|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
267-596 |
1.00e-105 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 321.31 E-value: 1.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 267 AGLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRY 346
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDY-LLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 347 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKGSLTCT 426
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHST--------------------------ENESLITDLFRGQLKSRLKCL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 427 DCGYCSTVFDPFWDLSLPIAKRGYPEVT--LMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKR 504
Cdd:pfam00443 134 SCGEVSETFEPFSDLSLPIPGDSAELKTasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 505 FSESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVT 579
Cdd:pfam00443 214 FSYNRSTWEKLNTEVEFPL-ELDLSRYLAEELkpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVT 292
|
330
....*....|....*...
gi 16552833 580 PMS-SSQVRTSDAYLLFY 596
Cdd:pfam00443 293 EVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
1.62e-104 |
|
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: 315.00 E-value: 1.62e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 347
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 prfvgyNQQDAQEFLRFLLDGLHnevnrvtlrpksnpenldhlpddekgrqmwrkyleredSRIGDLFVGQLKGSLTCTD 427
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 428 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKRF 505
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 506 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSS 583
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 16552833 584 SQVRTSDAYLLFYE 597
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
268-597 |
1.28e-72 |
|
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: 233.53 E-value: 1.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 347
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 prfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwRKYLEREDSRIGDLFVGQLKGSLTCTD 427
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 428 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKpTCCRCRGRKRCIKKFSIQRFPKILVLRLKRFS- 506
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNC-YKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 507 ESRIRTSKLTTFVNFPLRdLDLREFASENT-------NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDSSV 578
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLE-LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKV 231
|
330 340
....*....|....*....|....
gi 16552833 579 TPMSSSQV-----RTSDAYLLFYE 597
Cdd:cd02257 232 TEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
267-596 |
3.78e-71 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 231.40 E-value: 3.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 267 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKliQTIWTSSPNDVvsPSEFKTQIQRY 346
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSA--PRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 347 APRFVGYNQQDAQEFLRFLLDGLHnevnRVTLRPKSNPENLDHlpddekgrqmwrkyLEREDSRIGDLFVGQLKGSLTCT 426
Cdd:cd02661 78 SKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDP--------------SSQETTLVQQIFGGYLRSQVKCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 427 DCGYCSTVFDPFWDLSLPIAKRGypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKRFS 506
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 507 EsrIRTSKLTTFVNFPLRdLDLREFASENT-NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPgTGEWHTFNDSSVTPMSSS 584
Cdd:cd02661 216 N--FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIE 291
|
330
....*....|..
gi 16552833 585 QVRTSDAYLLFY 596
Cdd:cd02661 292 TVLSQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-596 |
5.75e-62 |
|
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: 208.00 E-value: 5.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELRDYclqrlYMRDLHH----GSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQI 343
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNY-----FLSDRHSctclSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 344 QRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpKSNPENLDHLPddekgrqmwrkyleredSRIGDLFVGQLKGSL 423
Cdd:cd02660 77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD----KNEANDESHCN-----------------CIIHQTFSGSLQSSV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 424 TCTDCGYCSTVFDPFWDLSLPI-----------AKRGYPEVTLMDCMRLFTKEDVLdGDEKPTCCRCRGRKRCIKKFSIQ 492
Cdd:cd02660 136 TCQRCGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 493 RFPKILVLRLKRFSESRIRTS-KLTTFVNFPLRdLDLREFAS----------ENTNHAVYNLYAVSNHSGTTMGGHYTAY 561
Cdd:cd02660 215 KLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTSssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAY 293
|
330 340 350
....*....|....*....|....*....|....*
gi 16552833 562 CRSpGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFY 596
Cdd:cd02660 294 CRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
3.91e-57 |
|
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: 193.76 E-value: 3.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRlymrdlhhgsnahtalveefakliqtiwtsspndvvsPSEFKTQIQRYA 347
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------------------------------PKELFSQVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKGSLTCTD 427
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 428 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKptcCRCRGRKRCIKKFSIQRFPKILVLRLKRFS- 506
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 507 ESRIRTSKLTTFVNFPLRdLDLREFASENTNHA------VYNLYAVSNHSGTTMGGHYTAYCRS---------------- 564
Cdd:cd02667 163 PRSANLRKVSRHVSFPEI-LDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 16552833 565 -----PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 597
Cdd:cd02667 242 adeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
265-445 |
2.04e-46 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 175.46 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 265 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDL----HHGSNAHTALVeeFAKLIQTIWTSSpNDVVSPSEFK 340
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESIneenPLGMHGSVASA--YADLIKQLYDGN-LHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 341 TQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENL---DHLPDDEKGRQMWRKYLEREDSRIGDLFVG 417
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLspgDDVVVKKKAKECWWEHLKRNDSIITDLFQG 420
|
170 180
....*....|....*....|....*...
gi 16552833 418 QLKGSLTCTDCGYCSTVFDPFWDLSLPI 445
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
265-601 |
4.83e-41 |
|
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: 151.64 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 265 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlyMRDLHHGSNAH---TALVEEFAKLiQTiwtsSPNDVVSPSEFKT 341
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYS---IPPTEDDDDNKsvpLALQRLFLFL-QL----SESPVKTTELTDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 342 QiqryapRFVG------YNQQDAQEFLRFLLDglhnevnrvtlrpksnpeNLDHlpddekgrqMWrKYLEREDSrIGDLF 415
Cdd:cd02659 73 T------RSFGwdslntFEQHDVQEFFRVLFD------------------KLEE---------KL-KGTGQEGL-IKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 416 VGQLKGSLTCTDCGYCSTVFDPFWDLSLPIakRGYpeVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFP 495
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAV--KGK--KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 496 KILVLRLKRF-----SESRIrtsKLTTFVNFPLRdLDLREFASENTNH------------AVYNLYAVSNHSGTTMGGHY 558
Cdd:cd02659 194 PVLTLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYTEKGLAKkegdsekkdsesYIYELHGVLVHSGDAHGGHY 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16552833 559 TAYCRSPGTGEWHTFNDSSVTPMSSSQV----------------------RTSDAYLLFYELASP 601
Cdd:cd02659 270 YSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYERKSP 334
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
7.89e-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: 139.86 E-value: 7.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELRDY-----CLQRLYMRDLHHGSNAH-TALVEEFAKLIQTIWTSSPNdVVSPSEFKT 341
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAvyecnSTEDAELKNMPPDKPHEpQTIIDQLQLIFAQLQFGNRS-VVDPSGFVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 342 qiqryAPRFVGYNQQDAQEFLRFLLDGLHNevnrvTLRPKSNPenldhlpddeKGRQMwrkyleredsrIGDLFVGQLKG 421
Cdd:cd02668 80 -----ALGLDTGQQQDAQEFSKLFLSLLEA-----KLSKSKNP----------DLKNI-----------VQDLFRGEYSY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 422 SLTCTDCGYCSTVFDPFWDLSLPIAKrgypEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLR 501
Cdd:cd02668 129 VTQCSKCGRESSLPSKFYELELQLKG----HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 502 LKRFSESRIRTS--KLTTFVNFPLrDLDLREF-ASENTNHAVYNLYAVSNHSGT-TMGGHYTAYCRSPGTGEWHTFNDSS 577
Cdd:cd02668 205 LLRFVFDRKTGAkkKLNASISFPE-ILDMGEYlAESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDED 283
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 16552833 578 VTPMSSSQVR---------------------TSDAYLLFYE 597
Cdd:cd02668 284 VEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
4.26e-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 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: 137.06 E-value: 4.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELrdYCLqrlymRDLHHGSNAHTALVeefakliqtiwtsspnDVVSPSEFKTQIQRYA 347
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL--TCL-----KDLFESISEQKKRT----------------GVISPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLR-PKSNPENLDHLPDDEKGrqmWrkyleredsrIGDLFVGQLkgsLTCT 426
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLLNEIAEILDAERKAeKANRKLNNNNNAEPQPT---W----------VHEIFQGIL---TNET 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 427 DCGYCSTVFD---PFWDLSLPIakrgYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLK 503
Cdd:cd02663 122 RCLTCETVSSrdeTFLDLSIDV----EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 504 RF--SESRIRTSKLTTFVNFPlrdLDLREFASENTNHAV---YNLYAVSNHSGTT-MGGHYTAYCRSpgTGEWHTFNDSS 577
Cdd:cd02663 198 RFkyDEQLNRYIKLFYRVVFP---LELRLFNTTDDAENPdrlYELVAVVVHIGGGpNHGHYVSIVKS--HGGWLLFDDET 272
|
330 340
....*....|....*....|....*...
gi 16552833 578 VTPMSSSQV-------RTSD-AYLLFYE 597
Cdd:cd02663 273 VEKIDENAVeeffgdsPNQAtAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
5.51e-34 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 131.30 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELRDYCLQrlYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpnDVVSPSEFKTQIQRYA 347
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN--YNPARRGANQSSDNLTNALRDLFDTMDKKQ--EPVPPIEFLQLLRMAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 PRFV------GYNQQDAQEFLRFLLDGLHNEvnrvtLRPKSnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKG 421
Cdd:cd02657 77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQK-----LPGAG-----------------------SKGSFIDQLFGIELET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 422 SLTCTDCGYCSTV-FDPFWDLSLPIAkrgypevTLMDCMRLFTK-EDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILV 499
Cdd:cd02657 129 KMKCTESPDEEEVsTESEYKLQCHIS-------ITTEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 500 LRLKRFS--ESRIRTSKLTTFVNFPLrDLDLREFAsenTNHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDS 576
Cdd:cd02657 202 VQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDD 277
|
330 340
....*....|....*....|....*...
gi 16552833 577 SVTPMSSSQVRTSD-------AYLLFYE 597
Cdd:cd02657 278 KVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
248-597 |
1.18e-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: 124.74 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 248 SRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLqrLYMRDLHHGSNAhTALVEEFAKLIQTIWt 327
Cdd:cd02669 101 DRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--LYENYENIKDRK-SELVKRLSELIRKIW- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 328 sSPND---VVSPSEFKTQIQRYAPRFVGYNQQ-DAQEFLRFLLDGLHNEVNRVTlrpKSNPENLDHLPDDEKgRQMWRKY 403
Cdd:cd02669 177 -NPRNfkgHVSPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSK---KPNSSIIHDCFQGKV-QIETQKI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 404 LEREDSrigdlfVGQLKGSLTCTDCGycSTVFDPFWDLSL-----PIAKRGY-----PEVTLMDcmrLFTKedvLDGDEK 473
Cdd:cd02669 252 KPHAEE------EGSKDKFFKDSRVK--KTSVSPFLLLTLdlpppPLFKDGNeeniiPQVPLKQ---LLKK---YDGKTE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 474 PTCCRCrgrkrcIKKFSIQRFPKILVLRLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTN----HAVYNLYAVSNH 549
Cdd:cd02669 318 TELKDS------LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPslnlSTKYNLVANIVH 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16552833 550 SGTTMG-GHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 597
Cdd:cd02669 392 EGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
451-597 |
1.33e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 124.61 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 451 PEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKRFSESRIRTSKLTTFVNFPLRDLDLRE 530
Cdd:COG5560 673 RTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSG 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16552833 531 FASENTNHAV-YNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 597
Cdd:COG5560 753 VEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
268-597 |
3.87e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 117.21 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLS-NTRELRDYCLQRLY----MRDLHHGSNAhTALVEEFAKLIQTIWTSspndvvspsefktQ 342
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKelkvLKNVIRKPEP-DLNQEEALKLFTALWSS-------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 343 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNE-VNRVTLRpksnpenlDHLPDDEKGRqmwrkyleredSRIGDLFvgqlkg 421
Cdd:COG5533 67 EHKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIR--------IFKTTKDKKK-----------TSTGDWF------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 422 SLTctdcgycstvfdpfwdLSLPIAKRGYPEVTLMDCmrlFTKEDVLDGDEKPTCCRCRGRKRCIKK----FSIQRFPKI 497
Cdd:COG5533 122 DII----------------IELPDQTWVNNLKTLQEF---IDNMEELVDDETGVKAKENEELEVQAKqeyeVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 498 LVLRLKRFSESrIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSpgTGEWHTFNDSS 577
Cdd:COG5533 183 LTIQLKRFANL-GGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSD 259
|
330 340
....*....|....*....|...
gi 16552833 578 VTPMSSSQVRTSD---AYLLFYE 597
Cdd:COG5533 260 VTPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
244-596 |
1.59e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 116.53 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 244 APGPSRSSSP-GRDGMNSksaqgLAGLRNLGNTCFMNSILQCLSntrelrdYCLQrlYMRDLHHGSNAHTALVEefaklI 322
Cdd:cd02671 6 APQPSSATSCeKRENLLP-----FVGLNNLGNTCYLNSVLQVLY-------FCPG--FKHGLKHLVSLISSVEQ-----L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 323 QTIWTSSPNDVVS------PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlrpksnpenldhlpddekg 396
Cdd:cd02671 67 QSSFLLNPEKYNDelanqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 397 rqmwrkyleredsrigdLFVGQLKGSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEV---------------TLMDCMRL 461
Cdd:cd02671 126 -----------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 462 FTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKRFSESRIRT------SKLTTFVNFPLrDLDLREFASEN 535
Cdd:cd02671 189 FASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL-KLSLEEWSTKP 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16552833 536 TNHaVYNLYAVSNHSGTTMG-GHYTAYCRspgtgeWHTFNDSSVTPM---------SSSQVRTSDAYLLFY 596
Cdd:cd02671 268 KND-VYRLFAVVMHSGATISsGHYTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
5.77e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 114.34 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELrdyclQRLYMRDLHHGSNA----HTALVEEFAKLIQTIWT---SSPNDVVS----- 335
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSF-----QWRYDDLENKFPSDvvdpANDLNCQLIKLADGLLSgrySKPASLKSendpy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 336 -----PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlRPKSNPENLdhlpddekgrqmwRKYLEREdsr 410
Cdd:cd02658 76 qvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK---NLGLNPNDL-------------FKFMIED--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 411 igdlfvgqlkgSLTCTDCGYCSTVFDPFWDLSLPI----------AKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR 480
Cdd:cd02658 137 -----------RLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 481 GrkrcIKKFSIQRFPKILVLRLKRFsesrirtsklTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT-TMGGHYT 559
Cdd:cd02658 206 A----TKTTGFKTFPDYLVINMKRF----------QLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTsVHSGHYV 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 16552833 560 AYCRSP--GTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 597
Cdd:cd02658 272 AHIKKEidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
6.75e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 106.68 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYmrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 347
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-LEEFL----------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 prfvgyNQQDAQEFLRFLLDGLHNEVnrvtlrpkSNPenldhlpddekgrqmwrkyleredsrigdlFVGQLKGSLTCTD 427
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------KFP------------------------------FDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 428 CGYCSTV-FDPFWDLSLPI-AKRGYPEVTLMDCMRLFTKEDVLDGDEKptccrcrgrkrCIKKFSIQRFPKILVLRLKRF 505
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDDYKC-----------DRCQTVIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 506 SESRIRTS-KLTTFVNFPLRdldlrefasenTNHAVYNLYAVSNHSGTTMGGHYTAYCRSP------------------- 565
Cdd:cd02662 138 VFDGRGTStKNSCKVSFPER-----------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 16552833 566 -GTGEWHTFNDSSVTPMSSSQVR-TSDAYLLFYE 597
Cdd:cd02662 207 sTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-597 |
4.04e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 106.42 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 268 GLRNLGNTCFMNSILQCLSNTRelrDYCLQRLyMRDLHHGSNAHTALVEEfaKLIQTIWTSSPNDVVSPSEFKTQIQRyA 347
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAK---DFRRQVL-SLNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEAPPDYFLEASR-P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 348 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKGSLTCTD 427
Cdd:cd02664 74 PWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRCLN 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 428 CGYCSTVFD--PFWDLSLPiakrgypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKRF 505
Cdd:cd02664 116 CNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 506 S---ESRIRTsKLTTFVNFPLrDLDL--------------------REFASENTNHAVYNLYAVSNHSGTTM-GGHYTAY 561
Cdd:cd02664 187 SydqKTHVRE-KIMDNVSINE-VLSLpvrveskssesplekkeeesGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYFTY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16552833 562 CRSPGTGE--------------------WHTFNDSSVTPMSSSQV-------RTSDAYLLFYE 597
Cdd:cd02664 265 ARDQTDADstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
259-586 |
9.32e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 106.49 E-value: 9.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 259 NSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRD-----------------YCLQRLY--MRDLHHGSNAhTALVEEFa 319
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvygiptdhprgrdsvaLALQRLFynLQTGEEPVDT-TELTRSF- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 320 kliqtIWTSspndvvspsefktqiqryaprFVGYNQQDAQEFLRFLLDGLHNEVNrvtlrpKSNPENLdhlpddekgrqm 399
Cdd:COG5077 264 -----GWDS---------------------DDSFMQHDIQEFNRVLQDNLEKSMR------GTVVENA------------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 400 wrkyleredsrIGDLFVGQLKGSLTCTDCGYCSTVFDPFWDLSLPIakRGYPevTLMDCMRLFTKEDVLDGDEKptCCRC 479
Cdd:COG5077 300 -----------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGDNR--YNAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 480 RGRKRCIKKFSI-QRFPKILVLRLKRFSESRIRTS--KLTTFVNFPLrDLDLREF------ASENTNHaVYNLYAVSNHS 550
Cdd:COG5077 363 KHGLQDAKKGVIfESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFldrdadKSENSDA-VYVLYGVLVHS 440
|
330 340 350
....*....|....*....|....*....|....*.
gi 16552833 551 GTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV 586
Cdd:COG5077 441 GDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
267-596 |
1.38e-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: 69.44 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 267 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlymrdlHHGSNAHTALVEEFAKLIqtiwtssPNDVVSPSEFKTQIQ-- 344
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLN-------FDESKAELASDYPTERRI-------GGREVSRSELQRSNQfv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 345 ---------------RYA-PR----FVGYNQQDAQEFLRFLLDGLhnevnRVTLRPKSNpENLDHLPDDEKgrqmwrkyl 404
Cdd:cd02666 68 yelrslfndlihsntRSVtPSkelaYLALRQQDVTECIDNVLFQL-----EVALEPISN-AFAGPDTEDDK--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 405 EREDsRIGDLFVGQLKGSLTCTDCGYCSTVFDP---FWDLSLPIAKRGYPEVT------LMDCM-RLFTKEDVLDGDEKP 474
Cdd:cd02666 133 EQSD-LIKRLFSGKTKQQLVPESMGNQPSVRTKterFLSLLVDVGKKGREIVVllepkdLYDALdRYFDYDSLTKLPQRS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 475 TCCRCRGRKRCIKKFSIQRF-PKILVLRLKRFSESRIRT-SKLTTFVNFPLRDLD-LREFASENTNHAVYNLYAVSNHSG 551
Cdd:cd02666 212 QVQAQLAQPLQRELISMDRYeLPSSIDDIDELIREAIQSeSSLVRQAQNELAELKhEIEKQFDDLKSYGYRLHAVFIHRG 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 16552833 552 TTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV----RTSDA--YLLFY 596
Cdd:cd02666 292 EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftLGNTAtpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-597 |
2.02e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 64.47 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 269 LRNLGNTCFMNSILQCLSNTRELRdyclqrlymrdlhhgsnahtalvEEFAkliqtiwtsspNDvvspsefktqiqryap 348
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKIN-----------------------TEFD-----------ND---------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 349 rfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRqmwrkyLEREDSRIgdlfvgqlkgsltCTDC 428
Cdd:cd02673 32 -----DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEAFK------YTIESSYV-------------CIGC 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 429 GYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDvldgdEKPTCCRCRGRKRCIKKFSiqRFPKILVLRLKRFsES 508
Cdd:cd02673 88 SFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EKDCSSCKCESAISSERIM--TFPECLSINLKRY-KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 509 RIRTSKLttfvnfpLRD--LDLREFASEntnHAVYNLYAVSNHSG-TTMGGHYTAYCRSPGTG-EWHTFNDSSVTPMSSS 584
Cdd:cd02673 160 RIATSDY-------LKKneEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
|
330
....*....|....*.
gi 16552833 585 QVR---TSDAYLLFYE 597
Cdd:cd02673 230 DVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
355-596 |
1.42e-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: 55.64 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 355 QQDAQEFLRFLLDGLHNEVNrvtlrPKSNpenlDHLPDDEKGRQMWRKYLEREdsrigdLFVGQLKGSLTCTdcgyCSTV 434
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQ-----AAAE----AISPGEKSKNPMVQLFYGTF------LTEGVLEGKPFCN----CETF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 435 FDpfwdlsLPIAKRGYPEvtLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKkfsiqrFPKILVLRLKRFSESRIRTSK 514
Cdd:cd02665 83 GQ------YPLQVNGYGN--LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 515 LTTFVNFPlrdldlREFASENtnhavYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV-------- 586
Cdd:cd02665 149 IHDKLEFP------QIIQQVP-----YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfggg 217
|
250
....*....|
gi 16552833 587 RTSDAYLLFY 596
Cdd:cd02665 218 RNPSAYCLMY 227
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
267-578 |
4.06e-07 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 52.27 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 267 AGLRNLGNTCFMNSILQCLSNTRELR-------------DYCL--QRLY---MRDLHHGSNAHT-----AL--VEEFAK- 320
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCLlcELGFlfdMLEKAKGKNCQAsnflrALssIPEASAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 321 -LIQTIWTSSPNDVVSPsefktQIQRyaprfvgynqqdaqeFLRFLLDGLHNEVNRVTLRPKSNPenldhlpddekgrqm 399
Cdd:pfam13423 81 gLLDEDRETNSAISLSS-----LIQS---------------FNRFLLDQLSSEENSTPPNPSPAE--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 400 wrkyleredSRIGDLFVGQLKGSLTCTDCGYCST------VFDpfwdLSLPIAK----RGYPEVTLMDCMRLFTKEDVLd 469
Cdd:pfam13423 126 ---------SPLEQLFGIDAETTIRCSNCGHESVressthVLD----LIYPRKPssnnKKPPNQTFSSILKSSLERETT- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 470 gdEKPTCCRCRGRKRCIKKFSIQRFPKILVLRLKRFSESRIRTSKLTTFvnFPLR-DLDLREFASENTNHAVYNLYA-VS 547
Cdd:pfam13423 192 --TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEiGLTLSDDLQGDNEIVKYELRGvVV 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 16552833 548 NHSGTTMGGHYTAYCR-------SPGTGEWHTFNDSSV 578
Cdd:pfam13423 268 HIGDSGTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
488-597 |
9.51e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 47.51 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16552833 488 KFSIQRFPKILVLRLKR-----------FSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYA-VSNHSGTTMG 555
Cdd:cd02672 149 TTSIRHLPDILLLVLVInlsvtngefddINVVLPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGyVCEINDSSRG 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 16552833 556 GHYTA----YCRSPGTGEWHTFNDSSVTPMSssqvrtSDAYLLFYE 597
Cdd:cd02672 229 QHNVVfvikVNEESTHGRWYLFNDFLVTPVS------ELAYILLYQ 268
|
|
| |
