|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
162-467 |
2.82e-151 |
|
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: 442.10 E-value: 2.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 162 GAGLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNpcNCGNEKFCVMQALRDHIELALRSSGYGINIDRFRDNLTYFS 241
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSK--DCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 242 SDFMINHQEDAHEFLQSFLDKLERCCLDPKNQLGSV--SSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEI 319
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVdpSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 320 EDVNTLWKALESFTCVEKLEDQLT--CDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNdgVTMEKIFDHIEFPLELDLSP 397
Cdd:cd02661 159 KGADSLEDALEQFTKPEQLDGENKykCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN--FRGGKINKQISFPETLDLSP 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 398 FMSSNHDPevSTRYHLYAFVEHIGIRATFGHYSSYVRSAPETWHNFDDSKVTRISEERVLSRPAYILFYA 467
Cdd:cd02661 237 YMSQPNDG--PLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
163-466 |
2.26e-76 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 248.51 E-value: 2.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 163 AGLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNPCNCGNEKFCVMQALRDHI-ELALRSSGYGINIDRFRDNLTYFS 241
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 242 SDFMINHQEDAHEFLQSFLDKLERCCLdpknqlGSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEIED 321
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 322 VNTLWKALESFTCVE--------KLEDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTMEKIFDHIEFPLEL 393
Cdd:pfam00443 155 DSAELKTASLQICFLqfskleelDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332008037 394 DLSPFMSSNHDPEVSTR--YHLYAFVEHIGiRATFGHYSSYVRSAPET-WHNFDDSKVTRISEER-VLSRPAYILFY 466
Cdd:pfam00443 235 DLSRYLAEELKPKTNNLqdYRLVAVVVHSG-SLSSGHYIAYIKAYENNrWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
164-466 |
1.17e-66 |
|
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: 220.82 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHtvplidslrsfmygnpcncgnekfcvmqalrdhielalrssgyginidrfrdnltyfssd 243
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 244 fminHQEDAHEFLQSFLDKLERCCLDPKNQlGSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEI---- 319
Cdd:cd02257 21 ----EQQDAHEFLLFLLDKLHEELKKSSKR-TSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkg 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 320 EDVNTLWKALESFTCVEKLEDQlTCDNC--KEKVTKEKQLRFDKLPPVATFHLKRFTNDGV-TMEKIFDHIEFPLELDLS 396
Cdd:cd02257 96 LPQVSLEDCLEKFFKEEILEGD-NCYKCekKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDgTKEKLNTKVSFPLELDLS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 397 PFMSSNH----DPEVSTRYHLYAFVEHIGIRATFGHYSSYVRSAPE-TWHNFDDSKVTRISEERVLSRP-----AYILFY 466
Cdd:cd02257 175 PYLSEGEkdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDgKWYKFNDDKVTEVSEEEVLEFGslsssAYILFY 254
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
6.90e-63 |
|
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: 213.00 E-value: 6.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNPCNCGNEKFCVMQALrDHIELALRSS----GYG-INIdrfrdnlt 238
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCAM-DEIFQEFYYSgdrsPYGpINL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 239 yFSSDFMINH------QEDAHEFLQSFLDKLERCCLDPKNQLGSVSSQDLnIVDNVFGGGLMSTLCCCNCNSVSNTFEPS 312
Cdd:cd02660 73 -LYLSWKHSRnlagysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNC-IIHQTFSGSLQSSVTCQRCGGVSTTVDPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 313 LGWSLEIEDVN---------------TLWKALESFTCVEKLED-QLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFT-N 375
Cdd:cd02660 151 LDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDfAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 376 DGVTMEKIFDHIEFPLELDLSPFMSSNHDPEVST-------RYHLYAFVEHIGIRATfGHYSSYVRSAPETWHNFDDSKV 448
Cdd:cd02660 231 LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSnsldpdyTYDLFAVVVHKGTLDT-GHYTAYCRQGDGQWFKFDDAMI 309
|
330
....*....|....*...
gi 332008037 449 TRISEERVLSRPAYILFY 466
Cdd:cd02660 310 TRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
4.00e-52 |
|
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: 180.56 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCfthtvplidslrsfmygnpcncgnekfcvmqalrdhielalrssgyginidrfrdnltyfssd 243
Cdd:cd02674 1 GLRNLGNTCYMNSILQC--------------------------------------------------------------- 17
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 244 fMINHQEDAHEFLQSFLDKLErccldpknqlgsvssqdlNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEI---- 319
Cdd:cd02674 18 -LSADQQDAQEFLLFLLDGLH------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgs 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 320 --EDVNTLWKALESFTCVEKLE--DQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTMEKIFDHIEFPLE-LD 394
Cdd:cd02674 79 gdAPKVTLEDCLRLFTKEETLDgdNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNdLD 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332008037 395 LSPFMSSNHDPEVsTRYHLYAFVEHIGIRATfGHYSSYVRSA-PETWHNFDDSKVTRISEERVLSRPAYILFY 466
Cdd:cd02674 159 LTPYVDTRSFTGP-FKYDLYAVVNHYGSLNG-GHYTAYCKNNeTNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
5.36e-52 |
|
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: 181.82 E-value: 5.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTvpliDSLRSFMYGNPCNCGNEkFCvmqalRDHIelalrssgyginidRFRDNltyfssd 243
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQT----PALRELLSETPKELFSQ-VC-----RKAP--------------QFKGY------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 244 fminHQEDAHEFLQSFLDKLErccldpknqlgsvssqdlNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSL----EI 319
Cdd:cd02667 50 ----QQQDSHELLRYLLDGLR------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEI 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 320 EDVNTLWKALESFTCVEKLEDQ--LTCDNCKEKVtkeKQLRFDKLPPVATFHLKRFTNDG-VTMEKIFDHIEFPLELDLS 396
Cdd:cd02667 108 KSECSIESCLKQFTEVEILEGNnkFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRsANLRKVSRHVSFPEILDLA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 397 PFMSS--NHDPEV-STRYHLYAFVEHIGiRATFGHYSSYVRSAPE----------------------TWHNFDDSKVTRI 451
Cdd:cd02667 185 PFCDPkcNSSEDKsSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPPqqrlsdltkskpaadeagpgsgQWYYISDSDVREV 263
|
330
....*....|....*
gi 332008037 452 SEERVLSRPAYILFY 466
Cdd:cd02667 264 SLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-469 |
3.81e-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: 173.21 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVPlidsLRSFMYGNPCNCGNE----KFCVMQALRdhIELALRSSGYGINIDRfrdNLTY 239
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPE----FRNAVYSIPPTEDDDdnksVPLALQRLF--LFLQLSESPVKTTELT---DKTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 240 F----SSDFMINHqeDAHEFLQSFLDKLERCcldpknqlgSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGW 315
Cdd:cd02659 75 SfgwdSLNTFEQH--DVQEFFRVLFDKLEEK---------LKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 316 SLEIEDVNTLWKALESFTCVEKLE--DQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTME--KIFDHIEFPL 391
Cdd:cd02659 144 QVAVKGKKNLEESLDAYVQGETLEgdNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMriKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 392 ELDLSPFM---------SSNHDPEVSTRYHLYAFVEHIGIrATFGHYSSYVRSAPET-WHNFDDSKVTRISEERVLS--- 458
Cdd:cd02659 224 ELDMEPYTekglakkegDSEKKDSESYIYELHGVLVHSGD-AHGGHYYSYIKDRDDGkWYKFNDDVVTPFDPNDAEEecf 302
|
330 340 350
....*....|....*....|....*....|
gi 332008037 459 -----------------RP--AYILFYARE 469
Cdd:cd02659 303 ggeetqktydsgprafkRTtnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
5.99e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 134.74 E-value: 5.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQC-FTHTvpLIDSLRSFMYGNPCN------CGNEKFcvMQALRdhielalrssgyginidrfRDN 236
Cdd:cd02663 1 GLENFGNTCYCNSVLQAlYFEN--LLTCLKDLFESISEQkkrtgvISPKKF--ITRLK-------------------REN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 237 LTYFSSDfminhQEDAHEFLQSFLDKLERCCLDPKNQL--------GSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNT 308
Cdd:cd02663 58 ELFDNYM-----HQDAHEFLNFLLNEIAEILDAERKAEkanrklnnNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 309 FEPSLGWSLEIEDVNTLWKALESFTCVEKL--EDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGV--TMEKIF 384
Cdd:cd02663 133 DETFLDLSIDVEQNTSITSCLRQFSATETLcgRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQlnRYIKLF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 385 DHIEFPLELDLspFMSSNHDPEVSTRYHLYAFVEHIGIRATFGHYSSYVRSApETWHNFDDSKVTRISEERVL------- 457
Cdd:cd02663 213 YRVVFPLELRL--FNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKIDENAVEeffgdsp 289
|
330
....*....|
gi 332008037 458 -SRPAYILFY 466
Cdd:cd02663 290 nQATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
3.31e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 133.31 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVPLidslRSFMYGNPCNCGNEKFCVM-------QALRDHIELALRSSGYG----INIDR 232
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEF----RKAVYECNSTEDAELKNMPpdkphepQTIIDQLQLIFAQLQFGnrsvVDPSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 233 FRDNLTYFSSDfminhQEDAHEFLQSFLDKLERCCLDPKNQLGSvssqdlNIVDNVFGGGLMSTLCCCNCNSVSNTFEPS 312
Cdd:cd02668 77 FVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPDLK------NIVQDLFRGEYSYVTQCSKCGRESSLPSKF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 313 LGWSLEIEDVNTLWKALESFTCVEKL--EDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTM--EKIFDHIE 388
Cdd:cd02668 146 YELELQLKGHKTLEECIDEFLKEEQLtgDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGakKKLNASIS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 389 FPLELDLSPFMsSNHDPEVSTrYHLYAFVEHIGIRATFGHYSSYVR-SAPETWHNFDDSKV------------------- 448
Cdd:cd02668 226 FPEILDMGEYL-AESDEGSYV-YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVeempgkplklgnsedpakp 303
|
330 340
....*....|....*....|
gi 332008037 449 --TRISEERVLSRPAYILFY 466
Cdd:cd02668 304 rkSEIKKGTHSSRTAYMLVY 323
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
4.43e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 112.42 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQC-FTHTVP--LIDSLRSFMYGNPCNCGNEKFCVMQALRDhielALRSSGY-------------- 226
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVlFSIPSFqwRYDDLENKFPSDVVDPANDLNCQLIKLAD----GLLSGRYskpaslksendpyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 227 -GINIDRFRDNLTYFSSDFMINHQEDAHEFLQSFLDKLERccldpknQLGSVSSQDLNivdNVFGGGLMSTLCCCNCNSV 305
Cdd:cd02658 77 vGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDR-------ESFKNLGLNPN---DLFKFMIEDRLECLSCKKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 306 SNTFEPSLGWSLEIEDVN--------------TLWKALESFTCVEKLEDqlTCDNCKEKVTKEKQLRFDKLPPVATFHLK 371
Cdd:cd02658 147 KYTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIED--FCSTCKEKTTATKTTGFKTFPDYLVINMK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 372 RFT--NDGVtmekifdhiefPLELDLSPFMSSNHDPEvstRYHLYAFVEHIGIRATFGHYSSYVR---SAPETWHNFDDS 446
Cdd:cd02658 225 RFQllENWV-----------PKKLDVPIDVPEELGPG---KYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDE 290
|
330 340
....*....|....*....|
gi 332008037 447 KVTRISEERVLSRPAYILFY 466
Cdd:cd02658 291 KVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-467 |
8.56e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 111.91 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 163 AGLYNSGNTCFIASVLQC------FTHTVPLIDSLRSFMYGNPCNC--GNEKFcvmqalrdHIELALRSSgyginiDRFR 234
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVlyfcpgFKHGLKHLVSLISSVEQLQSSFllNPEKY--------NDELANQAP------RRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 235 DNLTYFSSDFMINHQEDAHEFLQSFLDKLErccldpknqlgsvssqdlNIVDNVFGGGLMSTLCCCNCNSVSNTFE---- 310
Cdd:cd02671 91 NALREVNPMYEGYLQHDAQEVLQCILGNIQ------------------ELVEKDFQGQLVLRTRCLECETFTERREdfqd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 311 ----------PSLGWSLEIE-----DVNTLWKALESFTCVEKL--EDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRF 373
Cdd:cd02671 153 isvpvqeselSKSEESSEISpdpktEMKTLKWAISQFASVERIvgEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 374 TNDGVT------MEKIFDHIEFPLELDLSPFMSSNHDPEvstrYHLYAFVEHIGIRATFGHYSSYVRsapetWHNFDDSK 447
Cdd:cd02671 233 AANGSEfdcyggLSKVNTPLLTPLKLSLEEWSTKPKNDV----YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSE 303
|
330 340
....*....|....*....|....*....
gi 332008037 448 V---------TRISEERVLSRPAYILFYA 467
Cdd:cd02671 304 VkvteekdflEALSPNTSSTSTPYLLFYK 332
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
7.43e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 106.04 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVpliDSLRSFMYGNPCNCGNEKFCVMQALRDHIELALRSSGYGINIDRF-RDNL-TYFS 241
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAK---DFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFlEASRpPWFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 242 SDFminhQEDAHEFLQSFLDKLErccldpknqlgsvssqdlNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEIED 321
Cdd:cd02664 78 PGS----QQDCSEYLRYLLDRLH------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 322 VNTLwkaLESFTCVEKL--EDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTM--EKIFDHIEFPLELDL-- 395
Cdd:cd02664 136 VQDL---LNYFLSPEKLtgDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHvrEKIMDNVSINEVLSLpv 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 396 ------------SPFMSSNHDPEVSTR---YHLYAFVEHIGIRATFGHYSSYVRS---------------------APET 439
Cdd:cd02664 213 rveskssespleKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendESKN 292
|
330 340 350
....*....|....*....|....*....|....
gi 332008037 440 WHNFDDSKVTRISEE---RVLSRP----AYILFY 466
Cdd:cd02664 293 WYLFNDSRVTFSSFEsvqNVTSRFpkdtPYILFY 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
164-468 |
1.66e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 104.11 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVPLIDSL---RSFMYGNPCNCGNEKFCVMQalRDHIELALRSSgyginidrFRDNLTYF 240
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELlddLSKELKVLKNVIRKPEPDLN--QEEALKLFTAL--------WSSKEHKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 241 SSDFMINHQEDAHEFLQSFLDKLerccldpKNQLGSVSSQDLNIVDNvfggglmstlcccncNSVSNTFEPslgWSlEIE 320
Cdd:COG5533 71 GWIPPMGSQEDAHELLGKLLDEL-------KLDLVNSFTIRIFKTTK---------------DKKKTSTGD---WF-DII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 321 DVNTLWKALESFTCVEKLEDQLTCDNCKEKVTKEK-------------QLRFDKLPPVATFHLKRFTNDGvTMEKIFDHI 387
Cdd:COG5533 125 IELPDQTWVNNLKTLQEFIDNMEELVDDETGVKAKeneelevqakqeyEVSFVKLPKILTIQLKRFANLG-GNQKIDTEV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 388 EFPLELDLSPFMSSNHDPEvsTRYHLYAFVEHIGIRaTFGHYSSYVRSAPEtWHNFDDSKVTRISEERVL---SRPAYIL 464
Cdd:COG5533 204 DEKFELPVKHDQILNIVKE--TYYDLVGFVLHQGSL-EGGHYIAYVKKGGK-WEKANDSDVTPVSEEEAInekAKNAYLY 279
|
....
gi 332008037 465 FYAR 468
Cdd:COG5533 280 FYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
2.52e-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 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: 103.95 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFtHTVP-LIDSLRSFMYGNPCNCGNEKFCVmQALRDHIElALRSSGYGIN----IDRFRDNLT 238
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL-RSVPeLRDALKNYNPARRGANQSSDNLT-NALRDLFD-TMDKKQEPVPpiefLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 239 YFSSDFMINH--QEDAHEFLQSFLDKLERcCLDPKNQLGSVssqdlniVDNVFGGGLMSTLCCC-NCNSVSNTFEP--SL 313
Cdd:cd02657 78 QFAEKQNQGGyaQQDAEECWSQLLSVLSQ-KLPGAGSKGSF-------IDQLFGIELETKMKCTeSPDEEEVSTESeyKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 314 GWSLEIE-DVNTLwkalesftcVEKLEDQLtcdncKEKVTK-----------EKQLRFDKLPPVATFHLKRF--TNDGVT 379
Cdd:cd02657 150 QCHISITtEVNYL---------QDGLKKGL-----EEEIEKhsptlgrdaiyTKTSRISRLPKYLTVQFVRFfwKRDIQK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 380 MEKIFDHIEFPLELDLSPFMSsnhdpeVSTRYHLYAFVEHIGIRATFGHYSSYVRSA-PETWHNFDDSKVTRISEERVL- 457
Cdd:cd02657 216 KAKILRKVKFPFELDLYELCT------PSGYYELVAVITHQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILk 289
|
330
....*....|....*
gi 332008037 458 ------SRPAYILFY 466
Cdd:cd02657 290 lsgggdWHIAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
164-457 |
7.80e-23 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 104.57 E-value: 7.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFThtvpLIDSLRSFMYGNPCNCGNEkfcvmqalRDHIELALRSSGYGINIDRFRDNLTYFSSD 243
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLF----FIAKFRKDVYGIPTDHPRG--------RDSVALALQRLFYNLQTGEEPVDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 244 FMIN-----HQEDAHEFLQSFLDKLErccldpKNQLGSVSSQDLNivdNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLE 318
Cdd:COG5077 263 FGWDsddsfMQHDIQEFNRVLQDNLE------KSMRGTVVENALN---GIFVGKMKSYIKCVNVNYESARVEDFWDIQLN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 319 IEDVNTLWKALESFTCVEKLEDQlTCDNCKEK--VTKEKQLRFDKLPPVATFHLKRFTNDGVT--MEKIFDHIEFPLELD 394
Cdd:COG5077 334 VKGMKNLQESFRRYIQVETLDGD-NRYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYDFERdmMVKINDRYEFPLEID 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332008037 395 LSPFMSSNHD--PEVSTRYHLYAFVEHIGIRATfGHYSSYVRSAPET-WHNFDDSKVTRISEERVL 457
Cdd:COG5077 413 LLPFLDRDADksENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEKDGrWYKFDDTRVTRATEKEVL 477
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
324-468 |
4.98e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 101.50 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 324 TLWKALESFTCVEKL--EDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTMEKIFDHIEFPL-ELDLSPFMS 400
Cdd:COG5560 676 TLQDCLNEFSKPEQLglSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIdDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332008037 401 SNHDPEVStrYHLYAFVEHIGIRATfGHYSSYVRSAP-ETWHNFDDSKVTRISEERVLSRPAYILFYAR 468
Cdd:COG5560 756 MVDDPRLI--YDLYAVDNHYGGLSG-GHYTAYARNFAnNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
6.66e-21 |
|
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: 92.43 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQcfthtvplidslrsfmygnpcncgnekfcvmqalrdhielALRSsgyginIDRFRDNLTYFSSd 243
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------------------------------------ALAS------LPSLIEYLEEFLE- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 244 fminhQEDAHEFLQSFLDKLERCCLDPknqlgsvssqdlnivdnvFGGGLMSTLCCCNCNSVSN-TFEPSLGWSL----- 317
Cdd:cd02662 34 -----QQDAHELFQVLLETLEQLLKFP------------------FDGLLASRIVCLQCGESSKvRYESFTMLSLpvpnq 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 318 EIEDVNTLWKALESFTCVEKLEDqLTCDNCKEKVTkekqlrfdKLPPVATFHLKRFTNDG-VTMEKIFDHIEFPLELDls 396
Cdd:cd02662 91 SSGSGTTLEHCLDDFLSTEIIDD-YKCDRCQTVIV--------RLPQILCIHLSRSVFDGrGTSTKNSCKVSFPERLP-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 397 pfmssnhdpevSTRYHLYAFVEHIGiRATFGHYSSYVRSAP---------------------ETWHNFDDSKVTRISEER 455
Cdd:cd02662 160 -----------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPLfskdkepgsfvrmregpsstsHPWWRISDTTVKEVSESE 227
|
330
....*....|..
gi 332008037 456 VLSR-PAYILFY 466
Cdd:cd02662 228 VLEQkSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
256-448 |
1.29e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 75.38 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 256 LQSF----LDKLERCCldpkNQLGSVSSQDLNIVDNVFGGGLMSTLCCCNCN------SVSNTFEPSLGWSLEIEDVNTL 325
Cdd:pfam13423 99 IQSFnrflLDQLSSEE----NSTPPNPSPAESPLEQLFGIDAETTIRCSNCGhesvreSSTHVLDLIYPRKPSSNNKKPP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 326 WK----ALESFTCVEKLEdQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTMEKIFDhiEFPLELDLSPFMSS 401
Cdd:pfam13423 175 NQtfssILKSSLERETTT-KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPG--WLPPEIGLTLSDDL 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 332008037 402 NHDPEVsTRYHLYAFVEHIGIRATFGHYSSYVRSAPET--------WHNFDDSKV 448
Cdd:pfam13423 252 QGDNEI-VKYELRGVVVHIGDSGTSGHLVSFVKVADSEledptesqWYLFNDFLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
164-327 |
1.10e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 71.45 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNPCNCGNEKFC---VMQALRDHIELALRSSGYGINIDRFRDNLTYF 240
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMhgsVASAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 241 SSDFMINHQEDAHEFLQSFLD----KLERCCLDPKNQLGSVSSQDLNIVDNV-------------------FGGGLMSTL 297
Cdd:COG5560 347 NEEFSGYDQQDSQEFIAFLLDglheDLNRIIKKPYTSKPDLSPGDDVVVKKKakecwwehlkrndsiitdlFQGMYKSTL 426
|
170 180 190
....*....|....*....|....*....|
gi 332008037 298 CCCNCNSVSNTFEPSLGWSLEIEdVNTLWK 327
Cdd:COG5560 427 TCPGCGSVSITFDPFMDLTLPLP-VSMVWK 455
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
236-466 |
1.65e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 67.58 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 236 NLTYFSS--DFMINHQEDAHEFLQSFLDKLERCcLDPKNQLGSVSSQDLN-IVDNVFGGGLMSTLcccncnSVSNTFE-- 310
Cdd:cd02665 7 NTCWFSAviQSLFSQQQDVSEFTHLLLDWLEDA-FQAAAEAISPGEKSKNpMVQLFYGTFLTEGV------LEGKPFCnc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 311 PSLG-WSLEIEDVNTLWKALESFTcVEKLEDQLTCDNCKeKVTKEKQlrFDKLPPVATFHLKRFTNDGVTMEKIFDHIEF 389
Cdd:cd02665 80 ETFGqYPLQVNGYGNLHECLEAAM-FEGEVELLPSDHSV-KSGQERW--FTELPPVLTFELSRFEFNQGRPEKIHDKLEF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 390 PLELDLSPfmssnhdpevstrYHLYAFVEHIGiRATFGHYSSYVRSAP-ETWHNFDDSKVTRISEERV-------LSRP- 460
Cdd:cd02665 156 PQIIQQVP-------------YELHAVLVHEG-QANAGHYWAYIYKQSrQEWEKYNDISVTESSWEEVerdsfggGRNPs 221
|
....*.
gi 332008037 461 AYILFY 466
Cdd:cd02665 222 AYCLMY 227
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-466 |
1.01e-10 |
|
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: 64.65 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 164 GLYNSGNTCFIASVLQCFTHTVPLIDSLrsFMYGNPCNCGNEKFCVMQ-------------ALRDHI-------ELALRS 223
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFF--LLYENYENIKDRKSELVKrlselirkiwnprNFKGHVsphellqAVSKVS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 224 SGyginidRFRdnltyfssdfmINHQEDAHEFLQSFLDKLerccldpKNQLGSVSSQDLNIVDNVFGGGL---------- 293
Cdd:cd02669 199 KK------KFS-----------ITEQSDPVEFLSWLLNTL-------HKDLGGSKKPNSSIIHDCFQGKVqietqkikph 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 294 ---MSTLCCCNCNSVSNTFEPSLGWSL--------EIEDVN--------TLWKALESFTCVEkledqltcdnCKEKVTKE 354
Cdd:cd02669 255 aeeEGSKDKFFKDSRVKKTSVSPFLLLtldlppppLFKDGNeeniipqvPLKQLLKKYDGKT----------ETELKDSL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 355 KQLRFDKLPPVATFHLKRFT-NDGVTmEKIFDHIEFPLE-LDLSPFMSSN-HDPEVSTRYHLYAFVEHIGIRATFGHYSS 431
Cdd:cd02669 325 KRYLISRLPKYLIFHIKRFSkNNFFK-EKNPTIVNFPIKnLDLSDYVHFDkPSLNLSTKYNLVANIVHEGTPQEDGTWRV 403
|
330 340 350
....*....|....*....|....*....|....*.
gi 332008037 432 YVR-SAPETWHNFDDSKVTRISEERVLSRPAYILFY 466
Cdd:cd02669 404 QLRhKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-466 |
1.32e-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: 50.22 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 242 SDFMINHQEDAHEFLQSFL---DKLERCCLDPKNQLGSVSSQdLNIVdNVFGGGLMSTLCCCNCNSVSNTFepSLGWSLE 318
Cdd:cd02673 26 TEFDNDDQQDAHEFLLTLLeaiDDIMQVNRTNVPPSNIEIKR-LNPL-EAFKYTIESSYVCIGCSFEENVS--DVGNFLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 319 IEDVNTLWKALE----SFTCVEKLEDQLTCDNCKEKVTKEKQLRFdklPPVATFHLKRFTNDGVTMEKIFDHiefplELD 394
Cdd:cd02673 102 VSMIDNKLDIDEllisNFKTWSPIEKDCSSCKCESAISSERIMTF---PECLSINLKRYKLRIATSDYLKKN-----EEI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332008037 395 LSPFMSsnHDPevstRYHLYAFVEHIGIRATFGHYSSYVRS--APETWHNFDDSKVTRISEERVL---SRPAYILFY 466
Cdd:cd02673 174 MKKYCG--TDA----KYSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-466 |
1.87e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 49.83 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 245 MINHQEDAHEFLQSFLDKLERCCLDPKNQLGSVSSQDLNIVDNVfggglmstlcccNCNSVSNTFEPSLGwsleiedvnt 324
Cdd:cd02670 19 MFAEQQDPEEFFNFITDKLLMPLLEPKVDIIHGGKKDQDDDKLV------------NERLLQIPVPDDDD---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 325 lwkalesftcveklEDQLTCDNCKEKVTKEKQlrFDKLPPVATFHLKRFTNDGVTMEKIFDHIEFPLELDLSPFMS---- 400
Cdd:cd02670 77 --------------GGGITLEQCLEQYFNNSV--FAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVAddpr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 401 --SNHDPEVSTRYHLYAF--------------VEHIGIRATFGHYSSYVRSAPET------------WHNFDD------- 445
Cdd:cd02670 141 acSKCQLECRVCYDDKDFsptcgkfklslcsaVCHRGTSLETGHYVAFVRYGSYSltetdneaynaqWVFFDDmadrdgv 220
|
250 260
....*....|....*....|.
gi 332008037 446 SKVTRISEERVLSRPaYILFY 466
Cdd:cd02670 221 SNGFNIPAARLLEDP-YMLFY 240
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
262-467 |
2.34e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 46.74 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 262 KLERCCLdpkNQLG---SVSSQDLN-IVDNVFGGGLMSTLCCCNCNSVSNT--FEPSLGWSLE--IEDVNTLWKaLESFT 333
Cdd:cd02672 52 PKESCLL---CELGylfSTLIQNFTrFLLETISQDQLGTPFSCGTSRNSVSllYTLSLPLGSTktSKESTFLQL-LKRSL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 334 CVEKlEDQLTCDNCKEKVTKEKQLRFDKLPP----VATFHLKRFT---NDGVTMEKIFD----HIEFPLELDLSPfmSSN 402
Cdd:cd02672 128 DLEK-VTKAWCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTNgefDDINVVLPSGKvmqnKVSPKAIDHDKL--VKN 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008037 403 HDPEVSTRYHLYAFVEHIGIRATFGHYSSYVRSAPET-----WHNFDDSKVTRISEErvlsrpAYILFYA 467
Cdd:cd02672 205 RGQESIYKYELVGYVCEINDSSRGQHNVVFVIKVNEEsthgrWYLFNDFLVTPVSEL------AYILLYQ 268
|
|
| |
