|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
24-353 |
5.12e-109 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 321.31 E-value: 5.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 24 AGLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRY 103
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDY-LLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 104 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKSSLTCT 183
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHST--------------------------ENESLITDLFRGQLKSRLKCL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 184 DCGYCSTVFDPFWDLSLPIAKRGYPEVT--LMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKR 261
Cdd:pfam00443 134 SCGEVSETFEPFSDLSLPIPGDSAELKTasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 262 FSESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVT 336
Cdd:pfam00443 214 FSYNRSTWEKLNTEVEFPL-ELDLSRYLAEELkpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVT 292
|
330
....*....|....*...
gi 119587890 337 PMS-SSQVRTSDAYLLFY 353
Cdd:pfam00443 293 EVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
1.97e-108 |
|
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: 316.54 E-value: 1.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 prfvgyNQQDAQEFLRFLLDGLHnevnrvtlrpksnpenldhlpddekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 184
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 185 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 263 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSS 340
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 119587890 341 SQVRTSDAYLLFYE 354
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
25-354 |
1.59e-75 |
|
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: 233.91 E-value: 1.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 prfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwRKYLEREDSRIGDLFVGQLKSSLTCTD 184
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 185 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKpTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS- 263
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNC-YKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 264 ESRIRTSKLTTFVNFPLRdLDLREFASENT-------NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDSSV 335
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLE-LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKV 231
|
330 340
....*....|....*....|....
gi 119587890 336 TPMSSSQV-----RTSDAYLLFYE 354
Cdd:cd02257 232 TEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-353 |
3.19e-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: 234.48 E-value: 3.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKliQTIWTSSPNDVvsPSEFKTQIQRY 103
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSA--PRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 104 APRFVGYNQQDAQEFLRFLLDGLHnevnRVTLRPKSNPENLDHLpddekgrqmwrkylEREDSRIGDLFVGQLKSSLTCT 183
Cdd:cd02661 78 SKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS--------------SQETTLVQQIFGGYLRSQVKCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 184 DCGYCSTVFDPFWDLSLPIAKRGypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS 263
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 264 EsrIRTSKLTTFVNFPLRdLDLREFASENT-NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPgTGEWHTFNDSSVTPMSSS 341
Cdd:cd02661 216 N--FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIE 291
|
330
....*....|..
gi 119587890 342 QVRTSDAYLLFY 353
Cdd:cd02661 292 TVLSQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-353 |
1.26e-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: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELRDYclqrlYMRDLHH----GSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQI 100
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNY-----FLSDRHSctclSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 101 QRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpKSNPENLDHLPddekgrqmwrkyleredSRIGDLFVGQLKSSL 180
Cdd:cd02660 77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD----KNEANDESHCN-----------------CIIHQTFSGSLQSSV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 181 TCTDCGYCSTVFDPFWDLSLPI-----------AKRGYPEVTLMDCMRLFTKEDVLdGDEKPTCCRCRGRKRCIKKFSIQ 249
Cdd:cd02660 136 TCQRCGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 250 RFPKILVLHLKRFSESRIRTS-KLTTFVNFPLRdLDLREFAS----------ENTNHAVYNLYAVSNHSGTTMGGHYTAY 318
Cdd:cd02660 215 KLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTSssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAY 293
|
330 340 350
....*....|....*....|....*....|....*
gi 119587890 319 CRSpGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFY 353
Cdd:cd02660 294 CRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
1.01e-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: 196.45 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRlymrdlhhgsnahtalveefakliqtiwtsspndvvsPSEFKTQIQRYA 104
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------------------------------PKELFSQVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 184
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 185 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKptcCRCRGRKRCIKKFSIQRFPKILVLHLKRFS- 263
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 264 ESRIRTSKLTTFVNFPLRdLDLREFASENTNHA------VYNLYAVSNHSGTTMGGHYTAYCRS---------------- 321
Cdd:cd02667 163 PRSANLRKVSRHVSFPEI-LDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 119587890 322 -----PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:cd02667 242 adeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
10-202 |
1.57e-49 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 177.77 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 10 SSKKRQNSKSAQ--GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGS--NAHTALVEEFAKLIQTIWTS 85
Cdd:COG5560 250 SIVDDHNRSINKeaGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplGMHGSVASAYADLIKQLYDG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 86 SpNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENL---DHLPDDEKGRQMWRKYLE 162
Cdd:COG5560 330 N-LHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLspgDDVVVKKKAKECWWEHLK 408
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 119587890 163 REDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPI 202
Cdd:COG5560 409 RNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
22-358 |
8.70e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 153.95 E-value: 8.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 22 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlyMRDLHHGSNAH---TALVEEFAKLiQTiwtsSPNDVVSPSEFKT 98
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYS---IPPTEDDDDNKsvpLALQRLFLFL-QL----SESPVKTTELTDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 99 QiqryapRFVG------YNQQDAQEFLRFLLDglhnevnrvtlrpksnpeNLDHlpddekgrqMWrKYLEREDSrIGDLF 172
Cdd:cd02659 73 T------RSFGwdslntFEQHDVQEFFRVLFD------------------KLEE---------KL-KGTGQEGL-IKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 173 VGQLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYpeVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFP 252
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAV--KGK--KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 253 KILVLHLKRF-----SESRIrtsKLTTFVNFPLRdLDLREFASENTNH------------AVYNLYAVSNHSGTTMGGHY 315
Cdd:cd02659 194 PVLTLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYTEKGLAKkegdsekkdsesYIYELHGVLVHSGDAHGGHY 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119587890 316 TAYCRSPGTGEWHTFNDSSVTPMSSSQV----------------------RTSDAYLLFYELASP 358
Cdd:cd02659 270 YSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
4.56e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 138.21 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELrdYCLqrlymRDLHHGSNAHTALVeefakliqtiwtsspnDVVSPSEFKTQIQRYA 104
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL--TCL-----KDLFESISEQKKRT----------------GVISPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLR-PKSNPENLDHLPDDEKGrqmWrkyleredsrIGDLFVGQLKSSLTCT 183
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLLNEIAEILDAERKAeKANRKLNNNNNAEPQPT---W----------VHEIFQGILTNETRCL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 184 DCGYCSTVFDPFWDLSLPIakrgYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF- 262
Cdd:cd02663 125 TCETVSSRDETFLDLSIDV----EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFk 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 263 -SESRIRTSKLTTFVNFPlrdLDLREFASENTNHAV---YNLYAVSNHSGTT-MGGHYTAYCRSpgTGEWHTFNDSSVTP 337
Cdd:cd02663 201 yDEQLNRYIKLFYRVVFP---LELRLFNTTDDAENPdrlYELVAVVVHIGGGpNHGHYVSIVKS--HGGWLLFDDETVEK 275
|
330 340
....*....|....*....|....*
gi 119587890 338 MSSSQVR--------TSDAYLLFYE 354
Cdd:cd02663 276 IDENAVEeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
1.50e-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: 137.55 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELRDY-----CLQRLYMRDLHHGSNAH-TALVEEFAKLIQTIWTSSPNdVVSPSEFKT 98
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAvyecnSTEDAELKNMPPDKPHEpQTIIDQLQLIFAQLQFGNRS-VVDPSGFVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 99 qiqryAPRFVGYNQQDAQEFLRFLLDGLHNevnrvTLRPKSNPenldhlpddeKGRQMwrkyleredsrIGDLFVGQLKS 178
Cdd:cd02668 80 -----ALGLDTGQQQDAQEFSKLFLSLLEA-----KLSKSKNP----------DLKNI-----------VQDLFRGEYSY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 179 SLTCTDCGYCSTVFDPFWDLSLPIAKrgypEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLH 258
Cdd:cd02668 129 VTQCSKCGRESSLPSKFYELELQLKG----HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 259 LKRFSESRIRTS--KLTTFVNFPLrDLDLREF-ASENTNHAVYNLYAVSNHSGT-TMGGHYTAYCRSPGTGEWHTFNDSS 334
Cdd:cd02668 205 LLRFVFDRKTGAkkKLNASISFPE-ILDMGEYlAESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDED 283
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 119587890 335 VTPMSSSQVR---------------------TSDAYLLFYE 354
Cdd:cd02668 284 VEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
1.03e-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: 134.77 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELRDYCLQrlYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpnDVVSPSEFKTQIQRYA 104
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN--YNPARRGANQSSDNLTNALRDLFDTMDKKQ--EPVPPIEFLQLLRMAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 PRFV------GYNQQDAQEFLRFLLDGLHNEvnrvtLRPKSnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKS 178
Cdd:cd02657 77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQK-----LPGAG-----------------------SKGSFIDQLFGIELET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 179 SLTCTDCGYCSTV-FDPFWDLSLPIAkrgypevTLMDCMRLFTK-EDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILV 256
Cdd:cd02657 129 KMKCTESPDEEEVsTESEYKLQCHIS-------ITTEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 257 LHLKRFS--ESRIRTSKLTTFVNFPLrDLDLREFAsenTNHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDS 333
Cdd:cd02657 202 VQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDD 277
|
330 340
....*....|....*....|....*...
gi 119587890 334 SVTPMSSSQVRTSD-------AYLLFYE 354
Cdd:cd02657 278 KVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
208-354 |
6.37e-32 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 126.92 E-value: 6.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 208 PEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLRE 287
Cdd:COG5560 673 RTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSG 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119587890 288 FASENTNHAV-YNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:COG5560 753 VEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
4-353 |
3.00e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 120.77 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 4 PGSTRPSSKKRQNSKSaqgLAGLRNLGNTCFMNSILQCLSntrelrdYCLQrlYMRDLHHGSNAHTALVEefaklIQTIW 83
Cdd:cd02671 8 QPSSATSCEKRENLLP---FVGLNNLGNTCYLNSVLQVLY-------FCPG--FKHGLKHLVSLISSVEQ-----LQSSF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 84 TSSPNDVVS------PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlrpksnpenldhlpddekgrqmw 157
Cdd:cd02671 71 LLNPEKYNDelanqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 158 rkyleredsrigdLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEV---------------TLMDCMRLFTKE 222
Cdd:cd02671 126 -------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFASV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 223 DVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRT------SKLTTFVNFPLrDLDLREFASENTNHa 296
Cdd:cd02671 193 ERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL-KLSLEEWSTKPKND- 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119587890 297 VYNLYAVSNHSGTTMG-GHYTAYCRspgtgeWHTFNDSSVTPM---------SSSQVRTSDAYLLFY 353
Cdd:cd02671 271 VYRLFAVVMHSGATISsGHYTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
22-354 |
7.91e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 121.66 E-value: 7.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 22 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLqrLYMRDLHHGSNAhTALVEEFAKLIQTIWtsSPND---VVSPSEFKT 98
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--LYENYENIKDRK-SELVKRLSELIRKIW--NPRNfkgHVSPHELLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 99 QIQRYAPRFVGYNQQ-DAQEFLRFLLDGLHNEVNRVTlrpKSNPENLDHLPDDEKgRQMWRKYLEREDSrigdlfvgqLK 177
Cdd:cd02669 193 AVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSK---KPNSSIIHDCFQGKV-QIETQKIKPHAEE---------EG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 178 SSLTCTDCGYCSTVFD-PFWDLSL-----PIAKRGY-----PEVTLMDcmrLFTKedvLDGDEKPTCCRCrgrkrcIKKF 246
Cdd:cd02669 260 SKDKFFKDSRVKKTSVsPFLLLTLdlpppPLFKDGNeeniiPQVPLKQ---LLKK---YDGKTETELKDS------LKRY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 247 SIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTN----HAVYNLYAVSNHSGTTMG-GHYTAYCRS 321
Cdd:cd02669 328 LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPslnlSTKYNLVANIVHEGTPQEdGTWRVQLRH 407
|
330 340 350
....*....|....*....|....*....|...
gi 119587890 322 PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:cd02669 408 KSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
25-354 |
2.44e-30 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 117.21 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLS-NTRELRDYCLQRLY----MRDLHHGSNAhTALVEEFAKLIQTIWTSspndvvspsefktQ 99
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKelkvLKNVIRKPEP-DLNQEEALKLFTALWSS-------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 100 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNE-VNRVTLRpksnpenlDHLPDDEKGRqmwrkyleredSRIGDLFvgqlks 178
Cdd:COG5533 67 EHKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIR--------IFKTTKDKKK-----------TSTGDWF------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 179 SLTctdcgycstvfdpfwdLSLPIAKRGYPEVTLMDCmrlFTKEDVLDGDEKPTCCRCRGRKRCIKK----FSIQRFPKI 254
Cdd:COG5533 122 DII----------------IELPDQTWVNNLKTLQEF---IDNMEELVDDETGVKAKENEELEVQAKqeyeVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 255 LVLHLKRFSESrIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSpgTGEWHTFNDSS 334
Cdd:COG5533 183 LTIQLKRFANL-GGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSD 259
|
330 340
....*....|....*....|...
gi 119587890 335 VTPMSSSQVRTSD---AYLLFYE 354
Cdd:COG5533 260 VTPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
1.05e-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: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELrdyclQRLYMRDLHHGSNA----HTALVEEFAKLIQTIWT---SSPNDVVS----- 92
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSF-----QWRYDDLENKFPSDvvdpANDLNCQLIKLADGLLSgrySKPASLKSendpy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 93 -----PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlRPKSNPENLdhlpddekgrqmwRKYLEREdsr 167
Cdd:cd02658 76 qvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK---NLGLNPNDL-------------FKFMIED--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 168 igdlfvgqlksSLTCTDCGYCSTVFDPFWDLSLPI----------AKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR 237
Cdd:cd02658 137 -----------RLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 238 GrkrcIKKFSIQRFPKILVLHLKRFsesrirtsklTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT-TMGGHYT 316
Cdd:cd02658 206 A----TKTTGFKTFPDYLVINMKRF----------QLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTsVHSGHYV 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 119587890 317 AYCRSP--GTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:cd02658 272 AHIKKEidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
5.32e-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: 109.76 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYmrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-LEEFL----------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 prfvgyNQQDAQEFLRFLLDGLHNEVnrvtlrpkSNPenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 184
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------KFP------------------------------FDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 185 CGYCSTV-FDPFWDLSLPI-AKRGYPEVTLMDCMRLFTKEDVLDGdekptccrcrgRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD-----------YKCDRCQTVIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 263 SESRIRTS-KLTTFVNFPLRdldlrefasenTNHAVYNLYAVSNHSGTTMGGHYTAYCRSP------------------- 322
Cdd:cd02662 138 VFDGRGTStKNSCKVSFPER-----------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 119587890 323 -GTGEWHTFNDSSVTPMSSSQVR-TSDAYLLFYE 354
Cdd:cd02662 207 sTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-354 |
4.83e-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: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 25 GLRNLGNTCFMNSILQCLSNTRelrDYCLQRLyMRDLHHGSNAHTALVEEfaKLIQTIWTSSPNDVVSPSEFKTQIQRyA 104
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAK---DFRRQVL-SLNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEAPPDYFLEASR-P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 105 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 184
Cdd:cd02664 74 PWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRCLN 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 185 CGYCSTVFD--PFWDLSLPiakrgypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02664 116 CNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 263 S---ESRIRTsKLTTFVNFPL-------------------RDLDLREFASENTNHAVYNLYAVSNHSGTTM-GGHYTAYC 319
Cdd:cd02664 187 SydqKTHVRE-KIMDNVSINEvlslpvrveskssesplekKEEESGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYFTYA 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119587890 320 RSPGTGE--------------------WHTFNDSSVTPMSSSQV-------RTSDAYLLFYE 354
Cdd:cd02664 266 RDQTDADstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
16-343 |
4.45e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 103.80 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 16 NSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRD-----------------YCLQRLY--MRDLHHGSNAhTALVEEFa 76
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvygiptdhprgrdsvaLALQRLFynLQTGEEPVDT-TELTRSF- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 77 kliqtIWTSspndvvspsefktqiqryaprFVGYNQQDAQEFLRFLLDGLHNEVNrvtlrpKSNPENLdhlpddekgrqm 156
Cdd:COG5077 264 -----GWDS---------------------DDSFMQHDIQEFNRVLQDNLEKSMR------GTVVENA------------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 157 wrkyleredsrIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYPevTLMDCMRLFTKEDVLDGDEKptCCRC 236
Cdd:COG5077 300 -----------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGDNR--YNAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 237 RGRKRCIKKFSI-QRFPKILVLHLKRFSESRIRTS--KLTTFVNFPLrDLDLREF------ASENTNHaVYNLYAVSNHS 307
Cdd:COG5077 363 KHGLQDAKKGVIfESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFldrdadKSENSDA-VYVLYGVLVHS 440
|
330 340 350
....*....|....*....|....*....|....*.
gi 119587890 308 GTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV 343
Cdd:COG5077 441 GDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-353 |
1.58e-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: 67.90 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlymrdlHHGSNAHTALVEEFAKLIqtiwtssPNDVVSPSEFKTQIQ-- 101
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLN-------FDESKAELASDYPTERRI-------GGREVSRSELQRSNQfv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 102 ---------------RYA-PR----FVGYNQQDAQEFLRFLLDGLhnevnRVTLRPKSNpENLDHLPDDEKgrqmwrkyl 161
Cdd:cd02666 68 yelrslfndlihsntRSVtPSkelaYLALRQQDVTECIDNVLFQL-----EVALEPISN-AFAGPDTEDDK--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 162 EREDsRIGDLFVGQLKSSLTCTDCGYCSTVFDP---FWDLSLPIAKRGYPEVT------LMDCM-RLFTKEDVLDGDEKP 231
Cdd:cd02666 133 EQSD-LIKRLFSGKTKQQLVPESMGNQPSVRTKterFLSLLVDVGKKGREIVVllepkdLYDALdRYFDYDSLTKLPQRS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 232 TCCRCRGRKRCIKKFSIQRF-PKILVLHLKRFSESRIRT-SKLTTFVNFPLRDLD-LREFASENTNHAVYNLYAVSNHSG 308
Cdd:cd02666 212 QVQAQLAQPLQRELISMDRYeLPSSIDDIDELIREAIQSeSSLVRQAQNELAELKhEIEKQFDDLKSYGYRLHAVFIHRG 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 119587890 309 TTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV----RTSDA--YLLFY 353
Cdd:cd02666 292 EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftLGNTAtpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
26-354 |
2.08e-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: 66.40 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 26 LRNLGNTCFMNSILQCLSNTRELRdyclqrlymrdlhhgsnahtalvEEFAkliqtiwtsspNDvvspsefktqiqryap 105
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKIN-----------------------TEFD-----------ND---------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 106 rfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKgrqmwrkyleredsrigdlFVGQLKSSLTCTDC 185
Cdd:cd02673 32 -----DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEA-------------------FKYTIESSYVCIGC 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 186 GYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDvldgdEKPTCCRCRGRKRCIKKFSiqRFPKILVLHLKRFsES 265
Cdd:cd02673 88 SFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EKDCSSCKCESAISSERIM--TFPECLSINLKRY-KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 266 RIRTSKLttfvnfpLRD--LDLREFASEntnHAVYNLYAVSNHSG-TTMGGHYTAYCRSPGTG-EWHTFNDSSVTPMSSS 341
Cdd:cd02673 160 RIATSDY-------LKKneEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
|
330
....*....|....*.
gi 119587890 342 QVR---TSDAYLLFYE 354
Cdd:cd02673 230 DVStnaRSSGYLIFYD 245
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
24-335 |
2.09e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 54.97 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 24 AGLRNLGNTCFMNSILQCLSNTRELR-------------DYCL--QRLY---MRDLHHGSNAHT-----AL--VEEFAK- 77
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCLlcELGFlfdMLEKAKGKNCQAsnflrALssIPEASAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 78 -LIQTIWTSSPNDVVSPsefktQIQRyaprfvgynqqdaqeFLRFLLDGLHNEVNRVTLRPKSNPenldhlpddekgrqm 156
Cdd:pfam13423 81 gLLDEDRETNSAISLSS-----LIQS---------------FNRFLLDQLSSEENSTPPNPSPAE--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 157 wrkyleredSRIGDLFVGQLKSSLTCTDCGYCST------VFDpfwdLSLPIAK----RGYPEVTLMDCMRLFTKEDVLd 226
Cdd:pfam13423 126 ---------SPLEQLFGIDAETTIRCSNCGHESVressthVLD----LIYPRKPssnnKKPPNQTFSSILKSSLERETT- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 227 gdEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFvnFPLR-DLDLREFASENTNHAVYNLYA-VS 304
Cdd:pfam13423 192 --TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEiGLTLSDDLQGDNEIVKYELRGvVV 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 119587890 305 NHSGTTMGGHYTAYCR-------SPGTGEWHTFNDSSV 335
Cdd:pfam13423 268 HIGDSGTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-353 |
2.25e-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: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 112 QQDAQEFLRFLLDGLHNEVNRV--TLRPKSNPENldHLPDDEKGRQMWRKYLERedsrigdlfvgqlKSSLTCTDCGycs 189
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAaeAISPGEKSKN--PMVQLFYGTFLTEGVLEG-------------KPFCNCETFG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 190 tvfdpfwdlSLPIAKRGYPEvtLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKkfsiqrFPKILVLHLKRFSESRIRT 269
Cdd:cd02665 84 ---------QYPLQVNGYGN--LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 270 SKLTTFVNFPlrdldlREFASENtnhavYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV------ 343
Cdd:cd02665 147 EKIHDKLEFP------QIIQQVP-----YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfg 215
|
250
....*....|..
gi 119587890 344 --RTSDAYLLFY 353
Cdd:cd02665 216 ggRNPSAYCLMY 227
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-354 |
1.32e-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: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587890 245 KFSIQRFPKI----LVLHLKRFSESR-------IRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYA-VSNHSGTTMG 312
Cdd:cd02672 149 TTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGyVCEINDSSRG 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119587890 313 GHYTA----YCRSPGTGEWHTFNDSSVTPMSssqvrtSDAYLLFYE 354
Cdd:cd02672 229 QHNVVfvikVNEESTHGRWYLFNDFLVTPVS------ELAYILLYQ 268
|
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