|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-344 |
5.53e-134 |
|
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: 412.42 E-value: 5.53e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 39 NLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLT 118
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 119 DSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGL 198
Cdd:cd02659 74 RSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 199 EDALWNmYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLKPFCE 278
Cdd:cd02659 154 EESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918667 279 QSE---------LDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHLGNWQFQEEKSKP----DVNLKDLQSEEEIDHP 344
Cdd:cd02659 233 KGLakkegdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPfdpnDAEEECFGGEETQKTY 311
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
42-319 |
1.62e-53 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 189.96 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSlgpeelGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAA-STADLTDS 120
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 121 FGWTSNE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:pfam00443 76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 196 SGLE--DALWNMYVE---EEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFD---FVKCERYKEtscytF 267
Cdd:pfam00443 156 SAELktASLQICFLQfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNrstWEKLNTEVE-----F 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767918667 268 PLRINLKPFC--EQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNW 319
Cdd:pfam00443 231 PLELDLSRYLaeELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEN-NRW 283
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
35-319 |
1.36e-52 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 202.02 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 35 REFTNLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglfeDKDKPDAKvRIIPLQLQRLFAQLLLLDqEAAST 114
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQTGE-EPVDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 115 ADLTDSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKN 194
Cdd:COG5077 257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 195 VSGLEDALWNmYVEEEVFDCDNLYHCGTCDrLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLK 274
Cdd:COG5077 337 MKNLQESFRR-YIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767918667 275 PF----CEQSELDDleYIYDLFSVIIHKGGCYGGHYHVYIK-DVDhlGNW 319
Cdd:COG5077 415 PFldrdADKSENSD--AVYVLYGVLVHSGDLHEGHYYALLKpEKD--GRW 460
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-325 |
1.05e-47 |
|
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: 173.76 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLG-PEELGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLTDS 120
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNsTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 121 FGwTSNEEmrQHDVQELNRILFSALETSLVGTSGHDL---IYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG 197
Cdd:cd02668 81 LG-LDTGQ--QQDAQEFSKLFLSLLEAKLSKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 198 LEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLKPFC 277
Cdd:cd02668 158 LEECI-DEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767918667 278 EQSELDDleYIYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW-QFQEEK 325
Cdd:cd02668 237 AESDEGS--YVYELSGVLIHQGvSAYSGHYIAHIKD-EQTGEWyKFNDED 283
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
42-339 |
6.94e-45 |
|
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: 163.04 E-value: 6.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHftpefrealfslgpeelglfedkdkpdakvriiplqlqrlfaqlllldqeaastadltdsf 121
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 122 gwtsneeMRQHDVQELNRILFSALETSLVG--------TSGHDLIYRLYHGTIVNQIVCKECK--NVSERQEDFLDLTVA 191
Cdd:cd02257 20 -------SEQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGheSVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 192 VKNVSG--LEDALwNMYVEEEVFDCDNLYHCGtCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvKCERYKETSCYTFPL 269
Cdd:cd02257 93 VKGLPQvsLEDCL-EKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPL 169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918667 270 RINLKPFCEQSELDDLE----YIYDLFSVIIHKGG-CYGGHYHVYIKDVDHLGNWQFQ----EEKSKPDVNLKDLQSEE 339
Cdd:cd02257 170 ELDLSPYLSEGEKDSDSdngsYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNddkvTEVSEEEVLEFGSLSSS 248
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
41-319 |
4.26e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 142.03 E-value: 4.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 41 SGIRNQGGTCYLNSLLQTLHFTPEFREALFSLGpeelglfEDKDKPDAKVRIIpLQLQRLFAQLLLLDQEAASTADLTDS 120
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSRE-------HSKDCCNEGFCMM-CALEAHVERALASSGPGSAPRIFSSN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 121 FGWTSNEEM--RQHDVQELNRILFSALETS----LVGTSGHD-------LIYRLYHGTIVNQIVCKECKNVSERQEDFLD 187
Cdd:cd02661 74 LKQISKHFRigRQEDAHEFLRYLLDAMQKAcldrFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 188 LTVAVKNVSGLEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvkceRYKETSCYTF 267
Cdd:cd02661 154 LSLDIKGADSLEDAL-EQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR----GGKINKQISF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767918667 268 PLRINLKPFCEQSEldDLEYIYDLFSVIIHKGG-CYGGHYHVYIKDVDhlGNW 319
Cdd:cd02661 229 PETLDLSPYMSQPN--DGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSN--GKW 277
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-319 |
4.05e-29 |
|
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: 119.78 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGLFEDKDKpdakvrIIPLQLQRLFAQLllldqeaaSTADLTDSF 121
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNS------CLSCAMDEIFQEF--------YYSGDRSPY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 122 G--------WTSNEEM---RQHDVQELNRILFSALETSLVGTSGHD--------LIYRLYHGTIVNQIVCKECKNVSERQ 182
Cdd:cd02660 68 GpinllylsWKHSRNLagySQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcncIIHQTFSGSLQSSVTCQRCGGVSTTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 183 EDFLDLTVAVKNVSG---------------LEDALWNMYVEEEVfdCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLL 247
Cdd:cd02660 148 DPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL--GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918667 248 RFNFDFVKCERyKETSCYTFPLRINLKPFCEQSELDDLE-------YIYDLFSVIIHKGGCYGGHYHVYIKdvDHLGNW 319
Cdd:cd02660 226 RFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdYTYDLFAVVVHKGTLDTGHYTAYCR--QGDGQW 301
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-314 |
4.76e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 116.44 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGlfedkdkpdaKVRIIPLQLQRLFAQLLLLDQEAASTAD--LTD 119
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLG----------DSQSVMKKLQLLQAHLMHTQRRAEAPPDyfLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 120 SF--GWTSNeemRQHDVQELNRILFSALetslvgtsgHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVsg 197
Cdd:cd02664 71 SRppWFTPG---SQQDCSEYLRYLLDRL---------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSV-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 198 lEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvKCE-RYK---------------- 260
Cdd:cd02664 137 -QDLL-NYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ-KTHvREKimdnvsinevlslpvr 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 767918667 261 -ETSCYTFPLRINLKPFCEQSELDDLEYIYDLFSVIIHKG-GCYGGHYHVYIKDVD 314
Cdd:cd02664 214 vESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQT 269
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-325 |
1.39e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 114.33 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFtpefrEALFSLGPEelgLFEDKDKPDAKVRIIPLQLqrlFAQLLLLDQEAASTADLTDS- 120
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLTCLKD---LFESISEQKKRTGVISPKK---FITRLKRENELFDNYMHQDAh 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 121 --FGWTSN---EEMRQHDVQELNRILFSALETSlvgTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:cd02663 70 efLNFLLNeiaEILDAERKAEKANRKLNNNNNA---EPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 196 SGLEDALWNMYvEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDfVKCERYKETScYTFPLRINLKP 275
Cdd:cd02663 147 TSITSCLRQFS-ATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD-EQLNRYIKLF-YRVVFPLELRL 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767918667 276 FCEQSELDDLEYIYDLFSVIIHKG-GCYGGHyhvYIKDVDHLGNW-QFQEEK 325
Cdd:cd02663 224 FNTTDDAENPDRLYELVAVVVHIGgGPNHGH---YVSIVKSHGGWlLFDDET 272
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-342 |
4.84e-26 |
|
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: 109.40 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREaLFSLGPEELglfedkdkpdakvriiplqlqrlFAQLLLLDQEaastadltdsF 121
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSETPKEL-----------------------FSQVCRKAPQ----------F 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 122 gwtsnEEMRQHDVQELNRILFSALETslvgtsghdLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAV----KNVSG 197
Cdd:cd02667 47 -----KGYQQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRsdeiKSECS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 198 LEDALWNMYVEEEVFDcDNLYHCGTCDrlvKAAKSAKLRKLPPFLTVSLLRF----NFDFVKCERYKEtscytFPLRINL 273
Cdd:cd02667 113 IESCLKQFTEVEILEG-NNKFACENCT---KAKKQYLISKLPPVLVIHLKRFqqprSANLRKVSRHVS-----FPEILDL 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767918667 274 KPFCEQSEL---DDLEYIYDLFSVIIHKGGCYGGHYHVYIKDvdhlgnwQFQEEKSKPDVNLKDLQSEEEID 342
Cdd:cd02667 184 APFCDPKCNsseDKSSVLYRLYGVVEHSGTMRSGHYVAYVKV-------RPPQQRLSDLTKSKPAADEAGPG 248
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
130-312 |
1.11e-25 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 106.60 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 130 RQHDVQELNRILFSALetslvgtsgHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG------LEDALw 203
Cdd:cd02674 21 DQQDAQEFLLFLLDGL---------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGdapkvtLEDCL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 204 NMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvkCERYKETSCYTFPLRI-NLKPFCEQSEL 282
Cdd:cd02674 91 RLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPLNDlDLTPYVDTRSF 168
|
170 180 190
....*....|....*....|....*....|
gi 767918667 283 DDLeYIYDLFSVIIHKGGCYGGHYHVYIKD 312
Cdd:cd02674 169 TGP-FKYDLYAVVNHYGSLNGGHYTAYCKN 197
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
31-311 |
2.88e-22 |
|
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: 99.58 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 31 PPAPREFTNL---SGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeeLGLFEDKDkpdakvriiplQLQRLFAQLL-L 106
Cdd:cd02671 12 ATSCEKRENLlpfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVE-----------QLQSSFLLNPeK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 107 LDQEAASTA---------DLTDSFgwtsnEEMRQHDVQE-LNRILFSAletslvgtsgHDLIYRLYHGTIVNQIVCKECK 176
Cdd:cd02671 77 YNDELANQAprrllnalrEVNPMY-----EGYLQHDAQEvLQCILGNI----------QELVEKDFQGQLVLRTRCLECE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 177 NVSERQEDFLDLTVAV----------------KNVSGLEDALWNM--YVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKL 238
Cdd:cd02671 142 TFTERREDFQDISVPVqeselskseesseispDPKTEMKTLKWAIsqFASVERIVGEDKYFCENCHHYTEAERSLLFDKL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918667 239 PPFLTVSLLRFNFDFVKCERY----KETSCYTFPLRINLKPFCEQSELDDleyiYDLFSVIIHKGGCYG-GHYHVYIK 311
Cdd:cd02671 222 PEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLEEWSTKPKNDV----YRLFAVVMHSGATISsGHYTAYVR 295
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
42-342 |
2.29e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 84.08 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHF-TPEFREALFSLgPEELGLFED---KDKPDAKVRiiplQLQRLFAQLLLLDQEaastadl 117
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALyLPKLDELLDDL-SKELKVLKNvirKPEPDLNQE----EALKLFTALWSSKEH------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 118 tdSFGWTSNEEmRQHDVQELNRILFSALETSLVGTsghdlIYRLYHGTIVNqivckeckNVSERQEDFLDLTVAVKNVSG 197
Cdd:COG5533 69 --KVGWIPPMG-SQEDAHELLGKLLDELKLDLVNS-----FTIRIFKTTKD--------KKKTSTGDWFDIIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 198 LEDalwnmyveEEVFDC--DNLYHCGTCDRLVKAAKSAKLR------------KLPPFLTVSLLRFNFDFVKCERYKETS 263
Cdd:COG5533 133 VNN--------LKTLQEfiDNMEELVDDETGVKAKENEELEvqakqeyevsfvKLPKILTIQLKRFANLGGNQKIDTEVD 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918667 264 cytFPLRINLKPfcEQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHlgnWqfqEEKSKPDVNLKdlqSEEEID 342
Cdd:COG5533 205 ---EKFELPVKH--DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGK---W---EKANDSDVTPV---SEEEAI 269
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-325 |
7.83e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 82.76 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeELGLFEDKDKPDAKVRIiplQLQRLfAQLLLLDQEAASTADLTDSF 121
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL---ENKFPSDVVDPANDLNC---QLIKL-ADGLLSGRYSKPASLKSEND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 122 GWT--------------SNEE---MRQHDVQELNRILFSALETSLVGTSGHDLIyRLYHGTIVNQIVCKECKNV--SERQ 182
Cdd:cd02658 74 PYQvgikpsmfkaligkGHPEfstMRQQDALEFLLHLIDKLDRESFKNLGLNPN-DLFKFMIEDRLECLSCKKVkyTSEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 183 EDFLDLTV-------------AVKNVSgLEDALwNMYVEEEVFDcdnlYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRF 249
Cdd:cd02658 153 SEILSLPVpkdeatekeegelVYEPVP-LEDCL-KAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 250 nfDFVKCERYKETSCYTF-PLRINLKPfceqselddleyiYDLFSVIIHKG-GCYGGHYHVYI-KDVDHLGNW-QFQEEK 325
Cdd:cd02658 227 --QLLENWVPKKLDVPIDvPEELGPGK-------------YELIAFISHKGtSVHSGHYVAHIkKEIDGEGKWvLFNDEK 291
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-325 |
9.78e-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: 82.38 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELG--------------LFEDKDK-PDAKVRIIPLQ-LQRLFAQll 105
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGanqssdnltnalrdLFDTMDKkQEPVPPIEFLQlLRMAFPQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 106 lldqeaastadltdsFGWTSNEEM-RQHDVQELNRILFSALETSLVGTSGH-DLIYRLYHGTIVNQIVCKECKNVSE--- 180
Cdd:cd02657 79 ---------------FAEKQNQGGyAQQDAEECWSQLLSVLSQKLPGAGSKgSFIDQLFGIELETKMKCTESPDEEEvst 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 181 RQEDFLDLTVAVK-NVSGLEDALwNMYVEEEVfdcdnLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFnfdFVKCE-- 257
Cdd:cd02657 144 ESEYKLQCHISITtEVNYLQDGL-KKGLEEEI-----EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRF---FWKRDiq 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767918667 258 -RYKETSCYTFPLRINLKPFCEQSELddleyiYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW-QFQEEK 325
Cdd:cd02657 215 kKAKILRKVKFPFELDLYELCTPSGY------YELVAVITHQGrSADSGHYVAWVRR-KNDGKWiKFDDDK 278
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-309 |
3.26e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 76.64 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALfslgpeelglfedkdkpdakvriiplqlqrlfaqlllldqeaastadltdsf 121
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------------------------------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 122 gwtsNEEMRQHDVQELNRILFSALETSLVGtsghdliyrLYHGTIVNQIVCKECKNVSE-RQEDFLDLTVAVKNVSG--- 197
Cdd:cd02662 29 ----EEFLEQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSgsg 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 198 -LEDALWNMYVEEEvfDCDNLyhcgTCDRlvkaaKSAKLRKLPPFLTVSLLRFNFDfVKCERYKETSCYTFPLRINlkpf 276
Cdd:cd02662 96 tTLEHCLDDFLSTE--IIDDY----KCDR-----CQTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP---- 159
|
250 260 270
....*....|....*....|....*....|...
gi 767918667 277 ceqselddlEYIYDLFSVIIHKGGCYGGHYHVY 309
Cdd:cd02662 160 ---------KVLYRLRAVVVHYGSHSSGHYVCY 183
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
41-311 |
7.46e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 67.68 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 41 SGIRNQGGTCYLNSLLQTLHFTPEFRE-ALFSLGPE---------ELG-LF--EDKDKPdakvriIPLQ---LQRLF--- 101
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATEclkehcllcELGfLFdmLEKAKG------KNCQasnFLRALssi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 102 ---AQLLLLDQEAASTADLTDSfgwtsneemrqHDVQELNRILFS-----ALETSLVGTSGHDLIYRLYHGTIVNQIVCK 173
Cdd:pfam13423 75 peaSALGLLDEDRETNSAISLS-----------SLIQSFNRFLLDqlsseENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 174 ECKNVSERQEDF--LDLTVAVKNVSGLEDALWNMYVE--EEVFDCDNLY--HCGTCDRLVKAAKSAKLRKLPPFLTVSLL 247
Cdd:pfam13423 144 NCGHESVRESSThvLDLIYPRKPSSNNKKPPNQTFSSilKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767918667 248 RFNFDfvkcERYKETSCYTFPLRINLKPFcEQSELDDLEYIYDLFSVIIH-KGGCYGGHYHVYIK 311
Cdd:pfam13423 224 LTNEE----WRQLWKTPGWLPPEIGLTLS-DDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVK 283
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-312 |
2.67e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 66.75 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGLFEDKDK----PDAKVRIIPL--------QLQRLFAQLLLLDQ 109
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTerriGGREVSRSELqrsnqfvyELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 110 EAAS-TADLTdsfgwtsNEEMRQHDVQELNRILFSALETSLVGTSGH-------------DLIYRLYHGTIVNQIVcKEC 175
Cdd:cd02666 83 RSVTpSKELA-------YLALRQQDVTECIDNVLFQLEVALEPISNAfagpdteddkeqsDLIKRLFSGKTKQQLV-PES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 176 KN----VSERQEDFLDLTVAV------KNVSG----LEDALwnmyveEEVFDcdnlyhcgtCDRLVKA-AKSAKLRKLPP 240
Cdd:cd02666 155 MGnqpsVRTKTERFLSLLVDVgkkgreIVVLLepkdLYDAL------DRYFD---------YDSLTKLpQRSQVQAQLAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 241 FLTVSLLRFNF--------DFVKCERYKETSCYTFPL----RINLKPFCEQSELDDL-EYIYDLFSVIIHKGGCYGGHYH 307
Cdd:cd02666 220 PLQRELISMDRyelpssidDIDELIREAIQSESSLVRqaqnELAELKHEIEKQFDDLkSYGYRLHAVFIHRGEASSGHYW 299
|
....*
gi 767918667 308 VYIKD 312
Cdd:cd02666 300 VYIKD 304
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
198-325 |
1.72e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 59.13 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 198 LEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDfvKCERYKETSCYTFPL-RINLKPF 276
Cdd:COG5560 677 LQDCL-NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPIdDLDLSGV 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767918667 277 ceQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHLGNWQFQEEK 325
Cdd:COG5560 754 --EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSR 800
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
131-338 |
1.83e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 47.55 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 131 QHDVQELNRILFSALE---------TSLVGTSGHDLiYRLYHGTIVNQIVCKECKnvSERQEDFLDLTVAVKNVSGLEDA 201
Cdd:cd02665 22 QQDVSEFTHLLLDWLEdafqaaaeaISPGEKSKNPM-VQLFYGTFLTEGVLEGKP--FCNCETFGQYPLQVNGYGNLHEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 202 LWNMYVEEEVfdcDNLyhcgTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETScyTFPLRINLKPfceqse 281
Cdd:cd02665 99 LEAAMFEGEV---ELL----PSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKL--EFPQIIQQVP------ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767918667 282 lddleyiYDLFSVIIHKGGCYGGHYHVYIKDvDHLGNWQFQEEKSKPDVNLKDLQSE 338
Cdd:cd02665 164 -------YELHAVLVHEGQANAGHYWAYIYK-QSRQEWEKYNDISVTESSWEEVERD 212
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
40-190 |
1.84e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 46.03 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 40 LSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELglfEDKDKPDAkvriIPLQLQRLFAQLL--LLDQEAASTADL 117
Cdd:COG5560 265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEES---INEENPLG----MHGSVASAYADLIkqLYDGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918667 118 TDSFGWTSNEEM----RQHDVQE------------LNRILFSALETSLVGTSGHD--------------------LIYRL 161
Cdd:COG5560 338 GFKKTIGSFNEEfsgyDQQDSQEfiaflldglhedLNRIIKKPYTSKPDLSPGDDvvvkkkakecwwehlkrndsIITDL 417
|
170 180
....*....|....*....|....*....
gi 767918667 162 YHGTIVNQIVCKECKNVSERQEDFLDLTV 190
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
|
|
| |
