|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
50-341 |
4.20e-40 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 143.35 E-value: 4.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQESLLEILkLRCSSST----------LYATLYELLQKLNSG-PGNPITPGSFLNSLEiA 118
Cdd:pfam00443 2 GLVNL-GNTCYMNSVLQSLFSIPPFRDYL-LRISPLSedsrynkdinLLCALRDLFKALQKNsKSSSVSPKMFKKSLG-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 119 TNKKLVRSIQQDAQEFLQHLVETLE--LQKPHTykwSKVLSFPVDSpFIGTMEQKVQCCQCLAISISYSTATSIQLCLPP 196
Cdd:pfam00443 79 LNPDFSGYKQQDAQEFLLFLLDGLHedLNGNHS---TENESLITDL-FRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 197 EYSGNSNVSLLSLMEA----DREQHISDYKCDSCfksspkHSKTSCIRTVDWKNPPTILQIQLERTSYTCQGLTRNNVSI 272
Cdd:pfam00443 155 DSAELKTASLQICFLQfsklEELDDEEKYYCDKC------GCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 273 SFPSKL------------ILKNKHHYILRSLITHSGSVTYGHYLCYRLQDD--IWWKANDSLITKSSlNEALSQTRSACL 338
Cdd:pfam00443 229 EFPLELdlsrylaeelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEnnRWYKFDDEKVTEVD-EETAVLSSSAYI 307
|
...
gi 19112481 339 LFY 341
Cdd:pfam00443 308 LFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
50-342 |
1.61e-39 |
|
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: 140.31 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQeslleilklrcssstlyatlyellqklnsgpgnpitpgsflnsleiatnkklvrsiQQ 129
Cdd:cd02257 1 GLNNL-GNTCYLNSVLQALFSE--------------------------------------------------------QQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 130 DAQEFLQHLVETLE---LQKPHTYKWSKVLSFPVDSPFIGTMEQKVQCCQCLAISISYSTATSIQLCLPPEysGNSNVSL 206
Cdd:cd02257 24 DAHEFLLFLLDKLHeelKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVK--GLPQVSL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 207 LSLMEA-DREQHISDYKCDSCfkssPKHSKTSCIRTVDWKNPPTILQIQLERTSYTCQGLTR-NNVSISFPSKLILK--- 281
Cdd:cd02257 102 EDCLEKfFKEEILEGDNCYKC----EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEkLNTKVSFPLELDLSpyl 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112481 282 -----------NKHHYILRSLITHSG-SVTYGHYLCYRLQ--DDIWWKANDSLITKSSLNEALSQTR---SACLLFYE 342
Cdd:cd02257 178 segekdsdsdnGSYKYELVAVVVHSGtSADSGHYVAYVKDpsDGKWYKFNDDKVTEVSEEEVLEFGSlssSAYILFYE 255
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-342 |
7.64e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 135.57 E-value: 7.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQESLLEILKlrcssstlyatlyellqklnsgpgnpitpgSFLNsleiatnkklvrsiQQ 129
Cdd:cd02662 1 GLVNL-GNTCFMNSVLQALASLPSLIEYLE------------------------------EFLE--------------QQ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 130 DAQEFLQHLVETLELQkphtykwskvLSFPVDspfiGTMEQKVQCCQCLAIS-ISYSTATSIQLCLPPEYSGNSNVSLLS 208
Cdd:cd02662 36 DAHELFQVLLETLEQL----------LKFPFD----GLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSSGSGTTLEHC 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 209 LMEADREQHISDYKCDSCfksspkhsktscirTVDWKNPPTILQIQLERTSYTCQG-LTRNNVSISFPSKLilkNKHHYI 287
Cdd:cd02662 102 LDDFLSTEIIDDYKCDRC--------------QTVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERL---PKVLYR 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112481 288 LRSLITHSGSVTYGHYLCYR----------------------LQDDIWWKANDSLITKSSLNEALSQtRSACLLFYE 342
Cdd:cd02662 165 LRAVVVHYGSHSSGHYVCYRrkplfskdkepgsfvrmregpsSTSHPWWRISDTTVKEVSESEVLEQ-KSAYMLFYE 240
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-341 |
1.42e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 104.28 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQESLLEILKLRCSSST-------LYATLYELLQKLNSGPGNPITPGSFLNSLEIaTNKK 122
Cdd:cd02661 3 GLQNL-GNTCFLNSVLQCLTHTPPLANYLLSREHSKDccnegfcMMCALEAHVERALASSGPGSAPRIFSSNLKQ-ISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 123 LVRSIQQDAQEFLQHLVETLELQKPHTYKWSKVLSFP------VDSPFIGTMEQKVQCCQCLAISISYSTatSIQLCLpp 196
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSsqettlVQQIFGGYLRSQVKCLNCKHVSNTYDP--FLDLSL-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 197 EYSGNSNV--SLLSLMEADREQHISDYKCDSCFKSSPKhSKTSCIRTVdwknpPTILQIQLERTSYTCQG-LTRNnvsIS 273
Cdd:cd02661 157 DIKGADSLedALEQFTKPEQLDGENKYKCERCKKKVKA-SKQLTIHRA-----PNVLTIHLKRFSNFRGGkINKQ---IS 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112481 274 FPSKLILK----NKHH----YILRSLITHSG-SVTYGHYLCY-RLQDDIWWKANDSLITKSSLNEALSQTrsACLLFY 341
Cdd:cd02661 228 FPETLDLSpymsQPNDgplkYKLYAVLVHSGfSPHSGHYYCYvKSSNGKWYNMDDSKVSPVSIETVLSQK--AYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
49-341 |
7.99e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 100.14 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 49 KGLYNVsGNDCFLNCVLQSLA-----SQESLLEILKLRCSSSTLYATLY----ELLQKLN-SGPGNPITPGSFLNSLEIA 118
Cdd:cd02660 1 RGLINL-GATCFMNVILQALLhnpllRNYFLSDRHSCTCLSCSPNSCLScamdEIFQEFYySGDRSPYGPINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 119 tNKKLVRSIQQDAQEFLQHLVETLelqkpHT-YKWSKVLSF-------PVDSPFIGTMEQKVQCCQCLAISISYSTATSI 190
Cdd:cd02660 80 -SRNLAGYSQQDAHEFFQFLLDQL-----HThYGGDKNEANdeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 191 QLCLPPE--------YSGNSNVSLLS--LMEADREQHI--SDYKCDSCfksspkHSKTSCIRTVDWKNPPTILQIQLERT 258
Cdd:cd02660 154 SLDIPNKstpswalgESGVSGTPTLSdcLDRFTRPEKLgdFAYKCSGC------GSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 259 SYTCQGLTRN-NVSISFPSKL-----------------ILKNKHHYILRSLITHSGSVTYGHYLCY-RLQDDIWWKANDS 319
Cdd:cd02660 228 EHSLNKTSRKiDTYVQFPLELnmtpytsssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAYcRQGDGQWFKFDDA 307
|
330 340
....*....|....*....|..
gi 19112481 320 LITKSSLNEALSQtrSACLLFY 341
Cdd:cd02660 308 MITRVSEEEVLKS--QAYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-342 |
5.28e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 95.43 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQeslleilklrcssstlyatlyellqklnsgpgnpitpgsflnsleiatnkklvrsiQQ 129
Cdd:cd02674 1 GLRNL-GNTCYMNSILQCLSAD--------------------------------------------------------QQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 130 DAQEFLQHLVETLElqkphtykwskvlSFpVDSPFIGTMEQKVQCCQCLAISISYSTATSIQLCLPPEYSGNSNVSLLSL 209
Cdd:cd02674 24 DAQEFLLFLLDGLH-------------SI-IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDC 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 210 MEA----DREQHISDYKCDSCFKsspkhsKTSCIRTVDWKNPPTILQIQLERTSYTCQGLTRNNVSISFPSKLILKNKH- 284
Cdd:cd02674 90 LRLftkeETLDGDNAWKCPKCKK------KRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYv 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112481 285 ---------HYILRSLITHSGSVTYGHYLCY--RLQDDIWWKANDSLITKssLNEALSQTRSACLLFYE 342
Cdd:cd02674 164 dtrsftgpfKYDLYAVVNHYGSLNGGHYTAYckNNETNDWYKFDDSRVTK--VSESSVVSSSAYILFYE 230
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
50-342 |
1.64e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 87.16 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLAsqeslLEILKLRCSSSTLYATLYELLQKLNSG--PGNPITPGSFLNSLEIATNKKLVR-- 125
Cdd:COG5533 1 GLPNL-GNTCFMNSVLQILA-----LYLPKLDELLDDLSKELKVLKNVIRKPepDLNQEEALKLFTALWSSKEHKVGWip 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 126 --SIQQDAQEFLQHLVETLELQKphtykwskVLSFPVDSPFIGTMEQKVqccqclaisiSYSTATSIQLCLPPEYSGNSN 203
Cdd:COG5533 75 pmGSQEDAHELLGKLLDELKLDL--------VNSFTIRIFKTTKDKKKT----------STGDWFDIIIELPDQTWVNNL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 204 VSLLSLMEADREQhISDYKCDSCFKSSPKHSKTSCIRTVDWKNPPTILQIQLER--TSYTCQGLTRN-----NVSISFPS 276
Cdd:COG5533 137 KTLQEFIDNMEEL-VDDETGVKAKENEELEVQAKQEYEVSFVKLPKILTIQLKRfaNLGGNQKIDTEvdekfELPVKHDQ 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112481 277 KLILKNKHHYILRSLITHSGSVTYGHYLCYRLQDDIWWKANDSLITKSSLNEALS-QTRSACLLFYE 342
Cdd:COG5533 216 ILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGKWEKANDSDVTPVSEEEAINeKAKNAYLYFYE 282
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-323 |
1.40e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 82.08 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQESLLEILkLRCSSSTLYA-------------TLYELLQ----KLNSGPGNPITPGSFL 112
Cdd:cd02668 1 GLKNL-GATCYVNSFLQLWFMNLEFRKAV-YECNSTEDAElknmppdkphepqTIIDQLQlifaQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 113 NSLEIATnkklvrSIQQDAQEFLQHLVETLE--LQKPHTYKWSKVlsfpVDSPFIGTMEQKVQCCQCLAISISYSTATSI 190
Cdd:cd02668 79 KALGLDT------GQQQDAQEFSKLFLSLLEakLSKSKNPDLKNI----VQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 191 QLCLppeySGNsnvslLSLMEADR-----EQHISD--YKCDSCfksspkHSKTSCIRTVDWKNPPTILQIQLERTSYTCQ 263
Cdd:cd02668 149 ELQL----KGH-----KTLEECIDeflkeEQLTGDnqYFCESC------NSKTDATRRIRLTTLPPTLNFQLLRFVFDRK 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112481 264 GLTRN--NVSISFPSKLILK--------NKHHYILRSLITHSGSVTY-GHYLC--YRLQDDIWWKANDSLITK 323
Cdd:cd02668 214 TGAKKklNASISFPEILDMGeylaesdeGSYVYELSGVLIHQGVSAYsGHYIAhiKDEQTGEWYKFNDEDVEE 286
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-342 |
2.03e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 81.77 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLA-----SQESLLEILKLRCSSSTLYATLYELL------QKLNSGPGN---------PITPG 109
Cdd:cd02664 1 GLINL-GNTCYMNSVLQALFmakdfRRQVLSLNLPRLGDSQSVMKKLQLLQahlmhtQRRAEAPPDyfleasrppWFTPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 110 SflnsleiatnkklvrsiQQDAQEFLQHLVETLelqkpHTYkwskvlsfpVDSPFIGTMEQKVQCCQCLAISISYSTATS 189
Cdd:cd02664 80 S-----------------QQDCSEYLRYLLDRL-----HTL---------IEKMFGGKLSTTIRCLNCNSTSARTERFRD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 190 IQLCLPpeysgnSNVSLLSLMEAdREQHISD--YKCDSCFKSSPkhsktsCIRTVDWKNPPTILQIQLERTSYTCQGLTR 267
Cdd:cd02664 129 LDLSFP------SVQDLLNYFLS-PEKLTGDnqYYCEKCASLQD------AEKEMKVTGAPEYLILTLLRFSYDQKTHVR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 268 ----NNVSI-----------SFPSKLILKNKH--------------HYILRSLITHSG-SVTYGHYLCY----------- 306
Cdd:cd02664 196 ekimDNVSInevlslpvrveSKSSESPLEKKEeesgddgelvtrqvHYRLYAVVVHSGySSESGHYFTYardqtdadstg 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 19112481 307 -----------RLQDDIWWKANDSLITKSSLNEALSQTR-----SACLLFYE 342
Cdd:cd02664 276 qecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNVTSrfpkdTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-342 |
4.37e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 80.12 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQESLLEILKLrcssstlyatlyellqklnsgpgnpiTPGSFLNSLeiatNKKLVR---S 126
Cdd:cd02667 1 GLSNL-GNTCFFNAVMQNLSQTPALRELLSE--------------------------TPKELFSQV----CRKAPQfkgY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 127 IQQDAQEFLQHLVETLELQkphtykwskvlsfpVDSPFIGTMEQKVQCCQCLAISISYSTATSIQLclpPEYSGNSN-VS 205
Cdd:cd02667 50 QQQDSHELLRYLLDGLRTF--------------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL---PRSDEIKSeCS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 206 LLSLMEADREQHISDYKCDSCFKSSPKHSKTSCIrtvdwKNPPTILQIQLERTSYTCQG-LTRNNVSISFPSKLIL---- 280
Cdd:cd02667 113 IESCLKQFTEVEILEGNNKFACENCTKAKKQYLI-----SKLPPVLVIHLKRFQQPRSAnLRKVSRHVSFPEILDLapfc 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 281 ---------KNKHHYILRSLITHSGSVTYGHYLCYRLQD-----------------------DIWWKANDSLITKSSLNE 328
Cdd:cd02667 188 dpkcnssedKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEE 267
|
330
....*....|....
gi 19112481 329 ALSQtrSACLLFYE 342
Cdd:cd02667 268 VLKS--EAYLLFYE 279
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-342 |
6.91e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 80.06 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNvSGNDCFLNCVLQSLAS----QESLLEILKLRCSSSTLYAT-----LYELLQKLNSG----PGNPITPG-SFLNSL 115
Cdd:cd02658 1 GLRN-LGNSCYLNSVLQVLFSipsfQWRYDDLENKFPSDVVDPANdlncqLIKLADGLLSGryskPASLKSENdPYQVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 116 EIATNKKLV--------RSIQQDAQEFLQHLVETL--ELQKPHTYKWSKVLSFpvdspfigTMEQKVQCCQCLAISISYS 185
Cdd:cd02658 80 KPSMFKALIgkghpefsTMRQQDALEFLLHLIDKLdrESFKNLGLNPNDLFKF--------MIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 186 TATSIQLCLPPEYSGNS--------NVSLLSLMEADREQHISDYKCDSCfKSSPKHSKTSCIRTVdwknpPTILQIQLER 257
Cdd:cd02658 152 LSEILSLPVPKDEATEKeegelvyePVPLEDCLKAYFAPETIEDFCSTC-KEKTTATKTTGFKTF-----PDYLVINMKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 258 TSYTCQGL-TRNNVSISFPSKLilkNKHHYILRSLITHSG-SVTYGHYLCYRLQDDI----WWKANDSLITKSSLNEALS 331
Cdd:cd02658 226 FQLLENWVpKKLDVPIDVPEEL---GPGKYELIAFISHKGtSVHSGHYVAHIKKEIDgegkWVLFNDEKVVASQDPPEMK 302
|
330
....*....|.
gi 19112481 332 QTrsACLLFYE 342
Cdd:cd02658 303 KL--GYIYFYQ 311
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-341 |
3.39e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 72.62 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 35 SPSTGKRLVKNASIKGLYNVsGNDCFLNCVLQSLASQESLLEILKLRCSS----STLYATLYELLQKLNSGPGNPiTPGS 110
Cdd:cd02671 11 SATSCEKRENLLPFVGLNNL-GNTCYLNSVLQVLYFCPGFKHGLKHLVSLissvEQLQSSFLLNPEKYNDELANQ-APRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 111 FLNSLEiATNKKLVRSIQQDAQEFLQHLVETLElqkphtykwskvlSFpVDSPFIGTMEQKVQCCQCLAIS----ISYST 186
Cdd:cd02671 89 LLNALR-EVNPMYEGYLQHDAQEVLQCILGNIQ-------------EL-VEKDFQGQLVLRTRCLECETFTerreDFQDI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 187 ATSIQLCLPPEYSGNSNVSLLSLME-ADREQHISDYKCDSCFKSSPK------HSKTSCIRTVDWKNPPTILQIQLERTS 259
Cdd:cd02671 154 SVPVQESELSKSEESSEISPDPKTEmKTLKWAISQFASVERIVGEDKyfcencHHYTEAERSLLFDKLPEVITIHLKCFA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 260 YTCQ------GLTRNNVSISFPSKLIL------KNKHHYILRSLITHSG-SVTYGHYLCYRLqddiWWKANDS---LITK 323
Cdd:cd02671 234 ANGSefdcygGLSKVNTPLLTPLKLSLeewstkPKNDVYRLFAVVMHSGaTISSGHYTAYVR----WLLFDDSevkVTEE 309
|
330 340
....*....|....*....|..
gi 19112481 324 SSLNEALSQTRSAC----LLFY 341
Cdd:cd02671 310 KDFLEALSPNTSSTstpyLLFY 331
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-342 |
4.90e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 71.57 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 56 GNDCFLNCVLQSLAsQESLLEILKlrcssstlyaTLYELLQKLNSGPGNpITPGSFLNSLEiaTNKKLVRS-IQQDAQEF 134
Cdd:cd02663 6 GNTCYCNSVLQALY-FENLLTCLK----------DLFESISEQKKRTGV-ISPKKFITRLK--RENELFDNyMHQDAHEF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 135 ----LQHLVETLELQKPHTYKWSKVLSFPVDSP--------FIGTMEQKVQCCQC----------LAISISYSTATSIQL 192
Cdd:cd02663 72 lnflLNEIAEILDAERKAEKANRKLNNNNNAEPqptwvheiFQGILTNETRCLTCetvssrdetfLDLSIDVEQNTSITS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 193 CLPPEYSgnsnvsllslmeadREQHISDYK--CDSCfksspkHSKTSCIRTVDWKNPPTILQIQLERTSYT--CQGLTRN 268
Cdd:cd02663 152 CLRQFSA--------------TETLCGRNKfyCDEC------CSLQEAEKRMKIKKLPKILALHLKRFKYDeqLNRYIKL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 269 NVSISFPSKLILKNKHH--------YILRSLITHSGS-VTYGHYLCYRLQDDIWWKANDSLITK---SSLNEALSQTR-- 334
Cdd:cd02663 212 FYRVVFPLELRLFNTTDdaenpdrlYELVAVVVHIGGgPNHGHYVSIVKSHGGWLLFDDETVEKideNAVEEFFGDSPnq 291
|
....*....
gi 19112481 335 -SACLLFYE 342
Cdd:cd02663 292 aTAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-342 |
8.11e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 65.04 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQESLLEILK--------LRCSSSTLYATLYELLQKLNSGPgNPITPGSFLNSLEIA--- 118
Cdd:cd02657 1 GLTNL-GNTCYLNSTLQCLRSVPELRDALKnynparrgANQSSDNLTNALRDLFDTMDKKQ-EPVPPIEFLQLLRMAfpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 119 ----TNKKLVRsiQQDAQEFLQHLVETLELQKPHTYKWSKVlsfpVDSPFIGTMEQKVQCCQCLAI-SISYSTATSIQLC 193
Cdd:cd02657 79 faekQNQGGYA--QQDAEECWSQLLSVLSQKLPGAGSKGSF----IDQLFGIELETKMKCTESPDEeEVSTESEYKLQCH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 194 LppeySGNSNVS-----LLSLMEADREQHISDYKCDScfksspKHSKTSCIRTVdwknpPTILQIQLERTSYTCQGLTRN 268
Cdd:cd02657 153 I----SITTEVNylqdgLKKGLEEEIEKHSPTLGRDA------IYTKTSRISRL-----PKYLTVQFVRFFWKRDIQKKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 269 NV--SISFPSKL----ILKNKHHYILRSLITHSG-SVTYGHYLCYRLQDDI--WWKANDSLITKSSLNEAL-----SQTR 334
Cdd:cd02657 218 KIlrKVKFPFELdlyeLCTPSGYYELVAVITHQGrSADSGHYVAWVRRKNDgkWIKFDDDKVSEVTEEDILklsggGDWH 297
|
....*...
gi 19112481 335 SACLLFYE 342
Cdd:cd02657 298 IAYILLYK 305
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-346 |
2.50e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 63.82 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNvSGNDCFLNCVLQSLASQ----ESLLEILKLRCSSSTLYATLyeLLQKLNSgpgnpitpgsFLNSLEIA----TNK 121
Cdd:cd02659 4 GLKN-QGATCYMNSLLQQLYMTpefrNAVYSIPPTEDDDDNKSVPL--ALQRLFL----------FLQLSESPvkttELT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 122 KLVRS---------IQQDAQEFLQHLVETLElqkphtyKWSKVLSFP--VDSPFIGTMEQKVQCCQClaisISYSTATSI 190
Cdd:cd02659 71 DKTRSfgwdslntfEQHDVQEFFRVLFDKLE-------EKLKGTGQEglIKNLFGGKLVNYIICKEC----PHESEREEY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 191 QLCLPPEYSGNSNV--SLLSLMEADREQHISDYKCDSCfKSSPKHSKTSCIrtvdwKNPPTILQIQLERTSYTCQGLTRN 268
Cdd:cd02659 140 FLDLQVAVKGKKNLeeSLDAYVQGETLEGDNKYFCEKC-GKKVDAEKGVCF-----KKLPPVLTLQLKRFEFDFETMMRI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 269 --NVSISFP-------------------SKLILKNKHHYILRSLITHSGSVTYGHYLCYRLQ--DDIWWKANDSLITKSS 325
Cdd:cd02659 214 kiNDRFEFPleldmepytekglakkegdSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDrdDGKWYKFNDDVVTPFD 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 19112481 326 LNEALSQ--------------------TRSACLLFYEMESP 346
Cdd:cd02659 294 PNDAEEEcfggeetqktydsgprafkrTTNAYMLFYERKSP 334
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
50-330 |
2.04e-07 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 52.95 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNvSGNDCFLNCVLQSLASQESL------LEILKLRCSSSTLYA--TLYELLQKLNsgpgNPITPGSFLNSLEIATnk 121
Cdd:COG5077 195 GLRN-QGATCYMNSLLQSLFFIAKFrkdvygIPTDHPRGRDSVALAlqRLFYNLQTGE----EPVDTTELTRSFGWDS-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 122 kLVRSIQQDAQEFLQHLVETLELQKPHTykwskVLSFPVDSPFIGTMEQKVQCcqclaISISYSTATS---IQLCLPPEY 198
Cdd:COG5077 268 -DDSFMQHDIQEFNRVLQDNLEKSMRGT-----VVENALNGIFVGKMKSYIKC-----VNVNYESARVedfWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 199 SGNSNVSLLSLMEADREQHISDYKCDscfksspKHSKTSCIRTVDWKNPPTILQIQLERTSYTCqgLTRNNVSIS----F 274
Cdd:COG5077 337 MKNLQESFRRYIQVETLDGDNRYNAE-------KHGLQDAKKGVIFESLPPVLHLQLKRFEYDF--ERDMMVKINdryeF 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 275 PSKLILK------------NKHHYILRSLITHSGSVTYGHYLCY--RLQDDIWWKANDSLITKSSLNEAL 330
Cdd:COG5077 408 PLEIDLLpfldrdadksenSDAVYVLYGVLVHSGDLHEGHYYALlkPEKDGRWYKFDDTRVTRATEKEVL 477
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
43-195 |
1.70e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 43.33 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 43 VKNASIKGLYNVsGNDCFLNCVLQSLAS-------------QESLLEILKLRCSSStLYATLYELLQKLNSGPGNPITPG 109
Cdd:COG5560 260 NKEAGTCGLRNL-GNTCYMNSALQCLMHtwelrdyflsdeyEESINEENPLGMHGS-VASAYADLIKQLYDGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 110 SFLNSLEiATNKKLVRSIQQDAQEFLQHLVETLE------LQKPHTykwSKVLSFPVDSP-------------------- 163
Cdd:COG5560 338 GFKKTIG-SFNEEFSGYDQQDSQEFIAFLLDGLHedlnriIKKPYT---SKPDLSPGDDVvvkkkakecwwehlkrndsi 413
|
170 180 190
....*....|....*....|....*....|....*.
gi 19112481 164 ----FIGTMEQKVQCCQCLAISISYSTATSIQLCLP 195
Cdd:COG5560 414 itdlFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-328 |
3.19e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 41.39 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 50 GLYNVsGNDCFLNCVLQSLASQeslleilklrcssstlyatlyellqklnsgpgnpitpgsflnsleiatnkklvrsiQQ 129
Cdd:cd02665 1 GLKNV-GNTCWFSAVIQSLFSQ--------------------------------------------------------QQ 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 130 DAQEFLQHLVETLELqkphtykwSKVLSFPVDSPFIGTMEQKVQCCQCLAISISYSTATSIQLC-----LPPEYSGNSNv 204
Cdd:cd02665 24 DVSEFTHLLLDWLED--------AFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCetfgqYPLQVNGYGN- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 205 sLLSLMEADR-EQHISDYKCDSCFKSSPKHSKTSCirtvdwknpPTILQIQLERTSYTCQGLTRNNVSISFPSKLilkNK 283
Cdd:cd02665 95 -LHECLEAAMfEGEVELLPSDHSVKSGQERWFTEL---------PPVLTFELSRFEFNQGRPEKIHDKLEFPQII---QQ 161
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19112481 284 HHYILRSLITHSGSVTYGHYLCYRLQDDI--WWKANDSLITKSSLNE 328
Cdd:cd02665 162 VPYELHAVLVHEGQANAGHYWAYIYKQSRqeWEKYNDISVTESSWEE 208
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
51-342 |
1.00e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 40.20 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 51 LYNVsGNDCFLNCVLQSLASqeslleilklrcssstlyatlyelLQKLNSGpgnpitpgsFLNSLeiatnkklvrsiQQD 130
Cdd:cd02673 2 LVNT-GNSCYFNSTMQALSS------------------------IGKINTE---------FDNDD------------QQD 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 131 AQEFLQHLVETLE-------LQKPHTYKWSKVLSfPVDsPFIGTMEQKVQCCQClaisISYSTATSIQLCLPPEYSGNSN 203
Cdd:cd02673 36 AHEFLLTLLEAIDdimqvnrTNVPPSNIEIKRLN-PLE-AFKYTIESSYVCIGC----SFEENVSDVGNFLDVSMIDNKL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112481 204 VSLLSLMEADREQHISDYKCDSCfksSPKHSkTSCIRTVdwkNPPTILQIQLERT-SYTCQGLTRNNvsisfpSKLILKN 282
Cdd:cd02673 110 DIDELLISNFKTWSPIEKDCSSC---KCESA-ISSERIM---TFPECLSINLKRYkLRIATSDYLKK------NEEIMKK 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112481 283 KHH----YILRSLITHSG-SVTYGHYLCYRLQD---DIWWKANDSLITKSSLNE-ALSQTRSACLLFYE 342
Cdd:cd02673 177 YCGtdakYSLVAVICHLGeSPYDGHYIAYTKELyngSSWLYCSDDEIRPVSKNDvSTNARSSGYLIFYD 245
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
284-336 |
3.03e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 39.01 E-value: 3.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 19112481 284 HHYILRSLITHSGSVTYGHYLCY--RLQDDIWWKANDSLITKSSLNEALSQTRSA 336
Cdd:cd02666 279 YGYRLHAVFIHRGEASSGHYWVYikDFEENVWRKYNDETVTVVPASEVFLFTLGN 333
|
|
| |
