|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-346 |
5.61e-149 |
|
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: 429.39 E-value: 5.61e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 50 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKP----SQILTSA 125
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfssnLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 126 FHKHQQEDAHEFLMFTLETMHESCLQVHRQSE---PTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 203 AQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2739433 283 PTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYV 346
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
51-345 |
9.22e-96 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 293.96 E-value: 9.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCK--MCAMEAHVtQSLLHSHSGDVMKPSQILTSA--- 125
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInlLCALRDLF-KALQKNSKSSSVSPKMFKKSLgkl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 126 ---FHKHQQEDAHEFLMFTLETMHESCLQVHrqsepTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:pfam00443 80 npdFSGYKQQDAQEFLLFLLDGLHEDLNGNH-----STENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 203 AQSV------NQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFS--AFMGNKLDRKVSYPEFL 274
Cdd:pfam00443 155 DSAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2739433 275 DLKPYLSQPTGGPLP----YALYAVLVHEGaTCHSGHYFSYVKA-RHGAWYKMDDTKVTSCDV-TSVLNENAYVLFY 345
Cdd:pfam00443 235 DLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEeTAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
52-346 |
1.72e-69 |
|
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: 223.90 E-value: 1.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHtppladymlsqeysqtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhQQ 131
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS----------------------------------------------------------EQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 132 EDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRF----LDVPLDISSAQSVN 207
Cdd:cd02257 23 QDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPElflsLPLPVKGLPQVSLE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 208 QALWDTEKSEELRGENAYYCGRCRqKMPASKTLHIHSAPKVLLLVLKRFS---AFMGNKLDRKVSYPEFLDLKPYLSQPT 284
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2739433 285 ------GGPLPYALYAVLVHEGATCHSGHYFSYVKAR-HGAWYKMDDTKVTSCDVTSVL-----NENAYVLFYV 346
Cdd:cd02257 182 kdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKDPsDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-346 |
9.51e-68 |
|
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: 221.86 E-value: 9.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTC--CSPEGCKMCAMeAHVTQSLLHSHSGDVMKPSQILTSAFHK- 128
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAM-DEIFQEFYYSGDRSPYGPINLLYLSWKHs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 129 -----HQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDI--- 200
Cdd:cd02660 81 rnlagYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIpnk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 201 --------SSAQSVNQALW---DTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRF---SAFMGNKLDR 266
Cdd:cd02660 161 stpswalgESGVSGTPTLSdclDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKIDT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 267 KVSYPEFLDLKPYLSQPTGGPLP---------YALYAVLVHEGaTCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLN 337
Cdd:cd02660 241 YVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLK 319
|
....*....
gi 2739433 338 ENAYVLFYV 346
Cdd:cd02660 320 SQAYLLFYH 328
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
3.36e-53 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 180.18 E-value: 3.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHtppladymlsqeysqtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhQQ 131
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA----------------------------------------------------------DQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 132 EDAHEFLMFTLETMHesclqvhrqseptsedsSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQ------S 205
Cdd:cd02674 23 QDAQEFLLFLLDGLH-----------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvT 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 206 VNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSA--FMGNKLDRKVSYP-EFLDLKPYL-S 281
Cdd:cd02674 86 LEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFsrGSTRKLTTPVTFPlNDLDLTPYVdT 165
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2739433 282 QPTGGPLPYALYAVLVHEGaTCHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNENAYVLFY 345
Cdd:cd02674 166 RSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
51-350 |
6.98e-53 |
|
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: 182.84 E-value: 6.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 51 CGLQNTGNSCYLNAALQCLTHTPPL--ADYMLSQEYSQTCCSPEGCKM--CAMEAHVTQSLLHSHSGDVMKPS---QILT 123
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDDDNKSVPLALqrLFLFLQLSESPVKTTELTDKTRSfgwDSLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 124 SafhkHQQEDAHEFLMFTLETMHESclqvhrqSEPTSEDSSpIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSA 203
Cdd:cd02659 83 T----FEQHDVQEFFRVLFDKLEEK-------LKGTGQEGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 204 QSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSaF-----MGNKLDRKVSYPEFLDLKP 278
Cdd:cd02659 151 KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE-FdfetmMRIKINDRFEFPLELDMEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 279 YLSQ----PTGGPLP-------YALYAVLVHEGaTCHSGHYFSYVKAR-HGAWYKMDDTKVTSCDVTSVLNE-------- 338
Cdd:cd02659 230 YTEKglakKEGDSEKkdsesyiYELHGVLVHSG-DAHGGHYYSYIKDRdDGKWYKFNDDVVTPFDPNDAEEEcfggeetq 308
|
330 340
....*....|....*....|....*.
gi 2739433 339 --------------NAYVLFYVQQTD 350
Cdd:cd02659 309 ktydsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
4.68e-47 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 166.33 E-value: 4.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHT---PPLADYMlsqeYSQTCCSPegckmcameahvtqsllhshSGDVMKPSQILT----- 123
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEnllTCLKDLF----ESISEQKK--------------------RTGVISPKKFITrlkre 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 124 -SAFHKHQQEDAHEFLMFTLETMHEsCLQVHRQSEPTSEDSSP----------IHDIFGGLWRSQIKCLHCQGTSDTYDR 192
Cdd:cd02663 57 nELFDNYMHQDAHEFLNFLLNEIAE-ILDAERKAEKANRKLNNnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDET 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 193 FLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFsAFMGN-----KLDRK 267
Cdd:cd02663 136 FLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF-KYDEQlnryiKLFYR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 268 VSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKArHGAWYKMDDTKVTSCDVTSVLN--------EN 339
Cdd:cd02663 215 VVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENAVEEffgdspnqAT 293
|
....*.
gi 2739433 340 AYVLFY 345
Cdd:cd02663 294 AYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
2.41e-44 |
|
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: 158.32 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqeysqtccspegckmcameahvtqsllhshsgdvmKPSQILTSAFHKH-- 129
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-----------------------------------TPKELFSQVCRKApq 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 130 ----QQEDAHEFLMFTLETMhesclqvhrqseptsedSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPL----DIS 201
Cdd:cd02667 46 fkgyQQQDSHELLRYLLDGL-----------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 202 SAQSVNQALWDTEKSEELRGENAYYCGRCRQkmpASKTLHIHSAPKVLLLVLKRFSA-FMGN--KLDRKVSYPEFLDLKP 278
Cdd:cd02667 109 SECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQpRSANlrKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 279 YLSQPTGGP-----LPYALYAVLVHEGaTCHSGHYFSYVKARH----------------------GAWYKMDDTKVTSCD 331
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 2739433 332 VTSVLNENAYVLFY 345
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.26e-39 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 146.87 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQT-CCSPEGCKMCAMEAHvtqsLLHSHSGDVMKPSQILTSA----F 126
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLgDSQSVMKKLQLLQAH----LMHTQRRAEAPPDYFLEASrppwF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 127 HKHQQEDAHEFLMFTLETMHesclqvhrqseptsedsSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSV 206
Cdd:cd02664 77 TPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 207 nqaLWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFS----AFMGNKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02664 140 ---LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkTHVREKIMDNVSINEVLSLPVRVES 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 283 PTGGP-------------------LPYALYAVLVHEGATCHSGHYFSYvkARHGA-----------------------WY 320
Cdd:cd02664 217 KSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTY--ARDQTdadstgqecpepkdaeendesknWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 2739433 321 KMDDTKVTSCDVTSVLN-------ENAYVLFY 345
Cdd:cd02664 295 LFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-327 |
2.14e-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: 132.54 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSqtcCSPEGCKMCAMEAHVTQS----------LLHSHSGDVMKPSQ- 120
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNST---EDAELKNMPPDKPHEPQTiidqlqlifaQLQFGNRSVVDPSGf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 121 ILTSAFHKHQQEDAHEFLMFTLETMhESCLQVHRQSEPtsedSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDI 200
Cdd:cd02668 78 VKALGLDTGQQQDAQEFSKLFLSLL-EAKLSKSKNPDL----KNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 201 SSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSaFMGNKLDRK-----VSYPEFLD 275
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FDRKTGAKKklnasISFPEILD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2739433 276 LKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVK-ARHGAWYKMDDTKV 327
Cdd:cd02668 232 MGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.61e-32 |
|
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: 126.67 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCC--SPEGCKMCAMeAHVTQSLLhshSGDVMKPSQ--------- 120
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLL---SGRYSKPASlksendpyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 121 --ILTSAF-----HKHQ------QEDAHEFLMFTLETMHESCLQVHrQSEPTsedsspihDIFGGLWRSQIKCLHCQ--G 185
Cdd:cd02658 77 vgIKPSMFkaligKGHPefstmrQQDALEFLLHLIDKLDRESFKNL-GLNPN--------DLFKFMIEDRLECLSCKkvK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 186 TSDTYDRFLDVPLDISSAQSVNQalwDTEKSEELRGE-----------NAYYCGRCRQKMPASKTLHIHSAPKVLLLVLK 254
Cdd:cd02658 148 YTSELSEILSLPVPKDEATEKEE---GELVYEPVPLEdclkayfapetIEDFCSTCKEKTTATKTTGFKTFPDYLVINMK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 255 RFSAFMG---NKLDRKVSYPEFLdlkpylsqptgGPLPYALYAVLVHEGATCHSGHYFSYVK---ARHGAWYKMDDTKVT 328
Cdd:cd02658 225 RFQLLENwvpKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
|
330
....*....|....*..
gi 2739433 329 SCDVTSVLNENAYVLFY 345
Cdd:cd02658 294 ASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
52-373 |
5.34e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.04 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTpplaDYMLSQEYSQTCCSPEGCKMCAMEA----HVTQSLLHSHSGDVMKPSQILTSAFH 127
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHPRGRDSVALALqrlfYNLQTGEEPVDTTELTRSFGWDSDDS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 128 KHQQeDAHEF---LMFTLEtmhesclqvhrQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQ 204
Cdd:COG5077 271 FMQH-DIQEFnrvLQDNLE-----------KSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 205 SVNQALWDTEKSEELRGENAYYCgrcrQK---MPASKTLHIHSAPKVLLLVLKRFSA-F---MGNKLDRKVSYPEFLDLK 277
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNA----EKhglQDAKKGVIFESLPPVLHLQLKRFEYdFerdMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 278 PYLS----QPTGGPLPYALYAVLVHEGaTCHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNEN------------- 339
Cdd:COG5077 415 PFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEENfggdhpykdkird 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2739433 340 ---------AYVLFYVQQTDLKQV-----SIDMPEgRVHEVLDPEYQL 373
Cdd:COG5077 494 hsgikrfmsAYMLVYLRKSMLDDLlnpvaAVDIPP-HVEEVLSEEIDK 540
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.42e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 103.95 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQeysqtccSPEGCKMCAMEAHVTQSLLH-----SHSGDVMKPSqILTSAF 126
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNY-------NPARRGANQSSDNLTNALRDlfdtmDKKQEPVPPI-EFLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 127 HKH-------------QQEDAHEFLMftletmheSCLQVHRQS-EPTSEDSSPIHDIFGGLWRSQIKC------------ 180
Cdd:cd02657 73 RMAfpqfaekqnqggyAQQDAEECWS--------QLLSVLSQKlPGAGSKGSFIDQLFGIELETKMKCtespdeeevste 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 181 ----LHCQGTSDTYDRFLDVPLDISSAQSVnqalwdtEKSEELRGENAYYcgrcrqkmpaSKTLHIHSAPKVLLLVLKRF 256
Cdd:cd02657 145 seykLQCHISITTEVNYLQDGLKKGLEEEI-------EKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 257 ----SAFMGNKLDRKVSYPEFLDLKPYLSqPTGgplPYALYAVLVHEGATCHSGHYFSYVKARH-GAWYKMDDTKVTSCD 331
Cdd:cd02657 208 fwkrDIQKKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVT 283
|
330 340
....*....|....*....|.
gi 2739433 332 VTSVLN-------ENAYVLFY 345
Cdd:cd02657 284 EEDILKlsgggdwHIAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
49-345 |
1.81e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 104.20 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 49 PGCGLQNTGNSCYLNAALQCLTHTP-------PLADYMLSQEYSQTCC--SPEgckmcameaHVTQSLLHSHSGDVMKPS 119
Cdd:cd02671 23 PFVGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSSFllNPE---------KYNDELANQAPRRLLNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 120 QILTSAFHKHQQEDAHEFLMFTLETMHESclqvhrqseptsedsspIHDIFGGLWRSQIKCLHCQGTSDTYDRFLD--VP 197
Cdd:cd02671 94 REVNPMYEGYLQHDAQEVLQCILGNIQEL-----------------VEKDFQGQLVLRTRCLECETFTERREDFQDisVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 198 LDISSAQSVNQ--------------ALWDTEK---SEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAfM 260
Cdd:cd02671 157 VQESELSKSEEsseispdpktemktLKWAISQfasVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAA-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 261 GNKLD-----RKVSYPEFLDLKPYLSQPTGGPLP--YALYAVLVHEGATCHSGHYFSYVKarhgaWYKMDDTKV------ 327
Cdd:cd02671 236 GSEFDcygglSKVNTPLLTPLKLSLEEWSTKPKNdvYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvteek 310
|
330 340
....*....|....*....|.
gi 2739433 328 ---TSCDVTSVLNENAYVLFY 345
Cdd:cd02671 311 dflEALSPNTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
214-349 |
8.48e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 102.65 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 214 EKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMG--NKLDRKVSYPEF-LDLKPYLSQPTGGPLPY 290
Cdd:COG5560 685 SKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPIDdLDLSGVEYMVDDPRLIY 764
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 291 ALYAVLVHEGATcHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYVQQT 349
Cdd:COG5560 765 DLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
51-200 |
2.44e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 98.03 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHS-HSGDV--MKPSQI------ 121
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQlYDGNLhaFTPSGFkktigs 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 122 LTSAFHKHQQEDAHEFLMFTLETMHE--SCLQVHRQSE-PTSEDSSPIH---------------------DIFGGLWRSQ 177
Cdd:COG5560 346 FNEEFSGYDQQDSQEFIAFLLDGLHEdlNRIIKKPYTSkPDLSPGDDVVvkkkakecwwehlkrndsiitDLFQGMYKST 425
|
170 180
....*....|....*....|...
gi 2739433 178 IKCLHCQGTSDTYDRFLDVPLDI 200
Cdd:COG5560 426 LTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.26e-18 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 85.11 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMlsQEYSQtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhqQ 131
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL--EEFLE--------------------------------------------Q 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 132 EDAHEFLMFTLETMHESClqvhrqseptsedSSPIHdifgGLWRSQIKCLHCQGTSD-----TYDRFLDVPLDIS-SAQS 205
Cdd:cd02662 35 QDAHELFQVLLETLEQLL-------------KFPFD----GLLASRIVCLQCGESSKvryesFTMLSLPVPNQSSgSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 206 VNQALWDTEKSEELRGenaYYCGRCRQKmpasktlhIHSAPKVLLLVLKRFSaFMGN----KLDRKVSYPEFldLKPYLs 281
Cdd:cd02662 98 LEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSV-FDGRgtstKNSCKVSFPER--LPKVL- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 282 qptggplpYALYAVLVHEGaTCHSGHYFSYVKAR---------------------HGAWYKMDDTKVTSCDVTSVLNE-N 339
Cdd:cd02662 163 --------YRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQkS 233
|
....*.
gi 2739433 340 AYVLFY 345
Cdd:cd02662 234 AYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
52-347 |
1.76e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 86.01 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLT-HTPPLADYM---------LSQEYSQtccSPEGCKMCAMEAHVTQSLlhshSGDVMKPSQI 121
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTALW----SSKEHKVGWI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 122 LTSAfhkhQQEDAHEFLMFTLETMHESCL-QVHRQSEPTSED--SSPIHDIFgglwrsQIKCLHCQGTSD----TYDRFL 194
Cdd:COG5533 74 PPMG----SQEDAHELLGKLLDELKLDLVnSFTIRIFKTTKDkkKTSTGDWF------DIIIELPDQTWVnnlkTLQEFI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 195 D-VPLDISSAQSVNqalWDTEKSEELRGENAYYcgrcrqkmpasktLHIHSAPKVLLLVLKRFSAFMGN-KLDRKVSYPE 272
Cdd:COG5533 144 DnMEELVDDETGVK---AKENEELEVQAKQEYE-------------VSFVKLPKILTIQLKRFANLGGNqKIDTEVDEKF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 273 FLDLKPylsQPTGGPLP---YALYAVLVHEGaTCHSGHYFSYVKaRHGAWYKMDDTKVTSCDVTSVLN---ENAYVLFYV 346
Cdd:COG5533 208 ELPVKH---DQILNIVKetyYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYE 282
|
.
gi 2739433 347 Q 347
Cdd:COG5533 283 R 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
20-330 |
7.27e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 76.97 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 20 QQLHQDEAQVVVELTANDKPSLswecpqgPGC-GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQ---TCCSPEGCK 95
Cdd:cd02669 95 EQISDLDRDPKLSRDLDGKPYL-------PGFvGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYEnikDRKSELVKR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 96 MC----------AMEAHVTQ----SLLHSHSGdvmKPSQILtsafhkhQQEDAHEFLMFTLETMHeSCLQVHRQSeptse 161
Cdd:cd02669 168 LSelirkiwnprNFKGHVSPhellQAVSKVSK---KKFSIT-------EQSDPVEFLSWLLNTLH-KDLGGSKKP----- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 162 DSSPIHDIFGGLWR--------------SQIKCLHCQGTSDTYD-RFLDVPLDI------SSAQSVNQ----ALWD---- 212
Cdd:cd02669 232 NSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVsPFLLLTLDLpppplfKDGNEENIipqvPLKQllkk 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 213 -TEKSEELRGENayycgrcrqkmpaSKTLHIHSAPKVLLLVLKRFS--AFMGNKLDRKVSYP-EFLDLKPYLSQPTGGPL 288
Cdd:cd02669 312 yDGKTETELKDS-------------LKRYLISRLPKYLIFHIKRFSknNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSLN 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2739433 289 P---YALYAVLVHEGATCHSGHYFSYVkaRHGA---WYKMDDTKVTSC 330
Cdd:cd02669 379 LstkYNLVANIVHEGTPQEDGTWRVQL--RHKStnkWFEIQDLNVKEV 424
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
53-345 |
1.96e-13 |
|
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: 70.25 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 53 LQNTGNSCYLNAALQCLthtppladymlsqeysqtccspegckmcameahvtqsllhSHSGDVMKpsqiltsAFHKHQQE 132
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL----------------------------------------SSIGKINT-------EFDNDDQQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 133 DAHEFLMFTLETMhESCLQVHRQSEPTSEDS----SPIHDIFGGLWRSQIkCLHCQGTSDTYDRFLDVPLDISSAQSVNQ 208
Cdd:cd02673 35 DAHEFLLTLLEAI-DDIMQVNRTNVPPSNIEikrlNPLEAFKYTIESSYV-CIGCSFEENVSDVGNFLDVSMIDNKLDID 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 209 ALWDTEKSEELRGENAyyCGRCRQKMPASKTlHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFldlKPYLSQPTGgpl 288
Cdd:cd02673 113 ELLISNFKTWSPIEKD--CSSCKCESAISSE-RIMTFPECLSINLKRYKLRIATSDYLKKNEEIM---KKYCGTDAK--- 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2739433 289 pYALYAVLVHEGATCHSGHYFSYVKARHG--AWYKMDDT---KVTSCDVTSVLNENAYVLFY 345
Cdd:cd02673 184 -YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDeirPVSKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-346 |
3.36e-13 |
|
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: 70.98 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPE--------GCKMCAMEAHVTQS-----------LLHSHS 112
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterrigGREVSRSELQRSNQfvyelrslfndLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 113 GDVmKPSQILT-SAFhkhQQEDAHEFL---MFTLE--TMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQI---KCLHC 183
Cdd:cd02666 83 RSV-TPSKELAyLAL---RQQDVTECIdnvLFQLEvaLEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLvpeSMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 184 QGTSDTYDRFLDVPLDI----------SSAQSVNQAL----------------WDTEKSEELRGENAYYCGRCRQKMPAS 237
Cdd:cd02666 159 PSVRTKTERFLSLLVDVgkkgreivvlLEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRELISMDRYELPSSID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 238 KTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYpEFLDLKPYlsqptggplPYALYAVLVHEGATCHsGHYFSYVKARH- 316
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAELKHEIEK-QFDDLKSY---------GYRLHAVFIHRGEASS-GHYWVYIKDFEe 307
|
330 340 350
....*....|....*....|....*....|....*.
gi 2739433 317 GAWYKMDDTKVTSCDVTSVLNE------NAYVLFYV 346
Cdd:cd02666 308 NVWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
52-327 |
5.22e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 66.91 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 52 GLQNTGNSCYLNAALQCLTHTPPLadYMLSQEYSQTCCSPEGCKMCAM----------------------------EAHv 103
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPL--RNLALSHLATECLKEHCLLCELgflfdmlekakgkncqasnflralssipEAS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 104 TQSLL--HSHSGDVMKPSQILTSaFHKhqqedaheFLmftLETMHESCLqvhRQSEPTSEDSSPIHDIFGGLWRSQIKCL 181
Cdd:pfam13423 79 ALGLLdeDRETNSAISLSSLIQS-FNR--------FL---LDQLSSEEN---STPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 182 HCQGTSDTYDRFLDVPLDISS-AQSVNQALWDTEKSEELRG----ENAY--YCGRCRQKMPASKTLHIHSAPKVLLLVLK 254
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYPRkPSSNNKKPPNQTFSSILKSslerETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 255 RFSAFMGNkLDRKVSY--PEFldlKPYLSQPTGGPLP---YALYAVLVHEGATCHSGHYFSYVK--------ARHGAWYK 321
Cdd:pfam13423 224 LTNEEWRQ-LWKTPGWlpPEI---GLTLSDDLQGDNEivkYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQWYL 299
|
....*.
gi 2739433 322 MDDTKV 327
Cdd:pfam13423 300 FNDFLV 305
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
130-346 |
1.06e-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: 49.86 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 130 QQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGlwRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQA 209
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYG--TFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 210 LWDTEKSEELRGENAYYCGRCRQKMPASKTlhihsaPKVLLLVLKRFS--AFMGNKLDRKVSYPEFLDlkpylsqptggP 287
Cdd:cd02665 99 LEAAMFEGEVELLPSDHSVKSGQERWFTEL------PPVLTFELSRFEfnQGRPEKIHDKLEFPQIIQ-----------Q 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2739433 288 LPYALYAVLVHEGATcHSGHYFSYVKARH-GAWYKMDDTKVTSCDVTSV--------LNENAYVLFYV 346
Cdd:cd02665 162 VPYELHAVLVHEGQA-NAGHYWAYIYKQSrQEWEKYNDISVTESSWEEVerdsfgggRNPSAYCLMYI 228
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-345 |
1.79e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 46.37 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 245 APKVLLLVLKRFSAFMGN--KLDRKVSYPEFLDLKPYL----------------------SQPTGGPLPYALYAVLVHEG 300
Cdd:cd02670 98 APSCLIICLKRYGKTEGKaqKMFKKILIPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCHRG 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2739433 301 ATCHSGHYFSYVK------------ARHGAWYK---MDDTKVTSCDV---TSVLNENAYVLFY 345
Cdd:cd02670 178 TSLETGHYVAFVRygsysltetdneAYNAQWVFfddMADRDGVSNGFnipAARLLEDPYMLFY 240
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
51-345 |
4.93e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 45.20 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQeysQTCCSPEGCKMCAMeahvtqsllhshsgdvmkpsQILTSAFHKhq 130
Cdd:cd02672 16 AGLENHITNSYCNSLLQLLYFIPPFRNFTAII---LVACPKESCLLCEL--------------------GYLFSTLIQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 131 qedahEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDifgglwrsqikclhcqgtsdtydrfLDVPLDISSAQSVNQAL 210
Cdd:cd02672 71 -----NFTRFLLETISQDQLGTPFSCGTSRNSVSLLYT-------------------------LSLPLGSTKTSKESTFL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433 211 WDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLK-RFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLP 289
Cdd:cd02672 121 QLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLViNLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDK 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2739433 290 ------------YALYAVLVHEGATCHSGHYFSYV-----KARHGAWYKMDDTKVTSCDvtsvlnENAYVLFY 345
Cdd:cd02672 201 lvknrgqesiykYELVGYVCEINDSSRGQHNVVFVikvneESTHGRWYLFNDFLVTPVS------ELAYILLY 267
|
|
| |
