKETLKRLKDLFTGETCTRIVCK-CGQRSEREETAISLTLNIEGYC 261
Cdd:cd02659     77 GW-DSLNTfEQHDVQEFFRVLFDKLEEKLK----GTGQEGLIKNLFGGKLVNYIICKeCPHESEREEYFLDLQVAVKGKK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  262 TLLDALDAYFGEEHLDD---FKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKY--TSKGRQKLKTPMAYPREIPAKAF- 335
Cdd:cd02659    152 NLEESLDAYVQGETLEGdnkYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLELDMEPYt 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  336 -------QRTNNSIPPPAEMYDLFAVTIHEGnNAECGHYYDLIKSPLNQKWYRYNDEAIEAIpkppgteKPTTAK----- 403
Cdd:cd02659    232 ekglakkEGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPF-------DPNDAEeecfg 303
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1972232041  404 ---TEKSRKKDKEKYPTDQKAcYGLLYRRRD 431
Cdd:cd02659    304 geeTQKTYDSGPRAFKRTTNA-YMLFYERKS 333
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
189-392 2.10e-35

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: 134.72  E-value: 2.10e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  189 LNSEQQDSQEFGLKFFNALERclpdhpngketlkRLKDLFTGETCTRIVC-KCGQRSEREETAISLTLNI------EGYC 261
Cdd:cd02674     18 LSADQQDAQEFLLFLLDGLHS-------------IIVDLFQGQLKSRLTClTCGKTSTTFEPFTYLSLPIpsgsgdAPKV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  262 TLLDALDAYFGEEHLDD---FKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREIPAKAFQRT 338
Cdd:cd02674     85 TLEDCLRLFTKEETLDGdnaWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVD 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1972232041  339 NNSIPPPAEmYDLFAVTIHEGNNaECGHYYDLIKSPLNQKWYRYNDEAIEAIPK 392
Cdd:cd02674    165 TRSFTGPFK-YDLYAVVNHYGSL-NGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
107-390 3.73e-34

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: 133.56  E-value: 3.73e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  107 PAGLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVPPEAPRM-NVQA-TMLALQDIFYTLQTTPFNetDKTSNLG 184
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMcALEAhVERALASSGPGSAPRIFS--SNLKQIS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  185 KLLRLNSeQQDSQEFgLKFF-NALER-CLPDHPNGKETLKRLK------DLFTGETCTRIVC-KCGQRSEREETAISLTL 255
Cdd:cd02661     79 KHFRIGR-QEDAHEF-LRYLlDAMQKaCLDRFKKLKAVDPSSQettlvqQIFGGYLRSQVKClNCKHVSNTYDPFLDLSL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  256 NIEGYCTLLDALDAYFGEEHLDD---FKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGrqKLKTPMAYPREIPA 332
Cdd:cd02661    157 DIKGADSLEDALEQFTKPEQLDGenkYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFPETLDL 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972232041  333 KAFQRTNNSIPPpaeMYDLFAVTIHEGNNAECGHYYDLIKSPlNQKWYRYNDEAIEAI 390
Cdd:cd02661    235 SPYMSQPNDGPL---KYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDDSKVSPV 288
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-398 5.54e-30

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: 121.66  E-value: 5.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLiYDFRPSENFVPPEAPRMNVQATMLALQDIF----------YTLQTTPFNETD 178
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWR-YDDLENKFPSDVVDPANDLNCQLIKLADGLlsgryskpasLKSENDPYQVGI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  179 KTSNLGKLLRLN------SEQQDSQEFGLKFFNALERCLpdHPNGKETLKRLKDLFTGEtctRIVCKCGQR---SEREET 249
Cdd:cd02658     80 KPSMFKALIGKGhpefstMRQQDALEFLLHLIDKLDRES--FKNLGLNPNDLFKFMIED---RLECLSCKKvkyTSELSE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  250 AISLTLNIE------------GYCTLLDALDAYFGEEHLDDFKCSKCNKTGdVSKQSDYVKLPPVIVIQLNRYKYTSKGR 317
Cdd:cd02658    155 ILSLPVPKDeatekeegelvyEPVPLEDCLKAYFAPETIEDFCSTCKEKTT-ATKTTGFKTFPDYLVINMKRFQLLENWV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  318 Q-KLKTPMAYPREI-PAKafqrtnnsipppaemYDLFAVTIHEGNNAECGHYYDLIKSPLN--QKWYRYNDEAIEAIPKP 393
Cdd:cd02658    234 PkKLDVPIDVPEELgPGK---------------YELIAFISHKGTSVHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDP 298

                   ....*
gi 1972232041  394 PGTEK 398
Cdd:cd02658    299 PEMKK 303
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
109-485 1.64e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 127.68  E-value: 1.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDfrpsenfVPPEAPRMNvQATMLALQDIFYTLQTT--PFNETDKTSNLGKL 186
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYG-------IPTDHPRGR-DSVALALQRLFYNLQTGeePVDTTELTRSFGWD 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  187 LRLNSEQQDSQEFGLKFFNALERCLpdhpNGKETLKRLKDLFTGETCTRIVC-KCGQRSEREETAISLTLNIEGYCTLLD 265
Cdd:COG5077    267 SDDSFMQHDIQEFNRVLQDNLEKSM----RGTVVENALNGIFVGKMKSYIKCvNVNYESARVEDFWDIQLNVKGMKNLQE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  266 ALDAYFGEEHLDDFKCSKCNKTG--DVSKQSDYVKLPPVIVIQLNRYKYTSKGRQ--KLKTPMAYPREIPAKAF-QRTNN 340
Cdd:COG5077    343 SFRRYIQVETLDGDNRYNAEKHGlqDAKKGVIFESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLEIDLLPFlDRDAD 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  341 SIPPPAEMYDLFAVTIHEGNNAEcGHYYDLIKSPLNQKWYRYNDEAI------EAIPKPPGTEKPTtakTEKSRKKDKEK 414
Cdd:COG5077    423 KSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEKDGRWYKFDDTRVtratekEVLEENFGGDHPY---KDKIRDHSGIK 498
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972232041  415 YPTdqkACYGLLYRRRDafkplphpkLPPEELIIDSKTEIEELFEGLTKKKIEKSEKRLYDLERRINKVKI 485
Cdd:COG5077    499 RFM---SAYMLVYLRKS---------MLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGV 557
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-390 1.73e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 105.92  E-value: 1.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVPPEAPRMNVQATMLALQDIFYTLQTTPFNETD-------KTS 181
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINllylswkHSR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  182 NLGkllrlNSEQQDSQEFglkFFNALERCLPDHPNGKETLKRLKD-------LFTGETCTRIVC-KCGQRSEREETAISL 253
Cdd:cd02660     82 NLA-----GYSQQDAHEF---FQFLLDQLHTHYGGDKNEANDESHcnciihqTFSGSLQSSVTCqRCGGVSTTVDPFLDL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  254 TLNIE---------------GYCTLLDALDAYFGEEHLDDF--KCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKG 316
Cdd:cd02660    154 SLDIPnkstpswalgesgvsGTPTLSDCLDRFTRPEKLGDFayKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNK 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  317 -RQKLKTPMAYPREIPAKAFqrTNNSI--------PPPAEMYDLFAVTIHEGnNAECGHYYDLIKSPLNQkWYRYNDEAI 387
Cdd:cd02660    234 tSRKIDTYVQFPLELNMTPY--TSSSIgdtqdsnsLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQ-WFKFDDAMI 309

                   ...
gi 1972232041  388 EAI 390
Cdd:cd02660    310 TRV 312
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-392 2.07e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 105.08  E-value: 2.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNvpefrqliydfrpsenfvppeaprmnvqATML-ALQDIFYTL----------QTTPFNET 177
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYF----------------------------ENLLtCLKDLFESIseqkkrtgviSPKKFITR 52
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  178 DKTSNLgklLRLNSEQQDSQEFGLKFFNALERCLpDHPNGKETLKR--------------LKDLFTGETCTRIVC-KCGQ 242
Cdd:cd02663     53 LKRENE---LFDNYMHQDAHEFLNFLLNEIAEIL-DAERKAEKANRklnnnnnaepqptwVHEIFQGILTNETRClTCET 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  243 RSEREETAISLTLNIEGYCTLLDALDAYFGEEHL---DDFKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSK-GR- 317
Cdd:cd02663    129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLcgrNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQlNRy 208
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972232041  318 QKLKTPMAYPREIpaKAFQRTNNSiPPPAEMYDLFAVTIHEGNNAECGHYYDLIKSplNQKWYRYNDEAIEAIPK 392
Cdd:cd02663    209 IKLFYRVVFPLEL--RLFNTTDDA-ENPDRLYELVAVVVHIGGGPNHGHYVSIVKS--HGGWLLFDDETVEKIDE 278
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-392 1.75e-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 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: 102.41  E-value: 1.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVppeapRMNVQATMLALQDIFYTLQTTPFNETDKT--SNLGKL 186
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGA-----NQSSDNLTNALRDLFDTMDKKQEPVPPIEflQLLRMA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  187 LRLNSE--------QQDSQEFGLKFFNALERCLPdhPNGKETLKrLKDLFTGETCTRIVCKCGQRSE----REETAISLT 254
Cdd:cd02657     76 FPQFAEkqnqggyaQQDAEECWSQLLSVLSQKLP--GAGSKGSF-IDQLFGIELETKMKCTESPDEEevstESEYKLQCH 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  255 LNIEGYC-TLLDALDAYFGEEhlDDFKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKT--PMAYPREIP 331
Cdd:cd02657    153 ISITTEVnYLQDGLKKGLEEE--IEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIlrKVKFPFELD 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972232041  332 AKAFQrtnnsipPPAEMYDLFAVTIHEGNNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPK 392
Cdd:cd02657    231 LYELC-------TPSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTE 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-384 2.98e-20

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 93.33  E-value: 2.98e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFR-QLIYDFRPSENfvppeaprmNVQATMLALQDIFYTLQTtpfneTDKTSNLGKLL 187
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRrQVLSLNLPRLG---------DSQSVMKKLQLLQAHLMH-----TQRRAEAPPDY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  188 RLNS---------EQQDSQEFgLKFFnalerclpdhpngketLKRLKDL----FTGETCTRIVC-KCGQRSEREETAISL 253
Cdd:cd02664     67 FLEAsrppwftpgSQQDCSEY-LRYL----------------LDRLHTLiekmFGGKLSTTIRClNCNSTSARTERFRDL 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  254 TLNiegYCTLLDALDAYFGEEHLDD---FKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKG--RQKLKTPMAYPR 328
Cdd:cd02664    130 DLS---FPSVQDLLNYFLSPEKLTGdnqYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKThvREKIMDNVSINE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  329 --EIPAKAFQRTNNSIPPPAEM--------------YDLFAVTIHEGNNAECGHYYDLIKSP------------------ 374
Cdd:cd02664    207 vlSLPVRVESKSSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaee 286
                          330
                   ....*....|..
gi 1972232041  375 --LNQKWYRYND 384
Cdd:cd02664    287 ndESKNWYLFND 298
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-388 5.38e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 84.73  E-value: 5.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRqliydfrpsenfvppeaprmnvqatmlalqdifytlqttpfnetdktsnlgKLLR 188
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLI---------------------------------------------------EYLE 29
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  189 LNSEQQDSQEFGLKFFNALERcLPDHPngketlkrlkdlFTGETCTRIVC-KCGQRSE-REETAISLTLNI-----EGYC 261
Cdd:cd02662     30 EFLEQQDAHELFQVLLETLEQ-LLKFP------------FDGLLASRIVClQCGESSKvRYESFTMLSLPVpnqssGSGT 96
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  262 TLLDALDAYFGEEHLDDFKCSKCnktgdvskQSDYVKLPPVIVIQLNRYKYTSKGR-QKLKTPMAYPREIPAKafqrtnn 340
Cdd:cd02662     97 TLEHCLDDFLSTEIIDDYKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTsTKNSCKVSFPERLPKV------- 161
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972232041  341 sipppaeMYDLFAVTIHEGnNAECGHYYDLIKSPLNQK--------------------WYRYNDEAIE 388
Cdd:cd02662    162 -------LYRLRAVVVHYG-SHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVK 221
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
109-391 6.14e-16

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 79.74  E-value: 6.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQLIYDfRPSENF--VPPEAPRmnvqatmlalqdifytlqttpFNETDktsnlgkl 186
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-TPKELFsqVCRKAPQ---------------------FKGYQ-------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  187 lrlnseQQDSQEfglkffnaLERCLPDhpnGKETlkRLKDLFTGETCTRIVC-KCGQRSEREETAISLTL----NIEGYC 261
Cdd:cd02667     51 ------QQDSHE--------LLRYLLD---GLRT--FIDSIFGGELTSTIMCeSCGTVSLVYEPFLDLSLprsdEIKSEC 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  262 TLLDALDAYFGEEHLDD---FKCSKCNKTgdvSKQSDYVKLPPVIVIQLNRYKYTSKGR-QKLKTPMAYPREIPAKAFQR 337
Cdd:cd02667    112 SIESCLKQFTEVEILEGnnkFACENCTKA---KKQYLISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFPEILDLAPFCD 188
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972232041  338 TNNSIPPPAE--MYDLFAVTIHEGnNAECGHYYDLIKS---------------------PLNQKWYRYNDEAIEAIP 391
Cdd:cd02667    189 PKCNSSEDKSsvLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVS 264
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
107-391 3.80e-15

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 78.30  E-value: 3.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  107 PAGLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVP---PEAPRMNVQATMLA-----------LQDIFYTLQTT 172
Cdd:cd02666      1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELAsdyPTERRIGGREVSRSelqrsnqfvyeLRSLFNDLIHS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  173 PFNETDKTSNLGKL-LRlnseQQDSQE-FGLKFFN---ALER-----CLPDHPNGKETLKRLKDLFTGETCTRIV-CKCG 241
Cdd:cd02666     81 NTRSVTPSKELAYLaLR----QQDVTEcIDNVLFQlevALEPisnafAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  242 QRSERE---ETAISLTLNI----------EGYCTLLDALDAYFGEEHL-------DDFKCSKCNKTGDVSKQSDYvKLPP 301
Cdd:cd02666    157 NQPSVRtktERFLSLLVDVgkkgreivvlLEPKDLYDALDRYFDYDSLtklpqrsQVQAQLAQPLQRELISMDRY-ELPS 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  302 VIVIQLNRYKYTSKGRQKLKTPMAypREIPAKAFQRTN-----NSIPppaemYDLFAVTIHEGnNAECGHYYDLIKSPLN 376
Cdd:cd02666    236 SIDDIDELIREAIQSESSLVRQAQ--NELAELKHEIEKqfddlKSYG-----YRLHAVFIHRG-EASSGHYWVYIKDFEE 307
                          330
                   ....*....|....*
gi 1972232041  377 QKWYRYNDEAIEAIP 391
Cdd:cd02666    308 NVWRKYNDETVTVVP 322
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
189-387 4.99e-15

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 75.67  E-value: 4.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  189 LNSEQQDSQEFGLKFFNALERC----LPDHPNGKETLKRLKDLFTGETCTRIVCKcGQRSEREETAISLTLNIEGYCTLL 264
Cdd:cd02665     18 LFSQQQDVSEFTHLLLDWLEDAfqaaAEAISPGEKSKNPMVQLFYGTFLTEGVLE-GKPFCNCETFGQYPLQVNGYGNLH 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  265 DALDAYFGEEHLDDFKCSKCNKTGdvsKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREIpakafqrtnNSIPp 344
Cdd:cd02665     97 ECLEAAMFEGEVELLPSDHSVKSG---QERWFTELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII---------QQVP- 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1972232041  345 paemYDLFAVTIHEGnNAECGHYYDLIKSPLNQKWYRYNDEAI 387
Cdd:cd02665    164 ----YELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISV 201
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
108-389 1.18e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 70.69  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  108 AGLINGGNFCYVNSFLQVWFNVPEFRQLIYDFrpsenfvppeaprMNVQATMLALQDIFYTLQTTpFNETDKTSNLGKLL 187
Cdd:cd02671     25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL-------------VSLISSVEQLQSSFLLNPEK-YNDELANQAPRRLL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  188 ----RLNS-----EQQDSQEFGLKFFNALERClpdhpngketlkrLKDLFTGETCTRIVC-KCGQRSEREE--------T 249
Cdd:cd02671     91 nalrEVNPmyegyLQHDAQEVLQCILGNIQEL-------------VEKDFQGQLVLRTRClECETFTERREdfqdisvpV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  250 AISLTLNIEGYC-----------TLLDALDAYFGEEHL---DDFKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSK 315
Cdd:cd02671    158 QESELSKSEESSeispdpktemkTLKWAISQFASVERIvgeDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGS 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  316 ------GRQKLKTPMAYPREIPAKAFqrtnnSIPPPAEMYDLFAVTIHEGNNAECGHYYDLIksplnqKWYRYNDEAIEA 389
Cdd:cd02671    238 efdcygGLSKVNTPLLTPLKLSLEEW-----STKPKNDVYRLFAVVMHSGATISSGHYTAYV------RWLLFDDSEVKV 306
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
109-391 1.53e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 69.45  E-value: 1.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQV-WFNVPEFRQLIYDfrpsenfvppeaPRMNVQATMLALQDIFYTL---QTTPFNETDKTSNLG 184
Cdd:COG5533      1 GLPNLGNTCFMNSVLQIlALYLPKLDELLDD------------LSKELKVLKNVIRKPEPDLnqeEALKLFTALWSSKEH 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  185 KLLRLN--SEQQDSQEFGLKFFNALErcLPDHPNGKE----TLKRLKDLFTGETCTRIVCKCGQRSEREETaisltlnie 258
Cdd:COG5533     69 KVGWIPpmGSQEDAHELLGKLLDELK--LDLVNSFTIrifkTTKDKKKTSTGDWFDIIIELPDQTWVNNLK--------- 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  259 gycTLLDALDAYfgEEHLDDFKCSKC--NKTGDVSKQSDY----VKLPPVIVIQLNRYKYtSKGRQKLKTPMAYPREIPA 332
Cdd:COG5533    138 ---TLQEFIDNM--EELVDDETGVKAkeNEELEVQAKQEYevsfVKLPKILTIQLKRFAN-LGGNQKIDTEVDEKFELPV 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972232041  333 KAFQRTNNSippPAEMYDLFAVTIHEGNNAEcGHYYDLIKSplNQKWYRYNDEAIEAIP 391
Cdd:COG5533    212 KHDQILNIV---KETYYDLVGFVLHQGSLEG-GHYIAYVKK--GGKWEKANDSDVTPVS 264
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
262-390 9.53e-12

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 69.53  E-value: 9.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  262 TLLDALDAYFGEEHL---DDFKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPreIPAKAFQRT 338
Cdd:COG5560    676 TLQDCLNEFSKPEQLglsDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYP--IDDLDLSGV 753
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1972232041  339 NNSIPPPAEMYDLFAVTIHEGNNAEcGHYYDLIKSPLNQKWYRYNDEAIEAI 390
Cdd:COG5560    754 EYMVDDPRLIYDLYAVDNHYGGLSG-GHYTAYARNFANNGWYLFDDSRITEV 804
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
108-384 3.19e-10

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 63.06  E-value: 3.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  108 AGLINGGNFCYVNSFLQVWFNVPEFRQLI-------------------YDFRPSENfvppeAPRMNVQATmlalqdifyT 168
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAlshlateclkehcllcelgFLFDMLEK-----AKGKNCQAS---------N 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  169 LQTTpFNETDKTSNLGkLLRLNSEQQDSQEFG--LKFFNaleRCLPDH---------PNGKETLKRLKDLFTGETCTRIV 237
Cdd:pfam13423   67 FLRA-LSSIPEASALG-LLDEDRETNSAISLSslIQSFN---RFLLDQlsseenstpPNPSPAESPLEQLFGIDAETTIR 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  238 C-KCGQRSEREETAISLTL----------NIEGYCTLLDALDAYFGEEHLDDFKCSKCNKTGDVSKQSDYVKLPPVIVIQ 306
Cdd:pfam13423  142 CsNCGHESVRESSTHVLDLiyprkpssnnKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLN 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  307 LNRYkyTSKGRQKLKTPMAYPREIpaKAFQRTNNSIPPPAEMYDLFAVTIHEGNNAECGHYYDLIK-------SPLNQKW 379
Cdd:pfam13423  222 AALT--NEEWRQLWKTPGWLPPEI--GLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQW 297

                   ....*
gi 1972232041  380 YRYND 384
Cdd:pfam13423  298 YLFND 302
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
1159-1262 1.25e-09

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 56.52  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041 1159 RRGRAKNLyAIKMSSTNKLMELKVQLYDKTHQLPNDQLLYrTAGGEqfdVSNNQKTLFDLRLSPNNNdnpLILIAQQF-- 1236
Cdd:cd01795      1 RRVRGERK-SLTVSSTTTLKELKLQIMEKFSVAPFDQHLY-FNGRE---LTDDSATLADLGILPGDV---LYLKVDEPpd 72
                           90       100
                   ....*....|....*....|....*..
gi 1972232041 1237 -SPSASQADETGDRAPERGFVDTALAH 1262
Cdd:cd01795     73 dPDDADEADVSRARVPEEGFKGTALLG 99
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
174-392 6.78e-06

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 49.06  E-value: 6.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  174 FNET-DKTSNLGKLLR--LNSEQQDSQEFGLKFFNALERCL----PDHPNGKETLKRLKDL----FTGETCtRIVCKCGQ 242
Cdd:cd02673     11 FNSTmQALSSIGKINTefDNDDQQDAHEFLLTLLEAIDDIMqvnrTNVPPSNIEIKRLNPLeafkYTIESS-YVCIGCSF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  243 RSEREETAISLTLNIE--GYCTLLDALDAYFGEEHLDDfKCSKCNKTGDVSKQsDYVKLPPVIVIQLNRYKY---TSKGR 317
Cdd:cd02673     90 EENVSDVGNFLDVSMIdnKLDIDELLISNFKTWSPIEK-DCSSCKCESAISSE-RIMTFPECLSINLKRYKLriaTSDYL 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972232041  318 QKLKTPMaypreipaKAFQRTNNSipppaemYDLFAVTIHEGNNAECGHYYDLIKSPLN-QKWYRYNDEAIEAIPK 392
Cdd:cd02673    168 KKNEEIM--------KKYCGTDAK-------YSLVAVICHLGESPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSK 228
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
109-257 2.46e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 45.64  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  109 GLINGGNFCYVNSFLQVWFNVPEFRQ-LIYD-FRPSENFVPPEAPRMNVQATMLALQDIFYTLQTTPFNETDKTSNLGKl 186
Cdd:COG5560    267 GLRNLGNTCYMNSALQCLMHTWELRDyFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGS- 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972232041  187 lrLNSE-----QQDSQEFGLKFFNALERCL-----------PD-HPNGKETLKRLK----------------DLFTGETC 233
Cdd:COG5560    346 --FNEEfsgydQQDSQEFIAFLLDGLHEDLnriikkpytskPDlSPGDDVVVKKKAkecwwehlkrndsiitDLFQGMYK 423
                          170       180
                   ....*....|....*....|....*
gi 1972232041  234 TRIVCK-CGQRSEREETAISLTLNI 257
Cdd:COG5560    424 STLTCPgCGSVSITFDPFMDLTLPL 448
 
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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