|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
4-316 |
6.33e-53 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 176.09 E-value: 6.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 4 VGLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVPGGAEEQRRSVPF--QLLLLLEKMQD-SRKKAVQPTELAYCLQKYN 80
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 81 iPMFV---QHDAAQLYLTVWNLI---KNQITDVDLVARLQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVFDM-HWK 153
Cdd:pfam00443 81 -PDFSgykQQDAQEFLLFLLDGLhedLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDsAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 154 PLKTLEDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSIRNLRAEKVCHSLYFPQNLDLTKL 233
Cdd:pfam00443 160 KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 234 LETKGEPCSAEEQcggHYELFAVIAHVGNADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDVQCTygnhsyrwrETAYL 313
Cdd:pfam00443 240 LAEELKPKTNNLQ---DYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYI 307
|
...
gi 62988294 314 LFY 316
Cdd:pfam00443 308 LFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
5-317 |
1.34e-51 |
|
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: 170.74 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRnvgfakilkritvpggaeEQRRSVPFqLLLLLEKMQDSRKKAVQPTELAYCLqkynipmf 84
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------EQQDAHEF-LLFLLDKLHEELKKSSKRTSDSSSL-------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 85 vqhdaaqlyltvwnliKNQITDvdlvarlqaLYTIRLKESFVCLEC--TSEMSRNSSMLALPLSVFDmhwKPLKTLEDAL 162
Cdd:cd02257 54 ----------------KSLIHD---------LFGGKLESTIVCLECghESVSTEPELFLSLPLPVKG---LPQVSLEDCL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 163 HCFFQPQELSSKDKCFCESCGRKTLWKQvLTLTHLPQTLTIHLMRFSI-RNLRAEKVCHSLYFPQNLDLTKLLETKGEPC 241
Cdd:cd02257 106 EKFFKEEILEGDNCYKCEKKKKQEATKR-LKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYLSEGEKDS 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988294 242 SAEEQCGgHYELFAVIAHVG-NADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDVQCTYGNHSyrwreTAYLLFYV 317
Cdd:cd02257 185 DSDNGSY-KYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSS-----SAYILFYE 255
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2-318 |
1.27e-49 |
|
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: 168.20 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 2 GPVGLHNIGQTCCLNSLIQVLVRNVGFAK-ILKRITVPGGAEEQRRSVPFQLLLLLEKMQDSRKKAVQPTELAYCLQKYN 80
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNaVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 81 IPMFVQHDAAQLYLTVWNLIKNQITDVDLVARLQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVfdmhwKPLKTLED 160
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV-----KGKKNLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 161 ALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFS--IRNLRAEKVCHSLYFPQNLDLTKLLET-- 236
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLELDMEPYTEKgl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 237 KGEPCSAEEQCGGH--YELFAVIAHVGNADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDV--QCTYGNHSYRWRET-- 310
Cdd:cd02659 236 AKKEGDSEKKDSESyiYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeECFGGEETQKTYDSgp 315
|
330
....*....|....*.
gi 62988294 311 --------AYLLFYVK 318
Cdd:cd02659 316 rafkrttnAYMLFYER 331
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
7.25e-42 |
|
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: 147.57 E-value: 7.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVP--GGAEEQRRSVPF-------QLLLLLEKMQDSRKKAVQPTELAYC 75
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTedAELKNMPPDKPHepqtiidQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 76 LQkynIPMFVQHDAAQLYLTVWNLIKN---QITDVDLVARLQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVfdmhw 152
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLLEAklsKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 153 KPLKTLEDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSI--RNLRAEKVCHSLYFPQNLDL 230
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdrKTGAKKKLNASISFPEILDM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 231 TKLLetkgepcsAEEQCGGH-YELFAVIAHVGNADY-GHYCAYIRSSEDGEWFCFNDSNVSwvSWEDVQCTYGN------ 302
Cdd:cd02668 233 GEYL--------AESDEGSYvYELSGVLIHQGVSAYsGHYIAHIKDEQTGEWYKFNDEDVE--EMPGKPLKLGNsedpak 302
|
330 340
....*....|....*....|....
gi 62988294 303 ----------HSYRwreTAYLLFY 316
Cdd:cd02668 303 prkseikkgtHSSR---TAYMLVY 323
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
3.94e-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 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: 126.68 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVPGGAEEQRRSVPFQLLLLLEKMQDSRKKAVQPTELAYCL-------- 76
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLrmafpqfa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 77 QKYNIPMFVQHDAAQLYLTVWNLIKNQITDVDLVAR-LQALYTIRLKESFVCLEC-TSEMSRNSSMLALPLSVFDMHWKp 154
Cdd:cd02657 81 EKQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSfIDQLFGIELETKMKCTESpDEEEVSTESEYKLQCHISITTEV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 155 lKTLEDALHcffqpQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSIR---NLRAeKVCHSLYFPQNLDLT 231
Cdd:cd02657 160 -NYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKrdiQKKA-KILRKVKFPFELDLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 232 klletkgEPCSAEeqcgGHYELFAVIAHVG-NADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDVQCTYGN---HSyrw 307
Cdd:cd02657 233 -------ELCTPS----GYYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGgdwHI--- 298
|
....*....
gi 62988294 308 retAYLLFY 316
Cdd:cd02657 299 ---AYILLY 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-316 |
8.54e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 123.94 E-value: 8.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 86 QHDAAQLYLTVWNLIKNQITDvdlvarlqaLYTIRLKESFVCLEC--TSEMSRNSSMLALPLSVFDMHWKPLkTLEDALH 163
Cdd:cd02674 22 QQDAQEFLLFLLDGLHSIIVD---------LFQGQLKSRLTCLTCgkTSTTFEPFTYLSLPIPSGSGDAPKV-TLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 164 CFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSIRNLRAEKVCHSLYFPqnldLTKLLETKGEPCSA 243
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFP----LNDLDLTPYVDTRS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988294 244 EEQcGGHYELFAVIAHVGNADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDVQctygnhsyrwRETAYLLFY 316
Cdd:cd02674 168 FTG-PFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV----------SSSAYILFY 229
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-317 |
3.56e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 116.22 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 3 PVGLHNIGQTCCLNSLIQVLVRNVGFAKILKRitvpGGAEEQRRSVPFQLLLLLEKM----QDSRKKAVQPTELAYCLQK 78
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLS----REHSKDCCNEGFCMMCALEAHveraLASSGPGSAPRIFSSNLKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 79 YNIPMFV--QHDA---AQLYLTVW-----NLIKNQITDVDLVARLQALYTI---RLKESFVCLECTSEMSRNSSMLALPL 145
Cdd:cd02661 77 ISKHFRIgrQEDAhefLRYLLDAMqkaclDRFKKLKAVDPSSQETTLVQQIfggYLRSQVKCLNCKHVSNTYDPFLDLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 146 SVfdmhwKPLKTLEDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSirNLRAEKVCHSLYFP 225
Cdd:cd02661 157 DI-----KGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINKQISFP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 226 QNLDLTKLL-ETKGEPCSaeeqcgghYELFAVIAHVG-NADYGHYCAYIRSSeDGEWFCFNDSNVSWVSWEDVqctygnh 303
Cdd:cd02661 230 ETLDLSPYMsQPNDGPLK--------YKLYAVLVHSGfSPHSGHYYCYVKSS-NGKWYNMDDSKVSPVSIETV------- 293
|
330
....*....|....
gi 62988294 304 syrWRETAYLLFYV 317
Cdd:cd02661 294 ---LSQKAYILFYI 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
4-316 |
4.57e-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: 111.14 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 4 VGLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVPGGAEEQRRSVpfqlLLLLEKMQDSRKKAVQPTELAYCLQKYNiPM 83
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSS----FLLNPEKYNDELANQAPRRLLNALREVN-PM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 84 F---VQHDAAQLYLTVWNLIKNqitdvdLVARL-QALYTIRLKesfvCLECTSEMSRNSSMLALPLSV-----------F 148
Cdd:cd02671 100 YegyLQHDAQEVLQCILGNIQE------LVEKDfQGQLVLRTR----CLECETFTERREDFQDISVPVqeselskseesS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 149 DMHWKP---LKTLEDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSIRNLRA------EKVc 219
Cdd:cd02671 170 EISPDPkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKV- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 220 hSLYFPQNLDLtklletkgepcSAEEQCGGH----YELFAVIAHVG-NADYGHYCAYIRssedgeWFCFNDSNVSWVSWE 294
Cdd:cd02671 249 -NTPLLTPLKL-----------SLEEWSTKPkndvYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEK 310
|
330 340
....*....|....*....|..
gi 62988294 295 DVQcTYGNHSYRWRETAYLLFY 316
Cdd:cd02671 311 DFL-EALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
2.75e-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: 108.73 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVPGGAEEQrrSVPFQLLLLLEKMQDSRKKAVQPTE--LAYCLQKYNIP 82
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ--SVMKKLQLLQAHLMHTQRRAEAPPDyfLEASRPPWFTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 83 MFvQHDAAQlYLTVwnliknqitdvdLVARLQAL----YTIRLKESFVCLECTSEMSRNSSMLALPLSVfdmhwkplKTL 158
Cdd:cd02664 79 GS-QQDCSE-YLRY------------LLDRLHTLiekmFGGKLSTTIRCLNCNSTSARTERFRDLDLSF--------PSV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 159 EDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSI---RNLRaEKVCHSLYFPQNLDLTKLLE 235
Cdd:cd02664 137 QDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYdqkTHVR-EKIMDNVSINEVLSLPVRVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 236 TKG----------EPCSAEEQCGG--HYELFAVIAHVG-NADYGHYCAYIRSS--------------------EDGEWFC 282
Cdd:cd02664 216 SKSsesplekkeeESGDDGELVTRqvHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpepkdaeendESKNWYL 295
|
330 340 350
....*....|....*....|....*....|....*
gi 62988294 283 FNDSNVSWVSWEDVQctygNHSYRWR-ETAYLLFY 316
Cdd:cd02664 296 FNDSRVTFSSFESVQ----NVTSRFPkDTPYILFY 326
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
6.78e-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: 104.01 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLvrnvgfakilkritvpggaeeqrrsvpFQLLLLLEKMQDSrkkavqPTELAYCLQKYNIPM- 83
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNL---------------------------SQTPALRELLSET------PKELFSQVCRKAPQFk 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 84 -FVQHDAAQLYLTVWNLIknqITDVDLVARLQALYTIrlkesfVCLECTSEMSRNSSMLALPLSVFDMHwKPLKTLEDAL 162
Cdd:cd02667 48 gYQQQDSHELLRYLLDGL---RTFIDSIFGGELTSTI------MCESCGTVSLVYEPFLDLSLPRSDEI-KSECSIESCL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 163 HCFFQPQELSSKDKCFCESCGRKTlwKQVLtLTHLPQTLTIHLMRF---SIRNLRaeKVCHSLYFPQNLDLTKLLETKGE 239
Cdd:cd02667 118 KQFTEVEILEGNNKFACENCTKAK--KQYL-ISKLPPVLVIHLKRFqqpRSANLR--KVSRHVSFPEILDLAPFCDPKCN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 240 PCSAEEQCggHYELFAVIAHVGNADYGHYCAYIRS---------------------SEDGEWFCFNDSNVSWVSWEDVQc 298
Cdd:cd02667 193 SSEDKSSV--LYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVL- 269
|
330
....*....|....*...
gi 62988294 299 tygnhsyrwRETAYLLFY 316
Cdd:cd02667 270 ---------KSEAYLLFY 278
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
2-320 |
1.54e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 107.26 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 2 GPVGLHNIGQTCCLNSLIQVLVRNVGFAKILKRItvPGGAEEQRRSVPFQLLLLLEKMQDSRKkAVQPTELAYCLQKYNI 81
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 82 PMFVQHDAAQLYLTVWNLIKNQITDVDLVARLQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVfdmhwKPLKTLEDA 161
Cdd:COG5077 269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV-----KGMKNLQES 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 162 LHCFFQPQELSSKDKCFCESCGRKTLWKQVLtLTHLPQTLTIHLMRFSIRNLRAE--KVCHSLYFPQNLDLTKLLEtkgE 239
Cdd:COG5077 344 FRRYIQVETLDGDNRYNAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLEIDLLPFLD---R 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 240 PCSAEEQCGGHYELFAVIAHVGNADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDV-QCTYG----------NHSYRWR 308
Cdd:COG5077 420 DADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVlEENFGgdhpykdkirDHSGIKR 499
|
330
....*....|...
gi 62988294 309 ET-AYLLFYVKTE 320
Cdd:COG5077 500 FMsAYMLVYLRKS 512
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-317 |
2.71e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 95.13 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLV-----RNVGFAKILKRitvPGGAEEQRRSVPFQLLLLLEKMQDSRKKAVQ-PTELAYCLQK 78
Cdd:cd02660 2 GLINLGATCFMNVILQALLhnpllRNYFLSDRHSC---TCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYgPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 79 Y--NIPMFVQHDAAQLYLTVWNLIKNQITDVDLVAR--------LQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVF 148
Cdd:cd02660 79 HsrNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANdeshcnciIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 149 DM----------HWKPLKTLEDALHCFFQPQELSSKDKCfCESCGRKTLWKQVLTLTHLPQTLTIHLMRFS-IRNLRAEK 217
Cdd:cd02660 159 NKstpswalgesGVSGTPTLSDCLDRFTRPEKLGDFAYK-CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKTSRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 218 VCHSLYFPQNLDLTKLLET-KGEPCSAEEQCGGH-YELFAVIAHVGNADYGHYCAYIRsSEDGEWFCFNDSNVSWVSWED 295
Cdd:cd02660 238 IDTYVQFPLELNMTPYTSSsIGDTQDSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRVSEEE 316
|
330 340
....*....|....*....|..
gi 62988294 296 VQctygnhsyrwRETAYLLFYV 317
Cdd:cd02660 317 VL----------KSQAYLLFYH 328
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
3.37e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 94.30 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRNVGFAkilkritvpggaeeqrrsvpfQLLLLLEKMQDSRKK--AVQPTELAYCLQKYNiP 82
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT---------------------CLKDLFESISEQKKRtgVISPKKFITRLKREN-E 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 83 MF---VQHDAAQLYltvwNLIKNQITD-VDLVARLQALYTIRLKES-------FV-------------CLECTSEMSRNS 138
Cdd:cd02663 59 LFdnyMHQDAHEFL----NFLLNEIAEiLDAERKAEKANRKLNNNNnaepqptWVheifqgiltnetrCLTCETVSSRDE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 139 SMLALPLSVFdmhwkPLKTLEDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRF--SIRNLRAE 216
Cdd:cd02663 135 TFLDLSIDVE-----QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQLNRYI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 217 KVCHSLYFPQNLDLTKLLETKGEPCSAeeqcgghYELFAVIAHVGN-ADYGHYCAYIRSseDGEWFCFNDSNVSWVSWED 295
Cdd:cd02663 210 KLFYRVVFPLELRLFNTTDDAENPDRL-------YELVAVVVHIGGgPNHGHYVSIVKS--HGGWLLFDDETVEKIDENA 280
|
330 340
....*....|....*....|.
gi 62988294 296 VQCTYGNHsyRWRETAYLLFY 316
Cdd:cd02663 281 VEEFFGDS--PNQATAYVLFY 299
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
157-316 |
3.46e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 94.18 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 157 TLEDALHCFFQPQELSSKDKCFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSIRNLRAEKVCHSLYFP-QNLDLTKLLE 235
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 236 TKGEPcsaeeQCGghYELFAVIAHVGNADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDVQctygnhsyrwRETAYLLF 315
Cdd:COG5560 756 MVDDP-----RLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSV----------TSSAYVLF 818
|
.
gi 62988294 316 Y 316
Cdd:COG5560 819 Y 819
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-317 |
4.05e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 86.39 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 3 PVGLHNIGQTCCLNSLIQVL-----VRN---------VGFAKILKRITVPGGAE----EQRRSVPF--QLLLLLEKMQDS 62
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFftikpLRDlvlnfdeskAELASDYPTERRIGGREvsrsELQRSNQFvyELRSLFNDLIHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 63 RKKAVQPT-ELAYClqkynipMFVQHDAA--------QL--------YLTVWNLIKNQITDVDLVARLqalYTIRLKESF 125
Cdd:cd02666 81 NTRSVTPSkELAYL-------ALRQQDVTecidnvlfQLevalepisNAFAGPDTEDDKEQSDLIKRL---FSGKTKQQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 126 VclECTseMSRNSSM-------LALPLSVFDMHWKPL-----KTLEDALHCFFQPQELSSkdkcfcescGRKTLWKQVlt 193
Cdd:cd02666 151 V--PES--MGNQPSVrtkterfLSLLVDVGKKGREIVvllepKDLYDALDRYFDYDSLTK---------LPQRSQVQA-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 194 ltHLPQTLTIHLMRFSIRNL-----RAEKVCHSLYFPQNLDLTKLLETKGEPCSAEEQCGGH-----YELFAVIAHVGNA 263
Cdd:cd02666 216 --QLAQPLQRELISMDRYELpssidDIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDlksygYRLHAVFIHRGEA 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 62988294 264 DYGHYCAYIRSSEDGEWFCFNDSNVSWV-SWEDVQCTYGNhsyrwRETAYLLFYV 317
Cdd:cd02666 294 SSGHYWVYIKDFEENVWRKYNDETVTVVpASEVFLFTLGN-----TATPYFLVYV 343
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
1.62e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 80.10 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVpggaeeqrrsvpfqlllllekmqdsrkkavqptelayclqkynipmf 84
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 85 vQHDAAQLYLTvwnliknqitdvdLVARLQALYT----IRLKESFVCLECTSEMS-RNSSMLALPLSVFDMHWKPLKTLE 159
Cdd:cd02662 34 -QQDAHELFQV-------------LLETLEQLLKfpfdGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTTLE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 160 DALHCFFQPQELSSKdkcFCESCGrktlwkqvLTLTHLPQTLTIHLMR--FSIRNLRAEKVCHsLYFPqnLDLTKLLetk 237
Cdd:cd02662 100 HCLDDFLSTEIIDDY---KCDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTSTKNSCK-VSFP--ERLPKVL--- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 238 gepcsaeeqcgghYELFAVIAHVGNADYGHYCAY--------------------IRSSEDGEWFCFNDSNVSWVSWEDVQ 297
Cdd:cd02662 163 -------------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVL 229
|
330
....*....|....*....
gi 62988294 298 CTYGnhsyrwretAYLLFY 316
Cdd:cd02662 230 EQKS---------AYMLFY 239
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-316 |
1.90e-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: 81.22 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLV-----------RNVGFAKILKRIT---------VPGGAEEQRRSVPfqllLLLEKMQDSRK 64
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddLENKFPSDVVDPAndlncqlikLADGLLSGRYSKP----ASLKSENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 65 KAVQPTELAYCLQKYNiPMFV---QHDAAQLYLTVWNLIKNQITdVDLVARLQALYTIRLKESFVCLEC--TSEMSRNSS 139
Cdd:cd02658 77 VGIKPSMFKALIGKGH-PEFStmrQQDALEFLLHLIDKLDRESF-KNLGLNPNDLFKFMIEDRLECLSCkkVKYTSELSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 140 MLALPLSVFDMHWKPLK-------TLEDALHCFFQPQELSSkdkcFCESCGRKTLWKQVLTLTHLPQTLTIHLMRFSIR- 211
Cdd:cd02658 155 ILSLPVPKDEATEKEEGelvyepvPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLe 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 212 NLRAEKVCHSLYFPQNLDltklletkgepcsaeeqcGGHYELFAVIAHVGN-ADYGHYCAYIR--SSEDGEWFCFNDSNV 288
Cdd:cd02658 231 NWVPKKLDVPIDVPEELG------------------PGKYELIAFISHKGTsVHSGHYVAHIKkeIDGEGKWVLFNDEKV 292
|
330 340
....*....|....*....|....*...
gi 62988294 289 swvswedVQCTYGNHSyrwRETAYLLFY 316
Cdd:cd02658 293 -------VASQDPPEM---KKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
5-319 |
4.45e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.85 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVRNVgfAKILKRITVPggaeeqrrsvPFQLLLLLEKMQDSRKKAVQPTELA-----YCLQKY 79
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYL--PKLDELLDDL----------SKELKVLKNVIRKPEPDLNQEEALKlftalWSSKEH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 80 NI----PMFVQHDAAQLYLTVWNLIKNQitdvdlvarLQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVFDmhwKPL 155
Cdd:COG5533 69 KVgwipPMGSQEDAHELLGKLLDELKLD---------LVNSFTIRIFKTTKDKKKTSTGDWFDIIIELPDQTWV---NNL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 156 KTLEDALHCF--FQPQELSSKDKcfcESCGRKTLWKQ--VLTLTHLPQTLTIHLMRFSIRNLRAeKVCHSLyfPQNLDLT 231
Cdd:COG5533 137 KTLQEFIDNMeeLVDDETGVKAK---ENEELEVQAKQeyEVSFVKLPKILTIQLKRFANLGGNQ-KIDTEV--DEKFELP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 232 KLLETKGEpcSAEEqcgGHYELFAVIAHVGNADYGHYCAYIRssEDGEWFCFNDSNVSWVSWEDvqctygnhSYRW-RET 310
Cdd:COG5533 211 VKHDQILN--IVKE---TYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEE--------AINEkAKN 275
|
....*....
gi 62988294 311 AYLLFYVKT 319
Cdd:COG5533 276 AYLYFYERI 284
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-317 |
4.98e-14 |
|
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: 70.28 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 5 GLHNIGQTCCLNSLIQVLVrnvgfakilkritvpggaeEQRRSVPFQLLLLLEKMQDSRKKAVQPTELayclqkyniPMF 84
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF-------------------SQQQDVSEFTHLLLDWLEDAFQAAAEAISP---------GEK 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 85 VQHDAAQLYltvwnliknqitdvdlvarlqalYTIRLKESFvcLECTsEMSRNSSMLALPLSVfdmhwKPLKTLEDALHC 164
Cdd:cd02665 53 SKNPMVQLF-----------------------YGTFLTEGV--LEGK-PFCNCETFGQYPLQV-----NGYGNLHECLEA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 165 FFQPQELSSKDKCFCESCGRKTLWkqvltlTHLPQTLTIHLMRFSIRNLRAEKVCHSLYFPQNLdltklletKGEPcsae 244
Cdd:cd02665 102 AMFEGEVELLPSDHSVKSGQERWF------TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII--------QQVP---- 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988294 245 eqcgghYELFAVIAHVGNADYGHYCAYIRSSEDGEWFCFNDSNVSWVSWEDVQC-TYGNHSyrwRETAYLLFYV 317
Cdd:cd02665 164 ------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERdSFGGGR---NPSAYCLMYI 228
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
113-288 |
9.53e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 70.38 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 113 LQALYTIRLKESFVCLECTSEMSRNSSMLALPLSVFdmhWKPLKTLEDALHCFFqPQELSS------KDKCFCESCGRKT 186
Cdd:pfam13423 128 LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYP---RKPSSNNKKPPNQTF-SSILKSsleretTTKAWCEKCKRYQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 187 LWKQVLTLTHLPQTLTIHLMRFSIRNLRAEKVCHslYFPQNLDLTKLLETKGEPCSAEeqcgghYELFAVIAHVGNAD-Y 265
Cdd:pfam13423 204 PLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPG--WLPPEIGLTLSDDLQGDNEIVK------YELRGVVVHIGDSGtS 275
|
170 180 190
....*....|....*....|....*....|
gi 62988294 266 GHYCAYIRSSE-------DGEWFCFNDSNV 288
Cdd:pfam13423 276 GHLVSFVKVADseledptESQWYLFNDFLV 305
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|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
6-316 |
4.96e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 64.86 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 6 LHNIGQTCCLNSLIQVLvrnvgfAKILKRITvpGGAEEQRRSVPFQLLLLLEKMQDsrkkavqptelaycLQKYNIPmfv 85
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL------SSIGKINT--EFDNDDQQDAHEFLLTLLEAIDD--------------IMQVNRT--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 86 qhdaaqlyltvwnlikNQITDVDLVARLQALYTIRLK--ESFVCLECTSEMSRNSSMLALPLSVFDMhwkPLKTLEDALH 163
Cdd:cd02673 57 ----------------NVPPSNIEIKRLNPLEAFKYTieSSYVCIGCSFEENVSDVGNFLDVSMIDN---KLDIDELLIS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 164 CFFQPQELSSK-DKCFCE---SCGRktlwkqvltLTHLPQTLTIHLMRFSIRnlraekVCHSLYFPQNLDLTKLLETKGe 239
Cdd:cd02673 118 NFKTWSPIEKDcSSCKCEsaiSSER---------IMTFPECLSINLKRYKLR------IATSDYLKKNEEIMKKYCGTD- 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988294 240 pcsaeeqcgGHYELFAVIAHVGNADY-GHYCAYIRSSEDG-EWFCFNDSNVSWVSWEDVqctygnhSYRWRETAYLLFY 316
Cdd:cd02673 182 ---------AKYSLVAVICHLGESPYdGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDV-------STNARSSGYLIFY 244
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|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
175-316 |
2.90e-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: 41.73 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 175 DKCFCESCGRKTLWKQVLTLTHLPQTLTIHLmrfsIRNLRAEKVCHSLYFPQnldLTKLLETKGEPCSAEEQC------- 247
Cdd:cd02672 133 TKAWCDTCCKYQPLEQTTSIRHLPDILLLVL----VINLSVTNGEFDDINVV---LPSGKVMQNKVSPKAIDHdklvknr 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988294 248 GGH----YELFAVIAHV-GNADYGHYCAYIR----SSEDGEWFCFNDSNVSWVSwedvqctygnhsyrwrETAYLLFY 316
Cdd:cd02672 206 GQEsiykYELVGYVCEInDSSRGQHNVVFVIkvneESTHGRWYLFNDFLVTPVS----------------ELAYILLY 267
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2-289 |
1.38e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 39.99 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 2 GPVGLHNIGQTCCLNSLIQVLVRNVGFAKILKRITVPGGAEEQRRSVPFQLLLLLEKMQDSR--KKAVQPTELaycLQ-- 77
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRnfKGHVSPHEL---LQav 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 78 ----KYNIPMFVQHDAAQLYLTVWNLIKNQ----------ITDVDLVARLQaLYTIRLK-------ESFVCLECTSEMSR 136
Cdd:cd02669 195 skvsKKKFSITEQSDPVEFLSWLLNTLHKDlggskkpnssIIHDCFQGKVQ-IETQKIKphaeeegSKDKFFKDSRVKKT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 137 NSS---MLAL-----PLSVFDMHWK--PLKTLEDALHCFFQPQELSSKDKcfcescgrktlwKQVLTLTHLPQTLTIHLM 206
Cdd:cd02669 274 SVSpflLLTLdlpppPLFKDGNEENiiPQVPLKQLLKKYDGKTETELKDS------------LKRYLISRLPKYLIFHIK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 207 RFSIRNLRAEKVCHSLYFPQ-NLDLTKLLetkgEPCSAEEQCGGHYELFAVIAHVGN-ADYGHYCAYIRSSEDGEWFCFN 284
Cdd:cd02669 342 RFSKNNFFKEKNPTIVNFPIkNLDLSDYV----HFDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQ 417
|
....*
gi 62988294 285 DSNVS 289
Cdd:cd02669 418 DLNVK 422
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-316 |
2.61e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 38.66 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988294 194 LTHLPQTLTIHLMRFSIRNLRAEKVCHSLYFPQNLDLTKLLETKGEPCSAE-----------EQCG--GHYELF--AVIA 258
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCqlecrvcyddkDFSPtcGKFKLSlcSAVC 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62988294 259 HVGNADY-GHYCAYIRSSEDGEWFCFNDS-NVSWVSWEDVQCTYG-----NHSYRWR-ETAYLLFY 316
Cdd:cd02670 175 HRGTSLEtGHYVAFVRYGSYSLTETDNEAyNAQWVFFDDMADRDGvsngfNIPAARLlEDPYMLFY 240
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