|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
212-555 |
4.29e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 305.52 E-value: 4.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 212 VGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYV 291
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 292 PSFSGYSQQDAQEFLKLLMERLHLEINRRgrrappilasgpvpspprrggalheepelsdddranlmwkrYLEREDSKIV 371
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGN-----------------------------------------HSTENESLIT 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 372 DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLT 451
Cdd:pfam00443 120 DLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 452 VQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQ----RLSLGDFASDKVGSPVYQLYALCNHSGSVHYGHYTALCRCQT 527
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEldlsRYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYE 279
|
330 340 350
....*....|....*....|....*....|.
gi 189083712 528 G--WHVYNDSRVSPVS-ENQVASSEGYVLFY 555
Cdd:pfam00443 280 NnrWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
1.11e-85 |
|
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: 265.31 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 293 sfsgysQQDAQEFLKLLMERLHleinrrgrrappilasgpvpspprrggalheepelsdddranlmwkryleredSKIVD 372
Cdd:cd02674 22 ------QQDAQEFLLFLLDGLH-----------------------------------------------------SIIVD 42
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 373 LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLTV 452
Cdd:cd02674 43 LFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTI 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 453 QRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQRLSLGDF--ASDKVGSPVYQLYALCNHSGSVHYGHYTALCRCQ--TG 528
Cdd:cd02674 123 SRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNetND 202
|
330 340
....*....|....*....|....*...
gi 189083712 529 WHVYNDSRVSPVSENQVASSEGYVLFYQ 556
Cdd:cd02674 203 WYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
211-555 |
1.73e-70 |
|
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: 228.70 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 211 HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQE--VPGGGRAQELtEAFadVIGALWHPDSCEAVNPtrFRAVFQ 288
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDccNEGFCMMCAL-EAH--VERALASSGPGSAPRI--FSSNLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 289 KYVPSFSGYSQQDAQEFLKLLMERLHleinrrgrrappilasgpvPSPPRRGGALHEEPELSdddranlmwkryleREDS 368
Cdd:cd02661 76 QISKHFRIGRQEDAHEFLRYLLDAMQ-------------------KACLDRFKKLKAVDPSS--------------QETT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 369 KIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGfaggkvSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTK 448
Cdd:cd02661 123 LVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD------SLEDALEQFTKPEQLDGENKYKCERCKKKVKASK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 449 KLTVQRFPRILVLHLNRFSTSRGSikKSSVGVDFPlQRLSLGDFASDKV-GSPVYQLYALCNHSG-SVHYGHYTALCRCQ 526
Cdd:cd02661 197 QLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYMSQPNdGPLKYKLYAVLVHSGfSPHSGHYYCYVKSS 273
|
330 340 350
....*....|....*....|....*....|
gi 189083712 527 TG-WHVYNDSRVSPVSENQVASSEGYVLFY 555
Cdd:cd02661 274 NGkWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
213-556 |
2.62e-64 |
|
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: 210.80 E-value: 2.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSStrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 293 sfsgySQQDAQEFLKLLMERLHLEINRRGRRappilasgpvpspprrggalheepelsdddranlmwKRYLEREDSKIVD 372
Cdd:cd02257 21 -----EQQDAHEFLLFLLDKLHEELKKSSKR------------------------------------TSDSSSLKSLIHD 59
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 373 LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGfaGGKVSLRDCFSLFTKEEELESENAPVCDRCRqKTRSTKKLTV 452
Cdd:cd02257 60 LFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKG--LPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKI 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 453 QRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPLQ------RLSLGDFASDKVGSPVYQLYALCNHSG-SVHYGHYTALCR 524
Cdd:cd02257 137 KKLPPVLIIHLKRFSfNEDGTKEKLNTKVSFPLEldlspyLSEGEKDSDSDNGSYKYELVAVVVHSGtSADSGHYVAYVK 216
|
330 340 350
....*....|....*....|....*....|....*....
gi 189083712 525 CQT--GWHVYNDSRVSPVSENQV-----ASSEGYVLFYQ 556
Cdd:cd02257 217 DPSdgKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
3.68e-53 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 182.20 E-value: 3.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRrdfrqevpgggraqelteafadvigalwhpdsceavNPTRFRAVFQKYVP 292
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------TPKELFSQVCRKAP 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 293 SFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilasgpvpspprrggalheepelsdddranlmwkryleredskivd 372
Cdd:cd02667 45 QFKGYQQQDSHELLRYLLDGLRTFIDS----------------------------------------------------- 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 373 LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFagGKVSLRDCFSLFTKEEELESENAPVCDRCrqkTRSTKKLTV 452
Cdd:cd02667 72 IFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK--SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLI 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 453 QRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPlQRLSLGDFASDKVGSP------VYQLYALCNHSGSVHYGHYTALCRC 525
Cdd:cd02667 147 SKLPPVLVIHLKRFQqPRSANLRKVSRHVSFP-EILDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 189083712 526 -----------------------QTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 556
Cdd:cd02667 226 rppqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-555 |
1.15e-52 |
|
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: 182.57 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRrDFRQEVPGGGRAQ-----ELTEAFADvigaLWHPDSCEAVNPTRFRAVF 287
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS-DRHSCTCLSCSPNsclscAMDEIFQE----FYYSGDRSPYGPINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 288 QKYVPSFSGYSQQDAQEFLKLLMERLHleiNRRGRRAPPILASGPVPSPPRRggalheepelsdddranlmwkrylered 367
Cdd:cd02660 77 WKHSRNLAGYSQQDAHEFFQFLLDQLH---THYGGDKNEANDESHCNCIIHQ---------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 368 skivdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIP----KKGFAGGKV-----SLRDCFSLFTKEEELESeNAPVCD 438
Cdd:cd02660 126 -----TFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnkstPSWALGESGvsgtpTLSDCLDRFTRPEKLGD-FAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 439 RCRQKTRSTKKLTVQRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPLQrLSLGDFASDKVGSP----------VYQLYAL 507
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKTSRKIDTYVQFPLE-LNMTPYTSSSIGDTqdsnsldpdyTYDLFAV 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 189083712 508 CNHSGSVHYGHYTALCRCQTG-WHVYNDSRVSPVSENQVASSEGYVLFY 555
Cdd:cd02660 279 VVHKGTLDTGHYTAYCRQGDGqWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
148-407 |
1.85e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 156.97 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 148 PPTLRRSTSLRRLGGFPGPPTLLSIRTEPPPSHGSFHMISarPSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVL 227
Cdd:COG5560 204 DSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRN--PDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 228 QCLSSTRPLRDFCLRRDFRQEV----PGGGRAQeLTEAFADVIGALWHPDScEAVNPTRFRAVFQKYVPSFSGYSQQDAQ 303
Cdd:COG5560 282 QCLMHTWELRDYFLSDEYEESIneenPLGMHGS-VASAYADLIKQLYDGNL-HAFTPSGFKKTIGSFNEEFSGYDQQDSQ 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 304 EFLKLLMERLHLEINRRGRRappilasgPVPSPPrrggALHEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLK 383
Cdd:COG5560 360 EFIAFLLDGLHEDLNRIIKK--------PYTSKP----DLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLT 427
|
250 260
....*....|....*....|....
gi 189083712 384 CQACGYRSTTFEVFCDLSLPIPKK 407
Cdd:COG5560 428 CPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
8.36e-40 |
|
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: 147.07 E-value: 8.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSstrplrdfclrrdfrqevpgggrAQELTEAFADVIGALWHPDSCEAV-NPTRFRAVFQKYV 291
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-----------------------FENLLTCLKDLFESISEQKKRTGViSPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 292 PSFSGYSQQDAQEFLKLLMERLhLEINRRGRRAppilasgpvpspprrggalheepELSDDDRANLMwkrylEREDSK-- 369
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLLNEI-AEILDAERKA-----------------------EKANRKLNNNN-----NAEPQPtw 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 370 IVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKgfaggkVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKK 449
Cdd:cd02663 109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 450 LTVQRFPRILVLHLNRF--STSRGSIKKSSVGVDFPLQ-RL-SLGDFASDkvGSPVYQLYALCNHSGS-VHYGHYTALCR 524
Cdd:cd02663 183 MKIKKLPKILALHLKRFkyDEQLNRYIKLFYRVVFPLElRLfNTTDDAEN--PDRLYELVAVVVHIGGgPNHGHYVSIVK 260
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 189083712 525 CQTGWHVYNDSRVSPVSENQV--------ASSEGYVLFYQ 556
Cdd:cd02663 261 SHGGWLLFDDETVEKIDENAVeeffgdspNQATAYVLFYQ 300
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
210-558 |
9.61e-33 |
|
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: 128.14 E-value: 9.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 210 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPG-GGRAQELTEAFAdvigaLWHPDSCEAVNPTRFRAVFQ 288
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDnKSVPLALQRLFL-----FLQLSESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 289 KYVPSFSGYSQQDAQEFLKLLMERLhleinrrgrrappilasgpvpspprrggalhEEpelsdddranlMWKRyLEREDS 368
Cdd:cd02659 76 FGWDSLNTFEQHDVQEFFRVLFDKL-------------------------------EE-----------KLKG-TGQEGL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 369 kIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPkkgfagGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTK 448
Cdd:cd02659 113 -IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK------GKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 449 KLTVQRFPRILVLHLNRFSTS--RGSIKKSSVGVDFPLQ-----------RLSLGDFASDKVGSPVYQLYALCNHSGSVH 515
Cdd:cd02659 186 GVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLEldmepytekglAKKEGDSEKKDSESYIYELHGVLVHSGDAH 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083712 516 YGHYTALCRCQTG--WHVYNDSRVSPVSENQVA----------------------SSEGYVLFYQLM 558
Cdd:cd02659 266 GGHYYSYIKDRDDgkWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
1.54e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 121.83 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRplrDFclRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPT--RFRAVFQky 290
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAK---DF--RRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPdyFLEASRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 291 vPSFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilasgpvpspprrggalheepelsdddranlmwkryleredski 370
Cdd:cd02664 74 -PWFTPGSQQDCSEYLRYLLDRLHTLIEK--------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 371 vdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPkkgfaggkvSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKL 450
Cdd:cd02664 102 --MFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEM 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 451 TVQRFPRILVLHLNRFSTSRG---------------------SIKKSSVGVDFPLQRLSLGDFASDKVGSPVYQLYALCN 509
Cdd:cd02664 171 KVTGAPEYLILTLLRFSYDQKthvrekimdnvsinevlslpvRVESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVVV 250
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083712 510 HSG-SVHYGHYTALCRCQTG----------------------WHVYNDSRVSPVSENQV-------ASSEGYVLFYQ 556
Cdd:cd02664 251 HSGySSESGHYFTYARDQTDadstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-555 |
2.99e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 120.99 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIG------ALWHPDSCEAVNPTRF-RA 285
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDqlqlifAQLQFGNRSVVDPSGFvKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 286 VfqkyvpSFSGYSQQDAQEFLKLLMERLhleinrrgrrappilasgpvpspprrggalheEPELSDDDRANLmwkryler 365
Cdd:cd02668 81 L------GLDTGQQQDAQEFSKLFLSLL--------------------------------EAKLSKSKNPDL-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 366 edSKIV-DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIpkKGFAggkvSLRDCFSLFTKEEELESENAPVCDRCRQKT 444
Cdd:cd02668 115 --KNIVqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--KGHK----TLEECIDEFLKEEQLTGDNQYFCESCNSKT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 445 RSTKKLTVQRFPRILVLHLNRFSTSR--GSIKKSSVGVDFPLQrLSLGDFASD-KVGSPVYQLYALCNHSG-SVHYGHYT 520
Cdd:cd02668 187 DATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLNASISFPEI-LDMGEYLAEsDEGSYVYELSGVLIHQGvSAYSGHYI 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083712 521 A-LCRCQTG-WHVYNDSRVSPVSENQV---------------------ASSEGYVLFY 555
Cdd:cd02668 266 AhIKDEQTGeWYKFNDEDVEEMPGKPLklgnsedpakprkseikkgthSSRTAYMLVY 323
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
3.05e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 120.51 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRPL--RDFCLRRDFRQEV--PgggrAQELTEAFADVIGAL-------------WHPDSC 275
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVvdP----ANDLNCQLIKLADGLlsgryskpaslksENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 276 EAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPpilasgpvpspprrggalheepelsdddra 355
Cdd:cd02658 77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNP------------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 356 nlmwkryleredSKIVDLFVGQLkscLKCQACGYRSTTFEVFCDLSLPIPK--KGFAG------GKVSLRDCFSLFTKEE 427
Cdd:cd02658 127 ------------NDLFKFMIEDR---LECLSCKKVKYTSELSEILSLPVPKdeATEKEegelvyEPVPLEDCLKAYFAPE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 428 ELESEnapvCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSI-KKSSVGVDFPlqrlslgdfasDKVGSPVYQLYA 506
Cdd:cd02658 192 TIEDF----CSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVpKKLDVPIDVP-----------EELGPGKYELIA 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 189083712 507 LCNHSG-SVHYGHYTALCR----CQTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 556
Cdd:cd02658 257 FISHKGtSVHSGHYVAHIKkeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-555 |
5.11e-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 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: 113.97 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRPLRDfCLRRDFRQEVPGGGRAQELTEAFADVIGALwhPDSCEAVNPTRFRAVFQKYVP 292
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRD-ALKNYNPARRGANQSSDNLTNALRDLFDTM--DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 293 SFS------GYSQQDAQEFLKLLMERLhleinrrgRRAPPILAsgpvpspprrggalheepelsdddranlmwkryleRE 366
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVL--------SQKLPGAG-----------------------------------SK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 367 DSKIVDLFVGQLKSCLKCQACGY-RSTTFEVFCDLSLPIpkkgfaGGKVslrDCFSLFTK-EEELESENAPVCDRCRQKT 444
Cdd:cd02657 115 GSFIDQLFGIELETKMKCTESPDeEEVSTESEYKLQCHI------SITT---EVNYLQDGlKKGLEEEIEKHSPTLGRDA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 445 RSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSV--GVDFPLQrLSLGDFASdkvGSPVYQLYALCNHSG-SVHYGHYTA 521
Cdd:cd02657 186 IYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIlrKVKFPFE-LDLYELCT---PSGYYELVAVITHQGrSADSGHYVA 261
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 189083712 522 LCRCQTG--WHVYNDSRVSPVSENQVASSEG-------YVLFY 555
Cdd:cd02657 262 WVRRKNDgkWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
402-556 |
5.31e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 119.22 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 402 LPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGVD 481
Cdd:COG5560 663 WTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVE 742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083712 482 FPLQRLSLGDFASDKVGSPV-YQLYALCNHSGSVHYGHYTALCR--CQTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 556
Cdd:COG5560 743 YPIDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARnfANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
1.38e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 105.53 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFClrrdfrqevpgggraQELTEafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------EEFLE-------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 293 sfsgysQQDAQEFLKLLMERLHLEinrrgrrappilasgpvPSPPRRGgalheepelsdddranLMWKRyleredskivd 372
Cdd:cd02662 34 ------QQDAHELFQVLLETLEQL-----------------LKFPFDG----------------LLASR----------- 63
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 373 lfvgqlkscLKCQACGYRST-TFEVFCDLSLPIPKKGFAGGkVSLRDCFSLFTKEEELESenaPVCDRCrqktrstkKLT 451
Cdd:cd02662 64 ---------IVCLQCGESSKvRYESFTMLSLPVPNQSSGSG-TTLEHCLDDFLSTEIIDD---YKCDRC--------QTV 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 452 VQRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPLqRLSlgdfasdkvgSPVYQLYALCNHSGSVHYGHYTALCR------ 524
Cdd:cd02662 123 IVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFPE-RLP----------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfsk 191
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 189083712 525 --------------CQTG--WHVYNDSRVSPVSENQV-ASSEGYVLFYQ 556
Cdd:cd02662 192 dkepgsfvrmregpSSTShpWWRISDTTVKEVSESEVlEQKSAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
212-555 |
5.89e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 105.75 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 212 VGLRNLGNTCFLNAVLQCLSstrplrdFClrRDFRQEVP---GGGRAQELTEAFADVIGALWHpDSCEAVNPTRFRAVFQ 288
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLY-------FC--PGFKHGLKhlvSLISSVEQLQSSFLLNPEKYN-DELANQAPRRLLNALR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 289 KYVPSFSGYSQQDAQEFLKLLMERLHleinrrgrrappilasgpvpspprrggalheepelsdddraNLMWKrylereds 368
Cdd:cd02671 95 EVNPMYEGYLQHDAQEVLQCILGNIQ-----------------------------------------ELVEK-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 369 kivdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVS-------------LRDCFSLFTKEEELESENAP 435
Cdd:cd02671 126 ----DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESseispdpktemktLKWAISQFASVERIVGEDKY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 436 VCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSR------GSIKKSSVGVDFPLqRLSLGDFaSDKVGSPVYQLYALCN 509
Cdd:cd02671 202 FCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefdcyGGLSKVNTPLLTPL-KLSLEEW-STKPKNDVYRLFAVVM 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 189083712 510 HSG-SVHYGHYTALCRcqtgWHVYNDSRV---------SPVSENQVASSEGYVLFY 555
Cdd:cd02671 280 HSGaTISSGHYTAYVR----WLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
213-555 |
6.18e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 101.80 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTRP------LRDFCLRRDFRQEVPGGGRAQELTEAFAdVIGALWHPDSceavnptrfrav 286
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldellDDLSKELKVLKNVIRKPEPDLNQEEALK-LFTALWSSKE------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 287 fQKYVPSFSGYSQQDAQEFLKLLMERLHLE-INRRGRRAPPILAsgpvpspprrggalhEEPELSDDDRANLmwkrYLER 365
Cdd:COG5533 68 -HKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIRIFKTTK---------------DKKKTSTGDWFDI----IIEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 366 EDSKIVDlfvgqlksclkcqacgyRSTTFEVFCDL--SLPIPKKGfaggkvslrdcfslfTKEEELESENApvcdRCRQK 443
Cdd:COG5533 128 PDQTWVN-----------------NLKTLQEFIDNmeELVDDETG---------------VKAKENEELEV----QAKQE 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 444 TRSTKKltvqRFPRILVLHLNRFSTSRGSIK-KSSVGVDFplqRLSLG-DFASDKVGSPVYQLYALCNHSGSVHYGHYTA 521
Cdd:COG5533 172 YEVSFV----KLPKILTIQLKRFANLGGNQKiDTEVDEKF---ELPVKhDQILNIVKETYYDLVGFVLHQGSLEGGHYIA 244
|
330 340 350
....*....|....*....|....*....|....*..
gi 189083712 522 LCRCQTGWHVYNDSRVSPVSENQ---VASSEGYVLFY 555
Cdd:COG5533 245 YVKKGGKWEKANDSDVTPVSEEEainEKAKNAYLYFY 281
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
209-545 |
7.18e-20 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 94.17 E-value: 7.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 209 SGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVigalwhPDSCEAVNPTRFRAVFQ 288
Cdd:COG5077 191 TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNL------QTGEEPVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 289 kyVPSFSGYSQQDAQEFLKLLMERLhlEINRRGRrappilasgPVpspprrggalheepelsdddranlmwkrylereDS 368
Cdd:COG5077 265 --WDSDDSFMQHDIQEFNRVLQDNL--EKSMRGT---------VV---------------------------------EN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 369 KIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIpkKGFAggkvSLRDCFSLFTKEEELESENAPVCDRcRQKTRSTK 448
Cdd:COG5077 299 ALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK----NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 449 KLTVQRFPRILVLHLNRFSTS--RGSIKKSSVGVDFPLQrLSLGDFASDKV-----GSPVYQLYALCNHSGSVHYGHYTA 521
Cdd:COG5077 372 GVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLE-IDLLPFLDRDAdksenSDAVYVLYGVLVHSGDLHEGHYYA 450
|
330 340
....*....|....*....|....*.
gi 189083712 522 LCRCQTG--WHVYNDSRVSPVSENQV 545
Cdd:COG5077 451 LLKPEKDgrWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
210-556 |
8.23e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 82.75 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 210 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVpgGGRAQELTEAFADVIGALWhpdsceavNPTRFRAV--- 286
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENI--KDRKSELVKRLSELIRKIW--------NPRNFKGHvsp 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 287 --FQKYVPS-----FSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILA---SGPV-----PSPPrrggalHEEPELSD 351
Cdd:cd02669 188 heLLQAVSKvskkkFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSIIHdcfQGKVqietqKIKP------HAEEEGSK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 352 DDRANLmwkrylerEDSKIVdlfvgqlksclkcqacgyRSTTFEVF-CDLSLPIPKKGFAGGK----VSLRDCFSLFTKE 426
Cdd:cd02669 262 DKFFKD--------SRVKKT------------------SVSPFLLLtLDLPPPPLFKDGNEENiipqVPLKQLLKKYDGK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 427 EELESenapvcdrcrqkTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQRLSLGDF-ASDKVGSPV---Y 502
Cdd:cd02669 316 TETEL------------KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYvHFDKPSLNLstkY 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 189083712 503 QLYALCNHSGSVH-YGHY-TALCRCQTG-WHVYNDSRVSPVSENQVASSEGYVLFYQ 556
Cdd:cd02669 384 NLVANIVHEGTPQeDGTWrVQLRHKSTNkWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
212-537 |
1.11e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 59.98 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 212 VGLRNLGNTCFLNAVLQCLSSTRPLR-------------DFCLrrdfrqevpgggraqeLTEAfadviGALWHP--DS-- 274
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCL----------------LCEL-----GFLFDMleKAkg 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 275 --CEAVNptrfravFQKyvpSFSGYSQQDA--------------------QEFLKLLMERLHLEinrrGRRAPPILASGP 332
Cdd:pfam13423 60 knCQASN-------FLR---ALSSIPEASAlglldedretnsaislssliQSFNRFLLDQLSSE----ENSTPPNPSPAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 333 VPspprrggalheepelsdddranlmwkryleredskIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGG 412
Cdd:pfam13423 126 SP-----------------------------------LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSNN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 413 KVSLRDCF------SLftkeeELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGvdFPLQ- 485
Cdd:pfam13423 171 KKPPNQTFssilksSL-----ERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEi 243
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083712 486 RLSLGDFASDKVGSPVYQLYAL-CNHSGSVHYGHYTALCR---------CQTGWHVYNDSRV 537
Cdd:pfam13423 244 GLTLSDDLQGDNEIVKYELRGVvVHIGDSGTSGHLVSFVKvadseledpTESQWYLFNDFLV 305
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
212-555 |
2.52e-09 |
|
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: 59.04 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 212 VGLRNLGNTCFLNAVLQCLSSTRPLRDFCL---------------------RRDFRQEVPGGGR-AQELTEAFADVIGAL 269
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLnfdeskaelasdypterriggREVSRSELQRSNQfVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 270 WHpdsceAVNPTRFRAvfqkyvpsFSGYSQQDAQEFLKLLMERLHLEINRRGrrappilaSGPVPSPPRRGGALHEEpel 349
Cdd:cd02666 82 TR-----SVTPSKELA--------YLALRQQDVTECIDNVLFQLEVALEPIS--------NAFAGPDTEDDKEQSDL--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 350 sdddranlmwkryleredskIVDLFVGQLKSCL-KCQACGYRSTTFEVFCDLSLPI------PKKGFAGGKVSLRDCFSL 422
Cdd:cd02666 138 --------------------IKRLFSGKTKQQLvPESMGNQPSVRTKTERFLSLLVdvgkkgREIVVLLEPKDLYDALDR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 423 FTKEEELESenAPvcdrcrQKTRSTKKLTVQRFPRILvlhlnrfSTSRGSIKKSSVGVD----------FPLQRLSLGDF 492
Cdd:cd02666 198 YFDYDSLTK--LP------QRSQVQAQLAQPLQRELI-------SMDRYELPSSIDDIDelireaiqseSSLVRQAQNEL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 493 AS---------DKVGSPVYQLYALCNHSGSVHYGHYTALCR--CQTGWHVYNDSRVSPVSENQV------ASSEGYVLFY 555
Cdd:cd02666 263 AElkheiekqfDDLKSYGYRLHAVFIHRGEASSGHYWVYIKdfEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
214-555 |
2.46e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 55.23 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 214 LRNLGNTCFLNAVLQCLSStrplrdfclrrdfrqevpgggraqelteafadvIGalwhpdsceavnptrfravfqKYVPS 293
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSS---------------------------------IG---------------------KINTE 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 294 FSGYSQQDAQEFLKLLMERLHleinrrgrrapPILASGPVPSPPRRGGALHEEPELSdddranlmwkryleredskivdl 373
Cdd:cd02673 28 FDNDDQQDAHEFLLTLLEAID-----------DIMQVNRTNVPPSNIEIKRLNPLEA----------------------- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 374 FVGQLKSCLKCQACGYRSTTFEVFCDLSLPI-PKKGfaggkVSLRDCFSLFTKEEELESEnapvCDRCRQKTRSTKKlTV 452
Cdd:cd02673 74 FKYTIESSYVCIGCSFEENVSDVGNFLDVSMiDNKL-----DIDELLISNFKTWSPIEKD----CSSCKCESAISSE-RI 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 453 QRFPRILVLHLNRFstsrgsIKKSSVGVDFPLQRLSLGDFASDkvgSPVYQLYALCNHSG-SVHYGHYTALCRCQTG--- 528
Cdd:cd02673 144 MTFPECLSINLKRY------KLRIATSDYLKKNEEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNgss 214
|
330 340 350
....*....|....*....|....*....|
gi 189083712 529 WHVYNDSRVSPVSENQV---ASSEGYVLFY 555
Cdd:cd02673 215 WLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-547 |
8.98e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 47.17 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 213 GLRNLGNTCFLNAVLQCLSSTrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQ----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 293 sfsgysQQDAQEFLKLLMERLHLEINrrgrraPPILAsgpvpspprrggalHEEPELSDDDRANLMWKRYLEREdskivd 372
Cdd:cd02665 22 ------QQDVSEFTHLLLDWLEDAFQ------AAAEA--------------ISPGEKSKNPMVQLFYGTFLTEG------ 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 373 lfVGQLKSCLKCQACGyrsttfevfcdlSLPIPKKGFAggkvSLRDCFSLFTKEEELESEnapvcdrcrqKTRSTKKLTV 452
Cdd:cd02665 70 --VLEGKPFCNCETFG------------QYPLQVNGYG----NLHECLEAAMFEGEVELL----------PSDHSVKSGQ 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 453 QR----FPRILVLHLNRFSTSRGSIKKSSVGVDFP--LQRLSlgdfasdkvgspvYQLYALCNHSGSVHYGHYTA--LCR 524
Cdd:cd02665 122 ERwfteLPPVLTFELSRFEFNQGRPEKIHDKLEFPqiIQQVP-------------YELHAVLVHEGQANAGHYWAyiYKQ 188
|
330 340
....*....|....*....|...
gi 189083712 525 CQTGWHVYNDSRVSPVSENQVAS 547
Cdd:cd02665 189 SRQEWEKYNDISVTESSWEEVER 211
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
368-556 |
1.14e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 44.04 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 368 SKIVDLFVGQLKSCLKCQACGY-------RSTTFEVF-CDLSLPIPKKGFAGgkvSLRDCFSLFTkeeELESENAPVCDR 439
Cdd:cd02672 66 STLIQNFTRFLLETISQDQLGTpfscgtsRNSVSLLYtLSLPLGSTKTSKES---TFLQLLKRSL---DLEKVTKAWCDT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083712 440 CRQKTRSTKKLTVQRFP----RILVLHLNRFSTSRGSIKKSSV-------GVDFPLQRLSLGDFASDKVGSPVYQLYA-L 507
Cdd:cd02672 140 CCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVVLPsgkvmqnKVSPKAIDHDKLVKNRGQESIYKYELVGyV 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 189083712 508 CNHSGSVHYGHYTALCR------CQTGWHVYNDSRVSPVSEnqVAssegYVLFYQ 556
Cdd:cd02672 220 CEINDSSRGQHNVVFVIkvneesTHGRWYLFNDFLVTPVSE--LA----YILLYQ 268
|
|
| |
