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Conserved domains on  [gi|557947984|ref|NP_001273697|]
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ubiquitin carboxyl-terminal hydrolase 46 isoform 4 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 913)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1-217 1.82e-142

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.


The actual alignment was detected with superfamily member cd02663:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 300  Bit Score: 399.76  E-value: 1.82e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENnkpeltWVHEIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02663   64 MHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT------WVHEIFQGILTNETRCLTCETVSSRDETFL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVF 160
Cdd:cd02663  138 DLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557947984 161 PLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVE 217
Cdd:cd02663  218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVE 274
 
Name Accession Description Interval E-value
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-217 1.82e-142

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: 399.76  E-value: 1.82e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENnkpeltWVHEIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02663   64 MHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT------WVHEIFQGILTNETRCLTCETVSSRDETFL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVF 160
Cdd:cd02663  138 DLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557947984 161 PLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVE 217
Cdd:cd02663  218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVE 274
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-218 2.44e-57

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 183.80  E-value: 2.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984    1 MQQDAHEFLNYLLNTiadiLQEEKKQEkqngklkngnmnepaeNNKPELTWVHEIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:pfam00443  87 KQQDAQEFLLFLLDG----LHEDLNGN----------------HSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   81 DLSVDVEQNTSITH------CLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQLHRYTKL 154
Cdd:pfam00443 147 DLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--NRSTWEKL 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  155 SYRVVFPLELRLFNTSSDAVNLD----RMYDLVAVVVHCGSgPNRGHYITIVKS--HGFWLLFDDDIVEV 218
Cdd:pfam00443 225 NTEVEFPLELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTE 293
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1-225 2.17e-20

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 89.16  E-value: 2.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984    1 MQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:COG5077   272 MQHDIQEFNRVLQ----DNLEKSMRGTVVENALNG-------------------IFVGKMKSYIKCVNVNYESARVEDFW 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETcCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVF 160
Cdd:COG5077   329 DIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEF 407
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557947984  161 PLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKSH--GFWLLFDDDIV-EVGLQIILQ 225
Cdd:COG5077   408 PLEIDLLpfldRDADKSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFDDTRVtRATEKEVLE 478
 
Name Accession Description Interval E-value
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-217 1.82e-142

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: 399.76  E-value: 1.82e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENnkpeltWVHEIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02663   64 MHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT------WVHEIFQGILTNETRCLTCETVSSRDETFL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVF 160
Cdd:cd02663  138 DLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557947984 161 PLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVE 217
Cdd:cd02663  218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVE 274
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1-218 4.54e-60

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: 189.23  E-value: 4.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILQEEKKQEkqngklkngnmnepaENNKPELTWVHEIFQGTLTNETRCLNC--ETVSSKDED 78
Cdd:cd02257   21 EQQDAHEFLLFLLDKLHEELKKSSKRT---------------SDSSSLKSLIHDLFGGKLESTIVCLECghESVSTEPEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  79 FLDLSVDVEQ--NTSITHCLRDFSNTETLCSEQKYYCEtCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLhRYTKLSY 156
Cdd:cd02257   86 FLSLPLPVKGlpQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDG-TKEKLNT 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 157 RVVFPLELRLFN------TSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKS--HGFWLLFDDDIVEV 218
Cdd:cd02257  164 KVSFPLELDLSPylsegeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDpsDGKWYKFNDDKVTE 233
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-218 2.44e-57

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 183.80  E-value: 2.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984    1 MQQDAHEFLNYLLNTiadiLQEEKKQEkqngklkngnmnepaeNNKPELTWVHEIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:pfam00443  87 KQQDAQEFLLFLLDG----LHEDLNGN----------------HSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   81 DLSVDVEQNTSITH------CLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQLHRYTKL 154
Cdd:pfam00443 147 DLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--NRSTWEKL 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  155 SYRVVFPLELRLFNTSSDAVNLD----RMYDLVAVVVHCGSgPNRGHYITIVKS--HGFWLLFDDDIVEV 218
Cdd:pfam00443 225 NTEVEFPLELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTE 293
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-216 1.35e-46

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: 155.90  E-value: 1.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTiadilqeekkqeKQNGKLKNGNMNEPAENNKPELTWVHEIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02661   85 RQEDAHEFLRYLLDA------------MQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeqlHRYTKLSYRVVF 160
Cdd:cd02661  153 DLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQISF 228
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557947984 161 PLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK-SHGFWLLFDDDIV 216
Cdd:cd02661  229 PETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKsSNGKWYNMDDSKV 285
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-217 1.66e-46

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: 156.65  E-value: 1.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02659   85 EQHDVQEFFRVLF----DKLEEKLKGTGQEGLIKN-------------------LFGGKLVNYIICKECPHESEREEYFL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKY-MEQLHRYtKLSYRVV 159
Cdd:cd02659  142 DLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdFETMMRI-KINDRFE 220
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557947984 160 FPLEL-----------RLFNTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKS--HGFWLLFDDDIVE 217
Cdd:cd02659  221 FPLELdmepytekglaKKEGDSEKKDSESYIYELHGVLVHSGDAHG-GHYYSYIKDrdDGKWYKFNDDVVT 290
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-216 2.15e-40

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: 140.59  E-value: 2.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIAdilQEEKKQEKQNGKLKNGNmnepaennkpelTWVHEIFQGTLTNETRCLNCETVSSKDEDFLD 81
Cdd:cd02660   88 QQDAHEFFQFLLDQLH---THYGGDKNEANDESHCN------------CIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  82 LSVDVEQNT---------------SITHCLRDFSNTETLCSEQkYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmE 146
Cdd:cd02660  153 LSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEH-S 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 147 QLHRYTKLSYRVVFPLELRL--FNTSSDAVNLDR-------MYDLVAVVVHCGSgPNRGHYITIVKSH-GFWLLFDDDIV 216
Cdd:cd02660  231 LNKTSRKIDTYVQFPLELNMtpYTSSSIGDTQDSnsldpdyTYDLFAVVVHKGT-LDTGHYTAYCRQGdGQWFKFDDAMI 309
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-217 4.72e-39

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: 134.34  E-value: 4.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILQEekkqekqngklkngnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHSIIVD--------------------------------LFQGQLKSRLTCLTCGKTSTTFEPFT 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNT------SITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQlhRYTKL 154
Cdd:cd02674   69 YLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG--STRKL 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557947984 155 SYRVVFPLE---LRLFNTSSDAVNLDRmYDLVAVVVHCGSGpNRGHYITIVKSHGF--WLLFDDDIVE 217
Cdd:cd02674  147 TTPVTFPLNdldLTPYVDTRSFTGPFK-YDLYAVVNHYGSL-NGGHYTAYCKNNETndWYKFDDSRVT 212
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-217 2.15e-37

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: 132.93  E-value: 2.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIADILQEEKkqekqNGKLKNgnmnepaennkpeltWVHEIFQGTLTNETRCLNCETVSSKDEDFLD 81
Cdd:cd02668   88 QQDAQEFSKLFLSLLEAKLSKSK-----NPDLKN---------------IVQDLFRGEYSYVTQCSKCGRESSLPSKFYE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  82 LSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVFP 161
Cdd:cd02668  148 LELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFP 227
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557947984 162 LELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK--SHGFWLLFDDDIVE 217
Cdd:cd02668  228 EILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdeQTGEWYKFNDEDVE 285
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-205 1.41e-31

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: 116.33  E-value: 1.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIadilqeekkqekqngklkngnmnepaennkpeLTWVHEIFQGTLTNETRCLNCETVSSKDEDFLD 81
Cdd:cd02667   51 QQDSHELLRYLLDGL--------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  82 LS----VDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCskqEAQKRMRVKKLPMILALHLKRFKyMEQLHRYTKLSYR 157
Cdd:cd02667   99 LSlprsDEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ-QPRSANLRKVSRH 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557947984 158 VVFP--LELRLFNTSSDAVNLDR---MYDLVAVVVHCGSGpNRGHYITIVKSH 205
Cdd:cd02667  175 VSFPeiLDLAPFCDPKCNSSEDKssvLYRLYGVVEHSGTM-RSGHYVAYVKVR 226
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-218 2.09e-28

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 109.21  E-value: 2.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILQEekkqekqngklkngnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:cd02671  104 LQHDAQEVLQCILGNIQELVEK--------------------------------DFQGQLVLRTRCLECETFTERREDFQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVE-------------------QNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKR 141
Cdd:cd02671  152 DISVPVQeselskseesseispdpktEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKC 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 142 FKYMEQLHRY----TKLSYRVVFPLELRLFNTSSDAVNldRMYDLVAVVVHCGSGPNRGHYITIVKshgfWLLFDDDIVE 217
Cdd:cd02671  232 FAANGSEFDCygglSKVNTPLLTPLKLSLEEWSTKPKN--DVYRLFAVVMHSGATISSGHYTAYVR----WLLFDDSEVK 305

                 .
gi 557947984 218 V 218
Cdd:cd02671  306 V 306
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-216 3.95e-27

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: 105.65  E-value: 3.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLntiaDILQeekkqekqngklkngnmnepaennkpelTWVHEIFQGTLTNETRCLNCETVSSKDEDFLD 81
Cdd:cd02664   81 QQDCSEYLRYLL----DRLH----------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  82 LSVDVeqnTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVFP 161
Cdd:cd02664  129 LDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSIN 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 162 LELRL-----FNTSSDAVNLDRM--------------YDLVAVVVHCGSGPNRGHYITIVKS------------------ 204
Cdd:cd02664  206 EVLSLpvrveSKSSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepkdae 285
                        250
                 ....*....|....*.
gi 557947984 205 ----HGFWLLFDDDIV 216
Cdd:cd02664  286 endeSKNWYLFNDSRV 301
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1-225 2.17e-20

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 89.16  E-value: 2.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984    1 MQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSSKDEDFL 80
Cdd:COG5077   272 MQHDIQEFNRVLQ----DNLEKSMRGTVVENALNG-------------------IFVGKMKSYIKCVNVNYESARVEDFW 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   81 DLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETcCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVF 160
Cdd:COG5077   329 DIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEF 407
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557947984  161 PLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKSH--GFWLLFDDDIV-EVGLQIILQ 225
Cdd:COG5077   408 PLEIDLLpfldRDADKSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFDDTRVtRATEKEVLE 478
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-216 4.30e-20

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 86.61  E-value: 4.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIAdilQEEKKQEKQNgklkngnmnepaennkpeltwVHEIFQGTLTNETRCLNCETVSSKDEDFLD 81
Cdd:cd02658  100 QQDALEFLLHLIDKLD---RESFKNLGLN---------------------PNDLFKFMIEDRLECLSCKKVKYTSELSEI 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  82 LSVDVE--------------QNTSITHCLRDFSNTETLcseqKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQ 147
Cdd:cd02658  156 LSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN 231
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557947984 148 lHRYTKLSYRVVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGPNRGHYITIVK----SHGFWLLFDDDIV 216
Cdd:cd02658  232 -WVPKKLDVPIDVPEELGPGK-----------YELIAFISHKGTSVHSGHYVAHIKkeidGEGKWVLFNDEKV 292
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
91-217 6.78e-20

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 87.63  E-value: 6.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  91 SIT--HCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQLHRYTKLSYRVVFPLELRLFN 168
Cdd:COG5560  674 TITlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSS--VRSFRDKIDDLVEYPIDDLDLS 751
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557947984 169 TSSDAVNLDRM-YDLVAVVVHCGsGPNRGHYITIVK--SHGFWLLFDDDIVE 217
Cdd:COG5560  752 GVEYMVDDPRLiYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRIT 802
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-224 1.65e-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: 80.87  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIADILQEekkqekqngklkngnmnepaennkPeltwvheiFQGTLTNETRCLNCETVSSKDED-FL 80
Cdd:cd02662   34 QQDAHELFQVLLETLEQLLKF------------------------P--------FDGLLASRIVCLQCGESSKVRYEsFT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSIT-----HCLRDFSNTETLcseQKYYCETCcskQEAqkrmrVKKLPMILALHLKRFKYMEQLHrYTKLS 155
Cdd:cd02662   82 MLSLPVPNQSSGSgttleHCLDDFLSTEII---DDYKCDRC---QTV-----IVRLPQILCIHLSRSVFDGRGT-STKNS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 156 YRVVFPLELRlfntssdavnlDRMYDLVAVVVHCGSgPNRGHYITI-----------------------VKSHGFWLLFD 212
Cdd:cd02662  150 CKVSFPERLP-----------KVLYRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmregpsSTSHPWWRISD 217
                        250
                 ....*....|..
gi 557947984 213 DDIVEVGLQIIL 224
Cdd:cd02662  218 TTVKEVSESEVL 229
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-216 5.13e-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 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: 77.76  E-value: 5.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   1 MQQDAHEFLNYLLNTIADILqeekkqekqngklkngnmnepaENNKPELTWVHEIFQGTLTNETRCL---NCETVSSKDE 77
Cdd:cd02657   89 AQQDAEECWSQLLSVLSQKL----------------------PGAGSKGSFIDQLFGIELETKMKCTespDEEEVSTESE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  78 DFLDLSVDVEQNTSIthcLRDfSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYR 157
Cdd:cd02657  147 YKLQCHISITTEVNY---LQD-GLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRK 222
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557947984 158 VVFPLELRLFntssDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKS--HGFWLLFDDDIV 216
Cdd:cd02657  223 VKFPFELDLY----ELCTPSGYYELVAVITHQGRSADSGHYVAWVRRknDGKWIKFDDDKV 279
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-216 1.91e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 75.64  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIADILQEEKKQEKQNGKlkNGNMNEPAEnnkpeltwvheIFQGTLTNETRCLNC---ETVSSKDED 78
Cdd:cd02673   33 QQDAHEFLLTLLEAIDDIMQVNRTNVPPSNI--EIKRLNPLE-----------AFKYTIESSYVCIGCsfeENVSDVGNF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  79 fldLSVDVEQNTSITHCLRDFSNTETLCSEQKyyCETCcSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRV 158
Cdd:cd02673  100 ---LDVSMIDNKLDIDELLISNFKTWSPIEKD--CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557947984 159 VFPLELRLFNtssdavnldrmYDLVAVVVHCGSGPNRGHYITIVKS---HGFWLLFDDDIV 216
Cdd:cd02673  174 MKKYCGTDAK-----------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEI 223
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
39-213 1.05e-15

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 74.23  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   39 NEPAENNKPELTWVHEIFQGTLTNETRCLNCETVSSKDEDF--LDLSV--------DVEQNTSITHCLRDFSNTETLcse 108
Cdd:pfam13423 115 NSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSThvLDLIYprkpssnnKKPPNQTFSSILKSSLERETT--- 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  109 QKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFkymEQLHRYTKLSYRVvFPLELRLF-NTSSDAVNLDRMYDLVAVVV 187
Cdd:pfam13423 192 TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALT---NEEWRQLWKTPGW-LPPEIGLTlSDDLQGDNEIVKYELRGVVV 267
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 557947984  188 HCGSGPNRGHYITIVK---------SHGFWLLFDD 213
Cdd:pfam13423 268 HIGDSGTSGHLVSFVKvadseledpTESQWYLFND 302
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-217 1.06e-07

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 51.55  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIadilqeekkqEKQNGKLKNGNMNEpaennkpeltwVHEIFQGTLTNETRCLNCETVS-SKDEDFL 80
Cdd:cd02669  207 QSDPVEFLSWLLNTL----------HKDLGGSKKPNSSI-----------IHDCFQGKVQIETQKIKPHAEEeGSKDKFF 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  81 DLSVDVEQNTSITHCLR---------DFSNTETLCSE-------QKYYCETCCSKQEAQKRMRVKKLPMILALHLKRF-K 143
Cdd:cd02669  266 KDSRVKKTSVSPFLLLTldlpppplfKDGNEENIIPQvplkqllKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFsK 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 144 YMEQLHRYTKLsyrVVFPLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIV--KSHGFWLLFDDDIVE 217
Cdd:cd02669  346 NNFFKEKNPTI---VNFPIKNLDLsdyvHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrhKSTNKWFEIQDLNVK 422
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-213 7.01e-06

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 45.63  E-value: 7.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984   2 QQDAHEFLNYLLNTIADILQEEkkqekqngklkngnMNEPAENNKPELTWVhEIFQGTLTNE-----TRCLNCETvsskd 76
Cdd:cd02665   22 QQDVSEFTHLLLDWLEDAFQAA--------------AEAISPGEKSKNPMV-QLFYGTFLTEgvlegKPFCNCET----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984  77 edFLDLSVDVEQNTSITHCLRDFS---NTETLCSEQkyycetccSKQEAQKRMrVKKLPMILALHLKRFKYMEQlhRYTK 153
Cdd:cd02665   82 --FGQYPLQVNGYGNLHECLEAAMfegEVELLPSDH--------SVKSGQERW-FTELPPVLTFELSRFEFNQG--RPEK 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557947984 154 LSYRVVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGpNRGHYITIV--KSHGFWLLFDD 213
Cdd:cd02665  149 IHDKLEFPQIIQQVP-----------YELHAVLVHEGQA-NAGHYWAYIykQSRQEWEKYND 198
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
104-217 2.60e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 40.96  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947984 104 TLCSEQ--KYYCETCCSKQEAQKRMRVKKLPMI----LALHLKRFKYME-----QLHRYTKLSYRVVFPLELRLFNTSSD 172
Cdd:cd02672  126 SLDLEKvtKAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvVLPSGKVMQNKVSPKAIDHDKLVKNR 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557947984 173 AVNLDRMYDLVAVVVHCGSGPNRGHYITIV------KSHGFWLLFDDDIVE 217
Cdd:cd02672  206 GQESIYKYELVGYVCEINDSSRGQHNVVFVikvneeSTHGRWYLFNDFLVT 256
 
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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