|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
58-387 |
4.03e-108 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 320.16 E-value: 4.03e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 58 AGLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRY 137
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDY-LLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 138 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKSSLTCT 217
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHST--------------------------ENESLITDLFRGQLKSRLKCL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 218 DCGYCSTVFDPFWDLSLPIAKRGYPEVT--LMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKR 295
Cdd:pfam00443 134 SCGEVSETFEPFSDLSLPIPGDSAELKTasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 296 FSESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVT 370
Cdd:pfam00443 214 FSYNRSTWEKLNTEVEFPL-ELDLSRYLAEELkpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVT 292
|
330
....*....|....*...
gi 28565285 371 PMS-SSQVRTSDAYLLFY 387
Cdd:pfam00443 293 EVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
1.08e-107 |
|
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: 316.15 E-value: 1.08e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 138
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 prfvgyNQQDAQEFLRFLLDGLHnevnrvtlrpksnpenldhlpddekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 218
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 219 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 296
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 297 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSS 374
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 28565285 375 SQVRTSDAYLLFYE 388
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
58-387 |
5.70e-75 |
|
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: 235.25 E-value: 5.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 58 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKliQTIWTSSPNDVvsPSEFKTQIQRY 137
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSA--PRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 138 APRFVGYNQQDAQEFLRFLLDGLHnevnRVTLRPKSNPENLDHLpddekgrqmwrkylEREDSRIGDLFVGQLKSSLTCT 217
Cdd:cd02661 78 SKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS--------------SQETTLVQQIFGGYLRSQVKCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 218 DCGYCSTVFDPFWDLSLPIAKRGypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS 297
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 298 EsrIRTSKLTTFVNFPLRdLDLREFASENT-NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPgTGEWHTFNDSSVTPMSSS 375
Cdd:cd02661 216 N--FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIE 291
|
330
....*....|..
gi 28565285 376 QVRTSDAYLLFY 387
Cdd:cd02661 292 TVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
59-388 |
1.34e-74 |
|
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: 232.37 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 138
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 prfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwRKYLEREDSRIGDLFVGQLKSSLTCTD 218
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 219 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKpTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS- 297
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNC-YKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 298 ESRIRTSKLTTFVNFPLRdLDLREFASENT-------NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDSSV 369
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLE-LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKV 231
|
330 340
....*....|....*....|....
gi 28565285 370 TPMSSSQV-----RTSDAYLLFYE 388
Cdd:cd02257 232 TEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-387 |
3.01e-64 |
|
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: 208.38 E-value: 3.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELRDYclqrlYMRDLHH----GSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQI 134
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNY-----FLSDRHSctclSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 135 QRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpKSNPENLDHLPddekgrqmwrkyleredSRIGDLFVGQLKSSL 214
Cdd:cd02660 77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD----KNEANDESHCN-----------------CIIHQTFSGSLQSSV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 215 TCTDCGYCSTVFDPFWDLSLPI-----------AKRGYPEVTLMDCMRLFTKEDVLdGDEKPTCCRCRGRKRCIKKFSIQ 283
Cdd:cd02660 136 TCQRCGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 284 RFPKILVLHLKRFSESRIRTS-KLTTFVNFPLRdLDLREFAS----------ENTNHAVYNLYAVSNHSGTTMGGHYTAY 352
Cdd:cd02660 215 KLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTSssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAY 293
|
330 340 350
....*....|....*....|....*....|....*
gi 28565285 353 CRSpGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFY 387
Cdd:cd02660 294 CRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
1.95e-60 |
|
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: 196.84 E-value: 1.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRlymrdlhhgsnahtalveefakliqtiwtsspndvvsPSEFKTQIQRYA 138
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------------------------------PKELFSQVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 218
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 219 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKptcCRCRGRKRCIKKFSIQRFPKILVLHLKRFS- 297
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 298 ESRIRTSKLTTFVNFPLRdLDLREFASENTNHA------VYNLYAVSNHSGTTMGGHYTAYCRS---------------- 355
Cdd:cd02667 163 PRSANLRKVSRHVSFPEI-LDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 28565285 356 -----PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 388
Cdd:cd02667 242 adeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
56-236 |
1.13e-48 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 176.61 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 56 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGS--NAHTALVEEFAKLIQTIWTSSpNDVVSPSEFKTQ 133
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplGMHGSVASAYADLIKQLYDGN-LHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 134 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENL---DHLPDDEKGRQMWRKYLEREDSRIGDLFVGQL 210
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLspgDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
|
170 180
....*....|....*....|....*.
gi 28565285 211 KSSLTCTDCGYCSTVFDPFWDLSLPI 236
Cdd:COG5560 423 KSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-392 |
4.94e-43 |
|
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: 153.18 E-value: 4.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 56 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlyMRDLHHGSNAH---TALVEEFAKLiQTiwtsSPNDVVSPSEFKT 132
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYS---IPPTEDDDDNKsvpLALQRLFLFL-QL----SESPVKTTELTDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 133 QiqryapRFVG------YNQQDAQEFLRFLLDglhnevnrvtlrpksnpeNLDHlpddekgrqMWrKYLEREDSrIGDLF 206
Cdd:cd02659 73 T------RSFGwdslntFEQHDVQEFFRVLFD------------------KLEE---------KL-KGTGQEGL-IKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 207 VGQLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYpeVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFP 286
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAV--KGK--KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 287 KILVLHLKRF-----SESRIrtsKLTTFVNFPLRdLDLREFASENTNH------------AVYNLYAVSNHSGTTMGGHY 349
Cdd:cd02659 194 PVLTLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYTEKGLAKkegdsekkdsesYIYELHGVLVHSGDAHGGHY 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28565285 350 TAYCRSPGTGEWHTFNDSSVTPMSSSQV----------------------RTSDAYLLFYELASP 392
Cdd:cd02659 270 YSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
1.91e-37 |
|
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: 137.44 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELrdYCLqrlymRDLHHGSNAHTALVeefakliqtiwtsspnDVVSPSEFKTQIQRYA 138
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL--TCL-----KDLFESISEQKKRT----------------GVISPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLR-PKSNPENLDHLPDDEKGrqmWrkyleredsrIGDLFVGQLKSSLTCT 217
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLLNEIAEILDAERKAeKANRKLNNNNNAEPQPT---W----------VHEIFQGILTNETRCL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 218 DCGYCSTVFDPFWDLSLPIAkrgyPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF- 296
Cdd:cd02663 125 TCETVSSRDETFLDLSIDVE----QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFk 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 297 -SESRIRTSKLTTFVNFPlrdLDLREFASENTNHAV---YNLYAVSNHSGTT-MGGHYTAYCRSpgTGEWHTFNDSSVTP 371
Cdd:cd02663 201 yDEQLNRYIKLFYRVVFP---LELRLFNTTDDAENPdrlYELVAVVVHIGGGpNHGHYVSIVKS--HGGWLLFDDETVEK 275
|
330 340
....*....|....*....|....*
gi 28565285 372 MSSSQVR--------TSDAYLLFYE 388
Cdd:cd02663 276 IDENAVEeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
4.76e-37 |
|
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: 136.78 E-value: 4.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELRDY-----CLQRLYMRDLHHGSNAH-TALVEEFAKLIQTIWTSSPNdVVSPSEFKT 132
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAvyecnSTEDAELKNMPPDKPHEpQTIIDQLQLIFAQLQFGNRS-VVDPSGFVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 133 qiqryAPRFVGYNQQDAQEFLRFLLDGLHNevnrvTLRPKSNPenldhlpddeKGRQMwrkyleredsrIGDLFVGQLKS 212
Cdd:cd02668 80 -----ALGLDTGQQQDAQEFSKLFLSLLEA-----KLSKSKNP----------DLKNI-----------VQDLFRGEYSY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 213 SLTCTDCGYCSTVFDPFWDLSLPIAKrgypEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLH 292
Cdd:cd02668 129 VTQCSKCGRESSLPSKFYELELQLKG----HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 293 LKRFSESRIRTS--KLTTFVNFPLrDLDLREF-ASENTNHAVYNLYAVSNHSGT-TMGGHYTAYCRSPGTGEWHTFNDSS 368
Cdd:cd02668 205 LLRFVFDRKTGAkkKLNASISFPE-ILDMGEYlAESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDED 283
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 28565285 369 VTPMSSSQVR---------------------TSDAYLLFYE 388
Cdd:cd02668 284 VEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
2.97e-36 |
|
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: 134.38 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELRDYCLQrlYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpnDVVSPSEFKTQIQRYA 138
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN--YNPARRGANQSSDNLTNALRDLFDTMDKKQ--EPVPPIEFLQLLRMAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 PRFV------GYNQQDAQEFLRFLLDGLHNEvnrvtLRPKSnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKS 212
Cdd:cd02657 77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQK-----LPGAG-----------------------SKGSFIDQLFGIELET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 213 SLTCTDCGYCSTV-FDPFWDLSLPIAkrgypevTLMDCMRLFTK-EDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILV 290
Cdd:cd02657 129 KMKCTESPDEEEVsTESEYKLQCHIS-------ITTEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 291 LHLKRFS--ESRIRTSKLTTFVNFPLrDLDLREFAsenTNHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDS 367
Cdd:cd02657 202 VQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDD 277
|
330 340
....*....|....*....|....*...
gi 28565285 368 SVTPMSSSQVRTSD-------AYLLFYE 388
Cdd:cd02657 278 KVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
242-388 |
1.34e-31 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 126.92 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 242 PEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLRE 321
Cdd:COG5560 673 RTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSG 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28565285 322 FASENTNHAV-YNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 388
Cdd:COG5560 753 VEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-388 |
2.04e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 121.27 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 56 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLqrLYMRDLHHGSNAhTALVEEFAKLIQTIWtsSPND---VVSPSEFKT 132
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--LYENYENIKDRK-SELVKRLSELIRKIW--NPRNfkgHVSPHELLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 133 QIQRYAPRFVGYNQQ-DAQEFLRFLLDGLHNEVNRVTlrpKSNPENLDHLPDDEKgRQMWRKYLEREDSrigdlfvgqLK 211
Cdd:cd02669 193 AVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSK---KPNSSIIHDCFQGKV-QIETQKIKPHAEE---------EG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 212 SSLTCTDCGYCSTVFD-PFWDLSL-----PIAKRGY-----PEVTLMDcmrLFTKedvLDGDEKPTCCRCrgrkrcIKKF 280
Cdd:cd02669 260 SKDKFFKDSRVKKTSVsPFLLLTLdlpppPLFKDGNeeniiPQVPLKQ---LLKK---YDGKTETELKDS------LKRY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 281 SIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTN----HAVYNLYAVSNHSGTTMG-GHYTAYCRS 355
Cdd:cd02669 328 LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPslnlSTKYNLVANIVHEGTPQEdGTWRVQLRH 407
|
330 340 350
....*....|....*....|....*....|...
gi 28565285 356 PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 388
Cdd:cd02669 408 KSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
59-388 |
4.42e-30 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 117.21 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLS-NTRELRDYCLQRLY----MRDLHHGSNAhTALVEEFAKLIQTIWTSspndvvspsefktQ 133
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKelkvLKNVIRKPEP-DLNQEEALKLFTALWSS-------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 134 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNE-VNRVTLRpksnpenlDHLPDDEKGRqmwrkyleredSRIGDLFvgqlks 212
Cdd:COG5533 67 EHKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIR--------IFKTTKDKKK-----------TSTGDWF------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 213 SLTctdcgycstvfdpfwdLSLPIAKRGYPEVTLMDCmrlFTKEDVLDGDEKPTCCRCRGRKRCIKK----FSIQRFPKI 288
Cdd:COG5533 122 DII----------------IELPDQTWVNNLKTLQEF---IDNMEELVDDETGVKAKENEELEVQAKqeyeVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 289 LVLHLKRFSESrIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSpgTGEWHTFNDSS 368
Cdd:COG5533 183 LTIQLKRFANL-GGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSD 259
|
330 340
....*....|....*....|...
gi 28565285 369 VTPMSSSQVRTSD---AYLLFYE 388
Cdd:COG5533 260 VTPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
57-387 |
1.40e-29 |
|
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: 116.92 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 57 LAGLRNLGNTCFMNSILQCLSntrelrdYCLQrlYMRDLHHGSNAHTALVEefaklIQTIWTSSPNDVVS------PSEF 130
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLY-------FCPG--FKHGLKHLVSLISSVEQ-----LQSSFLLNPEKYNDelanqaPRRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 131 KTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlrpksnpenldhlpddekgrqmwrkyleredsrigdLFVGQL 210
Cdd:cd02671 90 LNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------------------DFQGQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 211 KSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEV---------------TLMDCMRLFTKEDVLDGDEKPTCCRCRGRKR 275
Cdd:cd02671 132 VLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 276 CIKKFSIQRFPKILVLHLKRFSESRIRT------SKLTTFVNFPLrDLDLREFASENTNHaVYNLYAVSNHSGTTMG-GH 348
Cdd:cd02671 212 AERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL-KLSLEEWSTKPKND-VYRLFAVVMHSGATISsGH 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 28565285 349 YTAYCRspgtgeWHTFNDSSVTPM---------SSSQVRTSDAYLLFY 387
Cdd:cd02671 290 YTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
2.31e-29 |
|
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: 115.88 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELrdyclQRLYMRDLHHGSNA----HTALVEEFAKLIQTIWT---SSPNDVVS----- 126
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSF-----QWRYDDLENKFPSDvvdpANDLNCQLIKLADGLLSgrySKPASLKSendpy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 127 -----PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlRPKSNPENLdhlpddekgrqmwRKYLEREdsr 201
Cdd:cd02658 76 qvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK---NLGLNPNDL-------------FKFMIED--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 202 igdlfvgqlksSLTCTDCGYCSTVFDPFWDLSLPI----------AKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR 271
Cdd:cd02658 137 -----------RLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 272 GrkrcIKKFSIQRFPKILVLHLKRFsesrirtsklTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT-TMGGHYT 350
Cdd:cd02658 206 A----TKTTGFKTFPDYLVINMKRF----------QLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTsVHSGHYV 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 28565285 351 AYCRSP--GTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 388
Cdd:cd02658 272 AHIKKEidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
6.50e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 110.15 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYmrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 138
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-LEEFL----------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 prfvgyNQQDAQEFLRFLLDGLHNEVnrvtlrpkSNPenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 218
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------KFP------------------------------FDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 219 CGYCSTV-FDPFWDLSLPI-AKRGYPEVTLMDCMRLFTKEDVLDGdekptccrcrgRKRCIKKFSIQRFPKILVLHLKRF 296
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD-----------YKCDRCQTVIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 297 SESRIRTS-KLTTFVNFPLRdldlrefasenTNHAVYNLYAVSNHSGTTMGGHYTAYCRSP------------------- 356
Cdd:cd02662 138 VFDGRGTStKNSCKVSFPER-----------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 28565285 357 -GTGEWHTFNDSSVTPMSSSQVR-TSDAYLLFYE 388
Cdd:cd02662 207 sTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-388 |
8.84e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 106.42 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 59 GLRNLGNTCFMNSILQCLSNTRelrDYCLQRLyMRDLHHGSNAHTALVEEfaKLIQTIWTSSPNDVVSPSEFKTQIQRyA 138
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAK---DFRRQVL-SLNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEAPPDYFLEASR-P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 139 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 218
Cdd:cd02664 74 PWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRCLN 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 219 CGYCSTVFD--PFWDLSLPiakrgypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 296
Cdd:cd02664 116 CNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 297 S---ESRIRTsKLTTFVNFPL-------------------RDLDLREFASENTNHAVYNLYAVSNHSGTTM-GGHYTAYC 353
Cdd:cd02664 187 SydqKTHVRE-KIMDNVSINEvlslpvrveskssesplekKEEESGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYFTYA 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28565285 354 RSPGTGE--------------------WHTFNDSSVTPMSSSQV-------RTSDAYLLFYE 388
Cdd:cd02664 266 RDQTDADstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
50-377 |
1.27e-23 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 103.41 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 50 NSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRD-----------------YCLQRLY--MRDLHHGSNAhTALVEEFa 110
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvygiptdhprgrdsvaLALQRLFynLQTGEEPVDT-TELTRSF- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 111 kliqtIWTSspndvvspsefktqiqryaprFVGYNQQDAQEFLRFLLDGLHNEVNrvtlrpKSNPENLdhlpddekgrqm 190
Cdd:COG5077 264 -----GWDS---------------------DDSFMQHDIQEFNRVLQDNLEKSMR------GTVVENA------------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 191 wrkyleredsrIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYPevTLMDCMRLFTKEDVLDGDEKptCCRC 270
Cdd:COG5077 300 -----------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGDNR--YNAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 271 RGRKRCIKKFSI-QRFPKILVLHLKRFSESRIRTS--KLTTFVNFPLrDLDLREF------ASENTNHaVYNLYAVSNHS 341
Cdd:COG5077 363 KHGLQDAKKGVIfESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFldrdadKSENSDA-VYVLYGVLVHS 440
|
330 340 350
....*....|....*....|....*....|....*.
gi 28565285 342 GTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV 377
Cdd:COG5077 441 GDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
60-388 |
2.81e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 66.01 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 60 LRNLGNTCFMNSILQCLSNTRELRdyclqrlymrdlhhgsnahtalvEEFAkliqtiwtsspNDvvspsefktqiqryap 139
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKIN-----------------------TEFD-----------ND---------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 140 rfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKgrqmwrkyleredsrigdlFVGQLKSSLTCTDC 219
Cdd:cd02673 32 -----DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEA-------------------FKYTIESSYVCIGC 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 220 GYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDvldgdEKPTCCRCRGRKRCIKKFSiqRFPKILVLHLKRFsES 299
Cdd:cd02673 88 SFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EKDCSSCKCESAISSERIM--TFPECLSINLKRY-KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 300 RIRTSKLttfvnfpLRD--LDLREFASEntnHAVYNLYAVSNHSG-TTMGGHYTAYCRSPGTG-EWHTFNDSSVTPMSSS 375
Cdd:cd02673 160 RIATSDY-------LKKneEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
|
330
....*....|....*.
gi 28565285 376 QVR---TSDAYLLFYE 388
Cdd:cd02673 230 DVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
58-387 |
2.89e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 67.13 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 58 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlymrdlHHGSNAHTALVEEFAKLIqtiwtssPNDVVSPSEFKTQIQ-- 135
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLN-------FDESKAELASDYPTERRI-------GGREVSRSELQRSNQfv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 136 ---------------RYA-PR----FVGYNQQDAQEFLRFLLDGLhnevnRVTLRPKSNpENLDHLPDDEKgrqmwrkyl 195
Cdd:cd02666 68 yelrslfndlihsntRSVtPSkelaYLALRQQDVTECIDNVLFQL-----EVALEPISN-AFAGPDTEDDK--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 196 EREDsRIGDLFVGQLKSSLTCTDCGYCSTVFDP---FWDLSLPIAKRGYPEVT------LMDCM-RLFTKEDVLDGDEKP 265
Cdd:cd02666 133 EQSD-LIKRLFSGKTKQQLVPESMGNQPSVRTKterFLSLLVDVGKKGREIVVllepkdLYDALdRYFDYDSLTKLPQRS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 266 TCCRCRGRKRCIKKFSIQRF-PKILVLHLKRFSESRIRT-SKLTTFVNFPLRDLD-LREFASENTNHAVYNLYAVSNHSG 342
Cdd:cd02666 212 QVQAQLAQPLQRELISMDRYeLPSSIDDIDELIREAIQSeSSLVRQAQNELAELKhEIEKQFDDLKSYGYRLHAVFIHRG 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 28565285 343 TTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV----RTSDA--YLLFY 387
Cdd:cd02666 292 EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftLGNTAtpYFLVY 342
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
58-369 |
2.62e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 54.97 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 58 AGLRNLGNTCFMNSILQCLSNTRELR-------------DYCL--QRLY---MRDLHHGSNAHT-----AL--VEEFAK- 111
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCLlcELGFlfdMLEKAKGKNCQAsnflrALssIPEASAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 112 -LIQTIWTSSPNDVVSPsefktQIQRyaprfvgynqqdaqeFLRFLLDGLHNEVNRVTLRPKSNPenldhlpddekgrqm 190
Cdd:pfam13423 81 gLLDEDRETNSAISLSS-----LIQS---------------FNRFLLDQLSSEENSTPPNPSPAE--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 191 wrkyleredSRIGDLFVGQLKSSLTCTDCGYCST------VFDpfwdLSLPIAK----RGYPEVTLMDCMRLFTKEDVLd 260
Cdd:pfam13423 126 ---------SPLEQLFGIDAETTIRCSNCGHESVressthVLD----LIYPRKPssnnKKPPNQTFSSILKSSLERETT- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 261 gdEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFvnFPLR-DLDLREFASENTNHAVYNLYA-VS 338
Cdd:pfam13423 192 --TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEiGLTLSDDLQGDNEIVKYELRGvVV 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 28565285 339 NHSGTTMGGHYTAYCR-------SPGTGEWHTFNDSSV 369
Cdd:pfam13423 268 HIGDSGTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
286-387 |
2.75e-08 |
|
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: 54.10 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 286 PKILVLHLKRFSESRIRTSKLTTFVNFPlrdldlREFASENtnhavYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFN 365
Cdd:cd02665 129 PPVLTFELSRFEFNQGRPEKIHDKLEFP------QIIQQVP-----YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYN 197
|
90 100 110
....*....|....*....|....*....|
gi 28565285 366 DSSVTPMSSSQV--------RTSDAYLLFY 387
Cdd:cd02665 198 DISVTESSWEEVerdsfgggRNPSAYCLMY 227
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-388 |
1.90e-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: 45.97 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28565285 279 KFSIQRFPKI----LVLHLKRFSESR-------IRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYA-VSNHSGTTMG 346
Cdd:cd02672 149 TTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGyVCEINDSSRG 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 28565285 347 GHYTA----YCRSPGTGEWHTFNDSSVTPMSssqvrtSDAYLLFYE 388
Cdd:cd02672 229 QHNVVfvikVNEESTHGRWYLFNDFLVTPVS------ELAYILLYQ 268
|
|
| |
