|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
84-380 |
1.66e-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: 435.94 E-value: 1.66e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 84 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKP----SQILTSA 159
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfssnLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 160 FHKHQQEDAHEFLMFTLETMHESCLQVHRQSDPTP---QDTSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISS 236
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDpssQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 237 AQSVNQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSAFTGNKLDRKVSYPEFLDLKPYLSE 316
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379698859 317 PTGGPLPYALYAVLVHDGATSNSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYV 380
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
85-379 |
8.49e-99 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 301.28 E-value: 8.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 85 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCK--MCAMEAHVtQSLLHSHSGDVMKPSQILTSA--- 159
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInlLCALRDLF-KALQKNSKSSSVSPKMFKKSLgkl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 160 ---FHKHQQEDAHEFLMFTLETMHESCLQVHRQSDPtpqdtSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISS 236
Cdd:pfam00443 80 npdFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENE-----SLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 237 AQSV------NQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFS--AFTGNKLDRKVSYPEFL 308
Cdd:pfam00443 155 DSAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379698859 309 DLKPYLSEPTGGPLP----YALYAVLVHDGaTSNSGHYFCCVKA-GHGKWYKMDDTKVTRCDV-TSVLNENAYVLFY 379
Cdd:pfam00443 235 DLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEeTAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-380 |
5.34e-71 |
|
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: 230.34 E-value: 5.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTC--CSPEGCKMCAMeAHVTQSLLHSHSGDVMKPSQILTSAFHK- 162
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAM-DEIFQEFYYSGDRSPYGPINLLYLSWKHs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 163 -----HQQEDAHEFLMFTLETMHESCLQVHRQSDPTPQDTSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISSA 237
Cdd:cd02660 81 rnlagYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 238 QSVNQALWDTGK--------------SEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRF---SAFTGNKLDR 300
Cdd:cd02660 161 STPSWALGESGVsgtptlsdcldrftRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKIDT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 301 KVSYPEFLDLKPYLSEPTGGPLP---------YALYAVLVHDGaTSNSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLN 371
Cdd:cd02660 241 YVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLK 319
|
....*....
gi 379698859 372 ENAYVLFYV 380
Cdd:cd02660 320 SQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
86-380 |
7.75e-68 |
|
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: 219.28 E-value: 7.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHtppladymlsqehsqtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhQQ 165
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS----------------------------------------------------------EQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 166 EDAHEFLMFTLETMHESCLQVHRQSDPTPQDTSPIHDIFGGWWRSQIKCLHCQGTSHTFDPF----LDVPLDISSAQSVN 241
Cdd:cd02257 23 QDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPElflsLPLPVKGLPQVSLE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 242 QALWDTGKSEELLGENAYYCGRCRqKMPASKTLHVHIAPKVLLLVLKRFS---AFTGNKLDRKVSYPEFLDLKPYLSEPT 318
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379698859 319 ------GGPLPYALYAVLVHDGATSNSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVL-----NENAYVLFYV 380
Cdd:cd02257 182 kdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
1.30e-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: 178.64 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHtppladymlsqehsqtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhQQ 165
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA----------------------------------------------------------DQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 166 EDAHEFLMFTLETMHesclqvhrqsdptpqdtSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISSAQ------S 239
Cdd:cd02674 23 QDAQEFLLFLLDGLH-----------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvT 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 240 VNQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSA--FTGNKLDRKVSYP-EFLDLKPYL-S 315
Cdd:cd02674 86 LEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFsrGSTRKLTTPVTFPlNDLDLTPYVdT 165
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379698859 316 EPTGGPLPYALYAVLVHDGaTSNSGHYFCCVKAGH-GKWYKMDDTKVTRCDVTSVLNENAYVLFY 379
Cdd:cd02674 166 RSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
85-384 |
4.51e-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: 169.75 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 85 CGLQNTGNSCYLNAALQCLTHTPPL--ADYMLSQEHSQTCCSPEGCKM--CAMEAHVTQSLLHSHSGDVMKPS---QILT 157
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDDDNKSVPLALqrLFLFLQLSESPVKTTELTDKTRSfgwDSLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 158 SafhkHQQEDAHEFLMFTLETMHESclqvhrqSDPTPQDTSpIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISSA 237
Cdd:cd02659 83 T----FEQHDVQEFFRVLFDKLEEK-------LKGTGQEGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 238 QSVNQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSaF-----TGNKLDRKVSYPEFLDLKP 312
Cdd:cd02659 151 KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE-FdfetmMRIKINDRFEFPLELDMEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 313 YLSE----PTGGPLP-------YALYAVLVHDGaTSNSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVLNE-------- 372
Cdd:cd02659 230 YTEKglakKEGDSEKkdsesyiYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetq 308
|
330 340
....*....|....*....|....*.
gi 379698859 373 --------------NAYVLFYVQQTD 384
Cdd:cd02659 309 ktydsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
4.70e-45 |
|
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: 160.55 E-value: 4.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHT---PPLADYMlsqeHSQTCCSPegckmcameahvtqsllhshSGDVMKPSQILT----- 157
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEnllTCLKDLF----ESISEQKK--------------------RTGVISPKKFITrlkre 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 158 -SAFHKHQQEDAHEFLMFTLETMHEsCLQVHRQSDPTPQDTSP----------IHDIFGGWWRSQIKCLHCQGTSHTFDP 226
Cdd:cd02663 57 nELFDNYMHQDAHEFLNFLLNEIAE-ILDAERKAEKANRKLNNnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDET 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 227 FLDVPLDISSAQSVNQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFsAFTGN-----KLDRK 301
Cdd:cd02663 136 FLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF-KYDEQlnryiKLFYR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 302 VSYPEFLDLKPYLSEPTGGPLPYALYAVLVHDGATSNSGHYFCCVKAgHGKWYKMDDTKVTRCDVTSVLN--------EN 373
Cdd:cd02663 215 VVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENAVEEffgdspnqAT 293
|
....*.
gi 379698859 374 AYVLFY 379
Cdd:cd02663 294 AYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
1.57e-40 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 147.92 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqehsqtccspegckmcameahvtqsllhshsgdvmKPSQILTSAFHKH-- 163
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-----------------------------------TPKELFSQVCRKApq 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 164 ----QQEDAHEFLMFTLETMhesclqvhrqsdptpqdTSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPL----DIS 235
Cdd:cd02667 46 fkgyQQQDSHELLRYLLDGL-----------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 236 SAQSVNQALWDTGKSEELLGENAYYCGRCRQkmpASKTLHVHIAPKVLLLVLKRFSA---FTGNKLDRKVSYPEFLDLKP 312
Cdd:cd02667 109 SECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQprsANLRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 313 YLSEPTGGP-----LPYALYAVLVHDGaTSNSGHYFCCVKAGH----------------------GKWYKMDDTKVTRCD 365
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 379698859 366 VTSVLNENAYVLFY 379
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
1.10e-38 |
|
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: 144.17 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLS-QEHSQTCCSPEGCKMCAMEAHvtqsLLHSHSGDVMKPSQILTSA----F 160
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSlNLPRLGDSQSVMKKLQLLQAH----LMHTQRRAEAPPDYFLEASrppwF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 161 HKHQQEDAHEFLMFTLETMHesclqvhrqsdptpqdtSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISSAQSV 240
Cdd:cd02664 77 TPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 241 -NQALwdtgKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFS--AFTGN--KLDRKVSYPEFLDLKPYLS 315
Cdd:cd02664 140 lNYFL----SPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVreKIMDNVSINEVLSLPVRVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 316 ------------EPTGG-------PLPYALYAVLVHDGATSNSGHYFC-------CVKAGH--------------GKWYK 355
Cdd:cd02664 216 skssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTyardqtdADSTGQecpepkdaeendesKNWYL 295
|
330 340 350
....*....|....*....|....*....|.
gi 379698859 356 MDDTKVTRCDVTSVLN-------ENAYVLFY 379
Cdd:cd02664 296 FNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-361 |
1.16e-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: 132.93 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSqtcCSPEGCKMCAMEAHVTQS----------LLHSHSGDVMKPSQ- 154
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNST---EDAELKNMPPDKPHEPQTiidqlqlifaQLQFGNRSVVDPSGf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 155 ILTSAFHKHQQEDAHEFLMFTLETMhESCLQVHRQSDPTpqdtSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDI 234
Cdd:cd02668 78 VKALGLDTGQQQDAQEFSKLFLSLL-EAKLSKSKNPDLK----NIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 235 SSAQSVNQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSaF---TGN--KLDRKVSYPEFLD 309
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkKLNASISFPEILD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 379698859 310 LKPYLSEPTGGPLPYALYAVLVHDGATSNSGHYFCCVKAGH-GKWYKMDDTKV 361
Cdd:cd02668 232 MGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDV 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
1.78e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 123.97 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCC--SPEGCKMCAMeAHVTQSLLhshSGDVMKPSQ--------- 154
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLL---SGRYSKPASlksendpyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 155 --ILTSAF-----HKHQ------QEDAHEFLMFTLETMHESCLQVHrQSDPTpqdtspihDIFGGWWRSQIKCLHCQGTS 221
Cdd:cd02658 77 vgIKPSMFkaligKGHPefstmrQQDALEFLLHLIDKLDRESFKNL-GLNPN--------DLFKFMIEDRLECLSCKKVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 222 HTFDP--FLDVPLDISSA------------QSVNQALWDTGKSEELlgenAYYCGRCRQKMPASKTLHVHIAPKVLLLVL 287
Cdd:cd02658 148 YTSELseILSLPVPKDEAtekeegelvyepVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 288 KRFSA---FTGNKLDRKVSYPEFLdlkpylseptgGPLPYALYAVLVHDGATSNSGHYFCCVK---AGHGKWYKMDDTKV 361
Cdd:cd02658 224 KRFQLlenWVPKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKV 292
|
330
....*....|....*...
gi 379698859 362 TRCDVTSVLNENAYVLFY 379
Cdd:cd02658 293 VASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
4.15e-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 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: 105.49 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQehsqtccSPEGCKMCAMEAHVTQSLLH-----SHSGDVMKPSqILTSAF 160
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNY-------NPARRGANQSSDNLTNALRDlfdtmDKKQEPVPPI-EFLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 161 HKH-------------QQEDAHEFLMftletmheSCLQVHRQS-DPTPQDTSPIHDIFGGWWRSQIKCLHCQG-TSHTFD 225
Cdd:cd02657 73 RMAfpqfaekqnqggyAQQDAEECWS--------QLLSVLSQKlPGAGSKGSFIDQLFGIELETKMKCTESPDeEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 226 PFLDVPLDISSAQSVN-------QALWDTG-KSEELLGENAYYcgrcrqkmpaSKTLHVHIAPKVLLLVLKRF----SAF 293
Cdd:cd02657 145 SEYKLQCHISITTEVNylqdglkKGLEEEIeKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRFfwkrDIQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 294 TGNKLDRKVSYPEFLDLKPYLSePTGgplPYALYAVLVHDGATSNSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVLN- 371
Cdd:cd02657 215 KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDILKl 290
|
330
....*....|....
gi 379698859 372 ------ENAYVLFY 379
Cdd:cd02657 291 sgggdwHIAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
86-407 |
6.56e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 109.57 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLAD--YMLSQEHSQTCCS-PEGCKMCAMEAHVTQsllHSHSGDVMKPSQILTSAFHK 162
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSvALALQRLFYNLQTGE---EPVDTTELTRSFGWDSDDSF 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 163 HQQeDAHEF---LMFTLEtmhesclqvhRQSDPTPQDTSpIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISSAQS 239
Cdd:COG5077 272 MQH-DIQEFnrvLQDNLE----------KSMRGTVVENA-LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 240 VNQALWDTGKSEELLGENAYYCgrcrQK---MPASKTLHVHIAPKVLLLVLKRFSA--FTGN--KLDRKVSYPEFLDLKP 312
Cdd:COG5077 340 LQESFRRYIQVETLDGDNRYNA----EKhglQDAKKGVIFESLPPVLHLQLKRFEYdfERDMmvKINDRYEFPLEIDLLP 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 313 YLSEPT----GGPLPYALYAVLVHDGATSNsGHYFCCVKAG-HGKWYKMDDTKVTRCDVTSVLNEN-------------- 373
Cdd:COG5077 416 FLDRDAdkseNSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEENfggdhpykdkirdh 494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 379698859 374 --------AYVLFYVQQTDLKQV-----SIDMPEgRVHEVLDPKYQL 407
Cdd:COG5077 495 sgikrfmsAYMLVYLRKSMLDDLlnpvaAVDIPP-HVEEVLSEEIDK 540
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
83-379 |
2.11e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 101.12 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 83 PGCGLQNTGNSCYLNAALQCLTHTP-------PLADYMLSQEHSQTCC--SPEgckmcameaHVTQSLLHSHSGDVMKPS 153
Cdd:cd02671 23 PFVGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSSFllNPE---------KYNDELANQAPRRLLNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 154 QILTSAFHKHQQEDAHEFLMFTLETMHESclqvhrqsdptpqdtspIHDIFGGWWRSQIKCLHCQGTSHTFDPFLD--VP 231
Cdd:cd02671 94 REVNPMYEGYLQHDAQEVLQCILGNIQEL-----------------VEKDFQGQLVLRTRCLECETFTERREDFQDisVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 232 LDISSAQSVNQ--------------ALWDTGK---SEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSAfT 294
Cdd:cd02671 157 VQESELSKSEEsseispdpktemktLKWAISQfasVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAA-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 295 GNKLD-----RKVSYPEFLDLKPYLSEPTGGPLP--YALYAVLVHDGATSNSGHYFCCVkaghgKWYKMDDTKV---TRC 364
Cdd:cd02671 236 GSEFDcygglSKVNTPLLTPLKLSLEEWSTKPKNdvYRLFAVVMHSGATISSGHYTAYV-----RWLLFDDSEVkvtEEK 310
|
330 340
....*....|....*....|.
gi 379698859 365 DVTSVLNENA------YVLFY 379
Cdd:cd02671 311 DFLEALSPNTsststpYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
14-234 |
7.51e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 99.96 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 14 ENLPSAPLEDSSKF----FEEVFGDMVVALSFPEADPALSSPDAPELHQDEAQVVEELTTNGKHSLSWESPQgpgCGLQN 89
Cdd:COG5560 194 PEIMGLRLGLDSFFrryrVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAGT---CGLRN 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 90 TGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHS-HSGDV--MKPSQI------LTSAF 160
Cdd:COG5560 271 LGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQlYDGNLhaFTPSGFkktigsFNEEF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 161 HKHQQEDAHEFLMFTLETMHESCLQVHRQ---SDPTPQDTSPIH---------------------DIFGGWWRSQIKCLH 216
Cdd:COG5560 351 SGYDQQDSQEFIAFLLDGLHEDLNRIIKKpytSKPDLSPGDDVVvkkkakecwwehlkrndsiitDLFQGMYKSTLTCPG 430
|
250
....*....|....*...
gi 379698859 217 CQGTSHTFDPFLDVPLDI 234
Cdd:COG5560 431 CGSVSITFDPFMDLTLPL 448
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
249-383 |
1.62e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 98.80 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 249 KSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSAFTG--NKLDRKVSYPEF-LDLKPYLSEPTGGPLPYA 325
Cdd:COG5560 686 KPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPIDdLDLSGVEYMVDDPRLIYD 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 379698859 326 LYAVLVHDGATSNsGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYVQQT 383
Cdd:COG5560 766 LYAVDNHYGGLSG-GHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-379 |
5.90e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 86.27 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMlsqehsqtccspegckmcameahvtQSLLhshsgdvmkpsqiltsafhkhQQ 165
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-------------------------EEFL---------------------EQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 166 EDAHEFLMFTLETMHESClqvhrqsdptpqdTSPIHDIFGgwwrSQIKCLHCQGTSH-TFDPF----LDVPLDIS-SAQS 239
Cdd:cd02662 35 QDAHELFQVLLETLEQLL-------------KFPFDGLLA----SRIVCLQCGESSKvRYESFtmlsLPVPNQSSgSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 240 VNQALWDTGKSEELLGenaYYCGRCrqkmpasKTLHVHiAPKVLLLVLKRFSaFTGN----KLDRKVSYPEFldLKPYLs 315
Cdd:cd02662 98 LEHCLDDFLSTEIIDD---YKCDRC-------QTVIVR-LPQILCIHLSRSV-FDGRgtstKNSCKVSFPER--LPKVL- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 316 eptggplpYALYAVLVHDGaTSNSGHYFC---------------------CVKAGHGKWYKMDDTKVTRCDVTSVLNE-N 373
Cdd:cd02662 163 --------YRLRAVVVHYG-SHSSGHYVCyrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQkS 233
|
....*.
gi 379698859 374 AYVLFY 379
Cdd:cd02662 234 AYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
86-381 |
1.06e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 83.31 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLT-HTPPLADYM---------LSQEHSQtccSPEGCKMCAMEAHVTQSLlhshSGDVMKPSQI 155
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTALW----SSKEHKVGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 156 LTSAfhkhQQEDAHEFLMFTLETMHESCL-QVHRQSDPTPQD-----TSPIHDIFGGwwRSQIKCLHcqgTSHTFDPFLD 229
Cdd:COG5533 74 PPMG----SQEDAHELLGKLLDELKLDLVnSFTIRIFKTTKDkkktsTGDWFDIIIE--LPDQTWVN---NLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 230 -VPLDISSAQSVNqalWDTGKSEELLGENAYYcgrcrqkMPASKTlhvhiaPKVLLLVLKRFSAFTGN-KLDRKVSYPEF 307
Cdd:COG5533 145 nMEELVDDETGVK---AKENEELEVQAKQEYE-------VSFVKL------PKILTIQLKRFANLGGNqKIDTEVDEKFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 308 LDLKPylsEPTGGPLP---YALYAVLVHDGaTSNSGHYFCCVKAGhGKWYKMDDTKVTRCDVTSVLN---ENAYVLFYVQ 381
Cdd:COG5533 209 LPVKH---DQILNIVKetyYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
83-379 |
2.51e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 81.21 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 83 PGC-GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQ---TCCSPEG------------CKmcAMEAHVT-QSLLH-- 143
Cdd:cd02669 117 PGFvGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYEnikDRKSELVkrlselirkiwnPR--NFKGHVSpHELLQav 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 144 -SHSGdvmKPSQILtsafhkhQQEDAHEFLMFTLETMHeSCLQVHRQSDptpqdTSPIHDIFGGWWR------------- 209
Cdd:cd02669 195 sKVSK---KKFSIT-------EQSDPVEFLSWLLNTLH-KDLGGSKKPN-----SSIIHDCFQGKVQietqkikphaeee 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 210 -SQIKCLHCQGTSHTFD-PFLDVPLDI------SSAQSVNQ----ALWD-----TGKSEELLGENayycgrcrqkmpaSK 272
Cdd:cd02669 259 gSKDKFFKDSRVKKTSVsPFLLLTLDLpppplfKDGNEENIipqvPLKQllkkyDGKTETELKDS-------------LK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 273 TLHVHIAPKVLLLVLKRFSAFTGNKlDRK---VSYP-EFLDLKPYLSEPTGGPLP---YALYAVLVHDGATSNSGHYFCC 345
Cdd:cd02669 326 RYLISRLPKYLIFHIKRFSKNNFFK-EKNptiVNFPiKNLDLSDYVHFDKPSLNLstkYNLVANIVHEGTPQEDGTWRVQ 404
|
330 340 350
....*....|....*....|....*....|....*...
gi 379698859 346 V-KAGHGKWYKMDDTKVTrcDVTS---VLNEnAYVLFY 379
Cdd:cd02669 405 LrHKSTNKWFEIQDLNVK--EVLPqliFLSE-SYIQIW 439
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
86-361 |
7.71e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 69.22 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLadYMLSQEHSQTCCSPEGCKMCAM----------------------------EAHv 137
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPL--RNLALSHLATECLKEHCLLCELgflfdmlekakgkncqasnflralssipEAS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 138 TQSLL--HSHSGDVMKPSQILTSaFHKhqqedaheFLmftLETMHESCLqvhRQSDPTPQDTSPIHDIFGGWWRSQIKCL 215
Cdd:pfam13423 79 ALGLLdeDRETNSAISLSSLIQS-FNR--------FL---LDQLSSEEN---STPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 216 HC------QGTSHTFDpfLDVPldiSSAQSVNQALWDTGKSEEL----LGENAY--YCGRCRQKMPASKTLHVHIAPKVL 283
Cdd:pfam13423 144 NCghesvrESSTHVLD--LIYP---RKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 284 LLVLKRFSAFTGNkLDRKVSY--PEFldlKPYLSEPTGGPLP---YALYAVLVHDGATSNSGHYFCCVKAGH-------- 350
Cdd:pfam13423 219 SLNAALTNEEWRQ-LWKTPGWlpPEI---GLTLSDDLQGDNEivkYELRGVVVHIGDSGTSGHLVSFVKVADseledpte 294
|
330
....*....|.
gi 379698859 351 GKWYKMDDTKV 361
Cdd:pfam13423 295 SQWYLFNDFLV 305
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
87-379 |
6.21e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 62.93 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 87 LQNTGNSCYLNAALQCLthtppladymlsqehsqtccspegckmcameahvtqsllhSHSGDVMKpsqiltsAFHKHQQE 166
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL----------------------------------------SSIGKINT-------EFDNDDQQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 167 DAHEFLMFTLETMhESCLQVHRQSDPTPQDT----SPIHDIfggwwRSQIK-CLHCQGTSH-----TFDPFLDV---PLD 233
Cdd:cd02673 35 DAHEFLLTLLEAI-DDIMQVNRTNVPPSNIEikrlNPLEAF-----KYTIEsSYVCIGCSFeenvsDVGNFLDVsmiDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 234 ISSAQSVNQALWDTGKSEELlgenayyCGRCRQKMPASKTLHVHIaPKVLLLVLKRFSAFTGNKLDRKVSYPEFldlKPY 313
Cdd:cd02673 109 LDIDELLISNFKTWSPIEKD-------CSSCKCESAISSERIMTF-PECLSINLKRYKLRIATSDYLKKNEEIM---KKY 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379698859 314 LSEPTGgplpYALYAVLVHDGATSNSGHYFCCVKAGHG--KWYKMDDT---KVTRCDVTSVLNENAYVLFY 379
Cdd:cd02673 178 CGTDAK----YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDeirPVSKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-380 |
1.17e-09 |
|
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: 60.20 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 86 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPE--------GCKMCAMEAHVTQS-----------LLHSHS 146
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterrigGREVSRSELQRSNQfvyelrslfndLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 147 GDVmKPSQILT-SAFhkhQQEDAHEFL---MFTLE--TMHESCLQVHRQSDPTPQDTSPIHDIFGGWWRSQIKCLHCQGT 220
Cdd:cd02666 83 RSV-TPSKELAyLAL---RQQDVTECIdnvLFQLEvaLEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVPESMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 221 SHTFDP---FLDVPLDI----------SSAQSVNQAL----------------WDTGKSEELLGENAYYCGRcRQKMPAS 271
Cdd:cd02666 159 PSVRTKterFLSLLVDVgkkgreivvlLEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRELISMDR-YELPSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 272 KTLHVHIAPKVL-LLVLKRFSAFTGNKLDRKVSYpEFLDLKPYlseptggplPYALYAVLVHDGATSnSGHYFCCVKAGH 350
Cdd:cd02666 238 DDIDELIREAIQsESSLVRQAQNELAELKHEIEK-QFDDLKSY---------GYRLHAVFIHRGEAS-SGHYWVYIKDFE 306
|
330 340 350
....*....|....*....|....*....|....*..
gi 379698859 351 GK-WYKMDDTKVTRCDVTSVLNE------NAYVLFYV 380
Cdd:cd02666 307 ENvWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-380 |
4.02e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 47.94 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 164 QQEDAHEFLMFTLETMHESC-LQVHRQSDPTpQDTSPIHDIFGGwwRSQIKCLHCQGTSHTFDPFLDVPLDISSAQSVNQ 242
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqAAAEAISPGE-KSKNPMVQLFYG--TFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 243 ALWDT---GKSEELLGENAYYCGRCRQKMPAsktlhvhiaPKVLLLVLKRFS--AFTGNKLDRKVSYPEFLDlkpylsep 317
Cdd:cd02665 98 CLEAAmfeGEVELLPSDHSVKSGQERWFTEL---------PPVLTFELSRFEfnQGRPEKIHDKLEFPQIIQ-------- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379698859 318 tggPLPYALYAVLVHDGaTSNSGHYFCCV-KAGHGKWYKMDDTKVTRCDVTSV--------LNENAYVLFYV 380
Cdd:cd02665 161 ---QVPYELHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVerdsfgggRNPSAYCLMYI 228
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
85-379 |
7.86e-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: 41.34 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 85 CGLQNTGNSCYLNAALQCLTHTPPLADYMLsqeHSQTCCSPEGCKMCAMeahvtqsllhshsgdvmkpsQILTSAFHKhq 164
Cdd:cd02672 16 AGLENHITNSYCNSLLQLLYFIPPFRNFTA---IILVACPKESCLLCEL--------------------GYLFSTLIQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 165 qedahEFLMFTLETMHESCLQVHRQSDPTPQDTSPIHDIfggwwrsqikCLHCQGTSHTFDPFLDVPLDISSAQSVNQAL 244
Cdd:cd02672 71 -----NFTRFLLETISQDQLGTPFSCGTSRNSVSLLYTL----------SLPLGSTKTSKESTFLQLLKRSLDLEKVTKA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 245 WdtgkseellgenayyCGRCRQKMPASKTLHVHIAPKVLLLVLKR-------------FSAFTGNKLDRKVSYPEFLDLK 311
Cdd:cd02672 136 W---------------CDTCCKYQPLEQTTSIRHLPDILLLVLVInlsvtngefddinVVLPSGKVMQNKVSPKAIDHDK 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379698859 312 PYLSEPTGGPLPYALYAVLVHDGATSNSGHYFCCV-----KAGHGKWYKMDDTKVTRCDvtsvlnENAYVLFY 379
Cdd:cd02672 201 LVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVikvneESTHGRWYLFNDFLVTPVS------ELAYILLY 267
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-379 |
2.16e-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: 39.82 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379698859 279 APKVLLLVLKRFSAFTGN--KLDRKVSYPEFLDLKPYL----------------------SEPTGGPLPYALYAVLVHDG 334
Cdd:cd02670 98 APSCLIICLKRYGKTEGKaqKMFKKILIPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCHRG 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379698859 335 ATSNSGHYFCCVKAGHG------------KWYKMDDTKVTRCDV------TSVLNENAYVLFY 379
Cdd:cd02670 178 TSLETGHYVAFVRYGSYsltetdneaynaQWVFFDDMADRDGVSngfnipAARLLEDPYMLFY 240
|
|
| |
