|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
212-556 |
7.98e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 304.75 E-value: 7.98e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 212 VGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYV 291
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 292 PSFSGYSQQDAQEFLKLLMERLHLEINRRgrrappilasgpvpsppcrgggalheepelsdddranlmwkrYLEREDSKI 371
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGN------------------------------------------HSTENESLI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 372 VDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKL 451
Cdd:pfam00443 119 TDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 452 TVQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQ----RLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQ 527
Cdd:pfam00443 199 KISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEldlsRYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY 278
|
330 340 350
....*....|....*....|....*....|..
gi 224809307 528 TG--WHVYNDSRVSPVS-ENQVASSEGYVLFY 556
Cdd:pfam00443 279 ENnrWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-557 |
2.66e-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: 264.53 E-value: 2.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 293 sfsgysQQDAQEFLKLLMERLHleinrrgrrappilasgpvpsppcrgggalheepelsdddranlmwkryleredSKIV 372
Cdd:cd02674 22 ------QQDAQEFLLFLLDGLH------------------------------------------------------SIIV 41
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 373 DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLT 452
Cdd:cd02674 42 DLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 453 VQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQRLSLGDF--ASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQ--T 528
Cdd:cd02674 122 ISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNetN 201
|
330 340
....*....|....*....|....*....
gi 224809307 529 GWHVYNDSRVSPVSENQVASSEGYVLFYQ 557
Cdd:cd02674 202 DWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
211-556 |
1.84e-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: 1.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 211 HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQE--VPGGGRAQELtEAFadVIGALWHPDSCEAVNPtrFRAVFQ 288
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDccNEGFCMMCAL-EAH--VERALASSGPGSAPRI--FSSNLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 289 KYVPSFSGYSQQDAQEFLKLLMERLHleinrrgrRAppilasgpvpsppC-RGGGALHEEPELSdddranlmwkryleRE 367
Cdd:cd02661 76 QISKHFRIGRQEDAHEFLRYLLDAMQ--------KA-------------ClDRFKKLKAVDPSS--------------QE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 368 DSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGfaggkvSLRDCFSLFTKEEELESENAPVCDRCRQKTRS 447
Cdd:cd02661 121 TTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD------SLEDALEQFTKPEQLDGENKYKCERCKKKVKA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 448 TKKLTVQRFPRILVLHLNRFSTSRGSikKSSVGVDFPlQRLSLGDFASDK-AGSPVYQLYALCNHSG-SVHYGHYTALCR 525
Cdd:cd02661 195 SKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFP-ETLDLSPYMSQPnDGPLKYKLYAVLVHSGfSPHSGHYYCYVK 271
|
330 340 350
....*....|....*....|....*....|..
gi 224809307 526 CQTG-WHVYNDSRVSPVSENQVASSEGYVLFY 556
Cdd:cd02661 272 SSNGkWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
213-557 |
4.40e-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: 210.42 E-value: 4.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSStrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 293 sfsgySQQDAQEFLKLLMERLHLEINRRGRRappilasgpvpsppcrgggalheepelsdddranlmwKRYLEREDSKIV 372
Cdd:cd02257 21 -----EQQDAHEFLLFLLDKLHEELKKSSKR-------------------------------------TSDSSSLKSLIH 58
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 373 DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGfaGGKVSLRDCFSLFTKEEELESENAPVCDRCRqKTRSTKKLT 452
Cdd:cd02257 59 DLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKG--LPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 453 VQRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPLQ------RLSLGDFASDKAGSPVYQLYALCNHSG-SVHYGHYTALC 524
Cdd:cd02257 136 IKKLPPVLIIHLKRFSfNEDGTKEKLNTKVSFPLEldlspyLSEGEKDSDSDNGSYKYELVAVVVHSGtSADSGHYVAYV 215
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 224809307 525 RCQT--GWHVYNDSRVSPVSENQV-----ASSEGYVLFYQ 557
Cdd:cd02257 216 KDPSdgKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
6.14e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 183.34 E-value: 6.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRrDFRQEVPGGGRAQ-----ELTEAFADvigaLWHPDSCEAVNPTRFRAVF 287
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS-DRHSCTCLSCSPNsclscAMDEIFQE----FYYSGDRSPYGPINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 288 QKYVPSFSGYSQQDAQEFLKLLMERLHleiNRRGRRAPPilaSGPVPSPPCrgggalheepelsdddranlmwkrylere 367
Cdd:cd02660 77 WKHSRNLAGYSQQDAHEFFQFLLDQLH---THYGGDKNE---ANDESHCNC----------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 368 dskIVD-LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIP----KKGFAGGKV-----SLRDCFSLFTKEEELESeNAPV 437
Cdd:cd02660 122 ---IIHqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnkstPSWALGESGvsgtpTLSDCLDRFTRPEKLGD-FAYK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 438 CDRCRQKTRSTKKLTVQRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPLQrLSLGDFASDKAGSP----------VYQLY 506
Cdd:cd02660 198 CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKTSRKIDTYVQFPLE-LNMTPYTSSSIGDTqdsnsldpdyTYDLF 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 224809307 507 ALCNHSGSVHYGHYTALCRCQTG-WHVYNDSRVSPVSENQVASSEGYVLFY 556
Cdd:cd02660 277 AVVVHKGTLDTGHYTAYCRQGDGqWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-557 |
1.56e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 180.66 E-value: 1.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRrdfrqevpgggraqelteafadvigalwhpdsceavNPTRFRAVFQKYVP 292
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------TPKELFSQVCRKAP 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 293 SFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilasgpvpsppcrgggalheepelsdddranlmwkryleredskiv 372
Cdd:cd02667 45 QFKGYQQQDSHELLRYLLDGLRTFIDS----------------------------------------------------- 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 373 dLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFagGKVSLRDCFSLFTKEEELESENAPVCDRCrqkTRSTKKLT 452
Cdd:cd02667 72 -IFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK--SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYL 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 453 VQRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPlQRLSLGDFASDKAGSP------VYQLYALCNHSGSVHYGHYTALCR 525
Cdd:cd02667 146 ISKLPPVLVIHLKRFQqPRSANLRKVSRHVSFP-EILDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVK 224
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 224809307 526 C-----------------------QTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 557
Cdd:cd02667 225 VrppqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
148-408 |
1.43e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 157.35 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 148 PPTLRRSTSLRRLGGFPGPPTLLSIRTEPPTSHGSFHMISarPSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVL 227
Cdd:COG5560 204 DSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRN--PDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 228 QCLSSTRPLRDFCLRRDFRQEV----PGGGRAQeLTEAFADVIGALWHPDScEAVNPTRFRAVFQKYVPSFSGYSQQDAQ 303
Cdd:COG5560 282 QCLMHTWELRDYFLSDEYEESIneenPLGMHGS-VASAYADLIKQLYDGNL-HAFTPSGFKKTIGSFNEEFSGYDQQDSQ 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 304 EFLKLLMERLHLEINRRGRRappilasgPVPSPPcrgggALHEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCL 383
Cdd:COG5560 360 EFIAFLLDGLHEDLNRIIKK--------PYTSKP-----DLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTL 426
|
250 260
....*....|....*....|....*
gi 224809307 384 KCQACGYRSTTFEVFCDLSLPIPKK 408
Cdd:COG5560 427 TCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-557 |
1.17e-39 |
|
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: 146.69 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSstrplrdfclrrdfrqevpgggrAQELTEAFADVIGALWHPDSCEAV-NPTRFRAVFQKYV 291
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-----------------------FENLLTCLKDLFESISEQKKRTGViSPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 292 PSFSGYSQQDAQEFLKLLMERLhLEINRRGRRAppilasgpvpsppcrgggalheepELSDDDRANLMwkrylEREDSK- 370
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLLNEI-AEILDAERKA------------------------EKANRKLNNNN-----NAEPQPt 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 371 -IVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKgfaggkVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTK 449
Cdd:cd02663 108 wVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 450 KLTVQRFPRILVLHLNRF--STSRGSIKKSSVGVDFPLQ-RL-SLGDFASDkaGSPVYQLYALCNHSGS-VHYGHYTALC 524
Cdd:cd02663 182 RMKIKKLPKILALHLKRFkyDEQLNRYIKLFYRVVFPLElRLfNTTDDAEN--PDRLYELVAVVVHIGGgPNHGHYVSIV 259
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 224809307 525 RCQTGWHVYNDSRVSPVSENQV--------ASSEGYVLFYQ 557
Cdd:cd02663 260 KSHGGWLLFDDETVEKIDENAVeeffgdspNQATAYVLFYQ 300
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
210-559 |
1.20e-32 |
|
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: 127.76 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 210 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPG-GGRAQELTEAFAdvigaLWHPDSCEAVNPTRFRAVFQ 288
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDnKSVPLALQRLFL-----FLQLSESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 289 KYVPSFSGYSQQDAQEFLKLLMERLhleinrrgrrappilasgpvpsppcrgggalhEEpelsdddranlMWKRyLERED 368
Cdd:cd02659 76 FGWDSLNTFEQHDVQEFFRVLFDKL--------------------------------EE-----------KLKG-TGQEG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 369 SkIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPkkgfagGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRST 448
Cdd:cd02659 112 L-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK------GKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 449 KKLTVQRFPRILVLHLNRFSTS--RGSIKKSSVGVDFPLQ-----------RLSLGDFASDKAGSPVYQLYALCNHSGSV 515
Cdd:cd02659 185 KGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLEldmepytekglAKKEGDSEKKDSESYIYELHGVLVHSGDA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224809307 516 HYGHYTALCRCQTG--WHVYNDSRVSPVSENQVA----------------------SSEGYVLFYQLM 559
Cdd:cd02659 265 HGGHYYSYIKDRDDgkWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-557 |
9.34e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 122.60 E-value: 9.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRplrDFclRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPT--RFRAVFQky 290
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAK---DF--RRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPdyFLEASRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 291 vPSFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilasgpvpsppcrgggalheepelsdddranlmwkryleredsk 370
Cdd:cd02664 74 -PWFTPGSQQDCSEYLRYLLDRLHTLIEK--------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 371 ivdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPkkgfaggkvSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKK 450
Cdd:cd02664 102 ---MFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 451 LTVQRFPRILVLHLNRFSTSRGS-------------------IKKSSVGVDFPLQRlSLGDFASDKAG---SPVYQLYAL 508
Cdd:cd02664 170 MKVTGAPEYLILTLLRFSYDQKThvrekimdnvsinevlslpVRVESKSSESPLEK-KEEESGDDGELvtrQVHYRLYAV 248
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224809307 509 CNHSG-SVHYGHYTALCRCQTG----------------------WHVYNDSRVSPVSENQV-------ASSEGYVLFYQ 557
Cdd:cd02664 249 VVHSGySSESGHYFTYARDQTDadstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
3.73e-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: 120.60 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIG------ALWHPDSCEAVNPTRF-RA 285
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDqlqlifAQLQFGNRSVVDPSGFvKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 286 VfqkyvpSFSGYSQQDAQEFLKLLMERLhleinrrgrrappilasgpvpsppcrgggalheEPELSDDDRANLmwkryle 365
Cdd:cd02668 81 L------GLDTGQQQDAQEFSKLFLSLL---------------------------------EAKLSKSKNPDL------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 366 redSKIV-DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIpkKGFAggkvSLRDCFSLFTKEEELESENAPVCDRCRQK 444
Cdd:cd02668 115 ---KNIVqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--KGHK----TLEECIDEFLKEEQLTGDNQYFCESCNSK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 445 TRSTKKLTVQRFPRILVLHLNRFSTSR--GSIKKSSVGVDFPLQrLSLGDFASD-KAGSPVYQLYALCNHSG-SVHYGHY 520
Cdd:cd02668 186 TDATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLNASISFPEI-LDMGEYLAEsDEGSYVYELSGVLIHQGvSAYSGHY 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 224809307 521 TA-LCRCQTG-WHVYNDSRVSPVSENQV---------------------ASSEGYVLFY 556
Cdd:cd02668 265 IAhIKDEQTGeWYKFNDEDVEEMPGKPLklgnsedpakprkseikkgthSSRTAYMLVY 323
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-557 |
8.92e-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: 119.35 E-value: 8.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRPL--RDFCLRRDFRQEV--PgggrAQELTEAFADVIGAL-------------WHPDSC 275
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVvdP----ANDLNCQLIKLADGLlsgryskpaslksENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 276 EAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPpilasgpvpsppcrgggalheepelsdddr 355
Cdd:cd02658 77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNP------------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 356 anlmwkryleredSKIVDLFVGQLkscLKCQACGYRSTTFEVFCDLSLPIPK--KGFAG------GKVSLRDCFSLFTKE 427
Cdd:cd02658 127 -------------NDLFKFMIEDR---LECLSCKKVKYTSELSEILSLPVPKdeATEKEegelvyEPVPLEDCLKAYFAP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 428 EELESEnapvCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSI-KKSSVGVDFPlqrlslgdfasDKAGSPVYQLY 506
Cdd:cd02658 191 ETIEDF----CSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVpKKLDVPIDVP-----------EELGPGKYELI 255
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 224809307 507 ALCNHSG-SVHYGHYTALCR----CQTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 557
Cdd:cd02658 256 AFISHKGtSVHSGHYVAHIKkeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
403-557 |
5.45e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 119.22 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 403 LPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGVD 482
Cdd:COG5560 663 WTIREIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVE 742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224809307 483 FPLQRLSLGDFASDKAGSPV-YQLYALCNHSGSVHYGHYTALCR--CQTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 557
Cdd:COG5560 743 YPIDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARnfANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-556 |
7.02e-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: 113.58 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRPLRDfCLRRDFRQEVPGGGRAQELTEAFADVIGALwhPDSCEAVNPTRFRAVFQKYVP 292
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRD-ALKNYNPARRGANQSSDNLTNALRDLFDTM--DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 293 SFS------GYSQQDAQEFLKLLMERLhleinrrgRRAPPILAsgpvpsppcrgggalheepelsdddranlmwkryleR 366
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVL--------SQKLPGAG------------------------------------S 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 367 EDSKIVDLFVGQLKSCLKCQACGY-RSTTFEVFCDLSLPIpkkgfaGGKVslrDCFSLFTK-EEELESENAPVCDRCRQK 444
Cdd:cd02657 114 KGSFIDQLFGIELETKMKCTESPDeEEVSTESEYKLQCHI------SITT---EVNYLQDGlKKGLEEEIEKHSPTLGRD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 445 TRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSV--GVDFPLQrLSLGDFASdkaGSPVYQLYALCNHSG-SVHYGHYT 521
Cdd:cd02657 185 AIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIlrKVKFPFE-LDLYELCT---PSGYYELVAVITHQGrSADSGHYV 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 224809307 522 ALCRCQTG--WHVYNDSRVSPVSENQVASSEG-------YVLFY 556
Cdd:cd02657 261 AWVRRKNDgkWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
212-556 |
3.71e-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: 106.52 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 212 VGLRNLGNTCFLNAVLQCLSstrplrdFClrRDFRQEVP---GGGRAQELTEAFADVIGALWHpDSCEAVNPTRFRAVFQ 288
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLY-------FC--PGFKHGLKhlvSLISSVEQLQSSFLLNPEKYN-DELANQAPRRLLNALR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 289 KYVPSFSGYSQQDAQEFLKLLMERLHleinrrgrrappilasgpvpsppcrgggalheepelsdddraNLMWKrylered 368
Cdd:cd02671 95 EVNPMYEGYLQHDAQEVLQCILGNIQ------------------------------------------ELVEK------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 369 skivdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVS-------------LRDCFSLFTKEEELESENA 435
Cdd:cd02671 126 -----DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESseispdpktemktLKWAISQFASVERIVGEDK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 436 PVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSR------GSIKKSSVGVDFPLqRLSLGDFaSDKAGSPVYQLYALC 509
Cdd:cd02671 201 YFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefdcyGGLSKVNTPLLTPL-KLSLEEW-STKPKNDVYRLFAVV 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 224809307 510 NHSG-SVHYGHYTALCRcqtgWHVYNDSRV---------SPVSENQVASSEGYVLFY 556
Cdd:cd02671 279 MHSGaTISSGHYTAYVR----WLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-557 |
5.29e-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: 103.60 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRPLRDFClrrdfrqevpgggraQELTEafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------EEFLE-------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 293 sfsgysQQDAQEFLKLLMERLHleinrrgrrappilasgpvpsppcrgggalheepelsdddranlmwkryleredSKIV 372
Cdd:cd02662 34 ------QQDAHELFQVLLETLE------------------------------------------------------QLLK 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 373 DLFVGQLKSCLKCQACGYRST-TFEVFCDLSLPIPKKGFAGGkVSLRDCFSLFTKEEELESenaPVCDRCrqktrstkKL 451
Cdd:cd02662 54 FPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSG-TTLEHCLDDFLSTEIIDD---YKCDRC--------QT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 452 TVQRFPRILVLHLNRFS-TSRGSIKKSSVGVDFPLqRLSlgdfasdkagSPVYQLYALCNHSGSVHYGHYTALCR----- 525
Cdd:cd02662 122 VIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFPE-RLP----------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfs 190
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 224809307 526 ---------------CQTG--WHVYNDSRVSPVSENQV-ASSEGYVLFYQ 557
Cdd:cd02662 191 kdkepgsfvrmregpSSTShpWWRISDTTVKEVSESEVlEQKSAYMLFYE 240
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
213-556 |
3.37e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 99.88 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTRP------LRDFCLRRDFRQEVPGGGRAQELTEAFAdVIGALWHPDSceavnptrfrav 286
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldellDDLSKELKVLKNVIRKPEPDLNQEEALK-LFTALWSSKE------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 287 fQKYVPSFSGYSQQDAQEFLKLLMERLHLE-INRRGRRAPPILAsgpvpsppcrgggalhEEPELSDDDRANLmwkrYLE 365
Cdd:COG5533 68 -HKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIRIFKTTK----------------DKKKTSTGDWFDI----IIE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 366 REDSKIVDlfvgqlksclkcqacgyRSTTFEVFCDL--SLPIPKKGfaggkvslrdcfslfTKEEELESENApvcdRCRQ 443
Cdd:COG5533 127 LPDQTWVN-----------------NLKTLQEFIDNmeELVDDETG---------------VKAKENEELEV----QAKQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 444 KTRSTKKltvqRFPRILVLHLNRFSTSRGSIK-KSSVGVDFPLQrlslgdFASDKAGSPV----YQLYALCNHSGSVHYG 518
Cdd:COG5533 171 EYEVSFV----KLPKILTIQLKRFANLGGNQKiDTEVDEKFELP------VKHDQILNIVketyYDLVGFVLHQGSLEGG 240
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 224809307 519 HYTALCRCQTGWHVYNDSRVSPVSENQ---VASSEGYVLFY 556
Cdd:COG5533 241 HYIAYVKKGGKWEKANDSDVTPVSEEEainEKAKNAYLYFY 281
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
209-546 |
4.58e-20 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 94.55 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 209 SGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVigalwhPDSCEAVNPTRFRAVFQ 288
Cdd:COG5077 191 TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNL------QTGEEPVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 289 kyVPSFSGYSQQDAQEFLKLLMERLhlEINRRGRrappilasgPVpsppcrgggalheepelsdddranlmwkrylereD 368
Cdd:COG5077 265 --WDSDDSFMQHDIQEFNRVLQDNL--EKSMRGT---------VV----------------------------------E 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 369 SKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIpkKGFAggkvSLRDCFSLFTKEEELESENAPVCDRcRQKTRST 448
Cdd:COG5077 298 NALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK----NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 449 KKLTVQRFPRILVLHLNRFSTS--RGSIKKSSVGVDFPLQ--RLSLGDFASDKAGSP--VYQLYALCNHSGSVHYGHYTA 522
Cdd:COG5077 371 KGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLEidLLPFLDRDADKSENSdaVYVLYGVLVHSGDLHEGHYYA 450
|
330 340
....*....|....*....|....*.
gi 224809307 523 LCRCQTG--WHVYNDSRVSPVSENQV 546
Cdd:COG5077 451 LLKPEKDgrWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
210-557 |
1.17e-16 |
|
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: 82.37 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 210 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVpgGGRAQELTEAFADVIGALWhpdsceavNPTRFRAV--- 286
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENI--KDRKSELVKRLSELIRKIW--------NPRNFKGHvsp 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 287 --FQKYVPS-----FSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILA---SGPV-----PSPPcrgggalHEEPELS 351
Cdd:cd02669 188 heLLQAVSKvskkkFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSIIHdcfQGKVqietqKIKP-------HAEEEGS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 352 DDDRANLmwkrylerEDSKIVdlfvgqlksclkcqacgyRSTTFEVF-CDLSLPIPKKGFAGGK----VSLRDCFSLFTK 426
Cdd:cd02669 261 KDKFFKD--------SRVKKT------------------SVSPFLLLtLDLPPPPLFKDGNEENiipqVPLKQLLKKYDG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 427 EEELESenapvcdrcrqkTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQRLSLGDF-ASDKAGSPV--- 502
Cdd:cd02669 315 KTETEL------------KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYvHFDKPSLNLstk 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 224809307 503 YQLYALCNHSGSVH-YGHY-TALCRCQTG-WHVYNDSRVSPVSENQVASSEGYVLFYQ 557
Cdd:cd02669 383 YNLVANIVHEGTPQeDGTWrVQLRHKSTNkWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
212-538 |
4.80e-10 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 61.13 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 212 VGLRNLGNTCFLNAVLQCLSSTRPLR-------------DFCLrrdfrqevpgggraqeLTEAfadviGALWHP--DS-- 274
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCL----------------LCEL-----GFLFDMleKAkg 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 275 --CEAVNptrfravFQKyvpSFSGYSQQDA--------------------QEFLKLLMERLHLEinrrGRRAPPILASGP 332
Cdd:pfam13423 60 knCQASN-------FLR---ALSSIPEASAlglldedretnsaislssliQSFNRFLLDQLSSE----ENSTPPNPSPAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 333 VPsppcrgggalheepelsdddranlmwkryleredskIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAG 412
Cdd:pfam13423 126 SP------------------------------------LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSN 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 413 GKVSLRDCF------SLftkeeELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGvdFPLQ 486
Cdd:pfam13423 170 NKKPPNQTFssilksSL-----ERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPE 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224809307 487 -RLSLGDFASDKAGSPVYQLYAL-CNHSGSVHYGHYTALCR---------CQTGWHVYNDSRV 538
Cdd:pfam13423 243 iGLTLSDDLQGDNEIVKYELRGVvVHIGDSGTSGHLVSFVKvadseledpTESQWYLFNDFLV 305
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
212-556 |
8.16e-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: 57.50 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 212 VGLRNLGNTCFLNAVLQCLSSTRPLRDFCL---------------------RRDFRQEVPGGGR-AQELTEAFADVIGAL 269
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLnfdeskaelasdypterriggREVSRSELQRSNQfVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 270 WHpdsceAVNPTRFRAvfqkyvpsFSGYSQQDAQEFLKLLMERLHLEINRRGrrappilaSGPVPSPPCRGGGALHEEPE 349
Cdd:cd02666 82 TR-----SVTPSKELA--------YLALRQQDVTECIDNVLFQLEVALEPIS--------NAFAGPDTEDDKEQSDLIKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 350 LsdddranlmwkrYLEREDSKIVDLFVGQLKSclkcqacgyRSTTFEVFcdLSLPI------PKKGFAGGKVSLRDCFSL 423
Cdd:cd02666 141 L------------FSGKTKQQLVPESMGNQPS---------VRTKTERF--LSLLVdvgkkgREIVVLLEPKDLYDALDR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 424 FTKEEELESenAPvcdrcrQKTRSTKKLTVQRFPRILvlhlnrfSTSRGSIKKSSVGVDFPL-----QRLSLGDFASDKA 498
Cdd:cd02666 198 YFDYDSLTK--LP------QRSQVQAQLAQPLQRELI-------SMDRYELPSSIDDIDELIreaiqSESSLVRQAQNEL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 499 GSP--------------VYQLYALCNHSGSVHYGHYTALCR--CQTGWHVYNDSRVSPVSENQV------ASSEGYVLFY 556
Cdd:cd02666 263 AELkheiekqfddlksyGYRLHAVFIHRGEASSGHYWVYIKdfEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
214-556 |
1.61e-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: 55.61 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 214 LRNLGNTCFLNAVLQCLSStrplrdfclrrdfrqevpgggraqelteafadvIGalwhpdsceavnptrfravfqKYVPS 293
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSS---------------------------------IG---------------------KINTE 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 294 FSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPIlasgpvpsppcrGGGALHEEPELSdddranlmwkryleredskivd 373
Cdd:cd02673 28 FDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPS------------NIEIKRLNPLEA---------------------- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 374 lFVGQLKSCLKCQACGYRSTTFEVFCDLSLPI-PKKGfaggkVSLRDCFSLFTKEEELESEnapvCDRCRQKTRSTKKlT 452
Cdd:cd02673 74 -FKYTIESSYVCIGCSFEENVSDVGNFLDVSMiDNKL-----DIDELLISNFKTWSPIEKD----CSSCKCESAISSE-R 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 453 VQRFPRILVLHLNRFstsrgsIKKSSVGVDFPLQRLSLGDFASDkagSPVYQLYALCNHSG-SVHYGHYTALCRCQTG-- 529
Cdd:cd02673 143 IMTFPECLSINLKRY------KLRIATSDYLKKNEEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNgs 213
|
330 340 350
....*....|....*....|....*....|.
gi 224809307 530 -WHVYNDSRVSPVSENQV---ASSEGYVLFY 556
Cdd:cd02673 214 sWLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-548 |
1.21e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 46.78 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 213 GLRNLGNTCFLNAVLQCLSSTrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 292
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLFSQ----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 293 sfsgysQQDAQEFLKLLMERLHLEINrrgrraPPILAsgpvpsppcrgggalHEEPELSDDDRANLMWKRYLEREdskiv 372
Cdd:cd02665 22 ------QQDVSEFTHLLLDWLEDAFQ------AAAEA---------------ISPGEKSKNPMVQLFYGTFLTEG----- 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 373 dlfVGQLKSCLKCQACGyrsttfevfcdlSLPIPKKGFAggkvSLRDCFSLFTKEEELESEnapvcdrcrqKTRSTKKLT 452
Cdd:cd02665 70 ---VLEGKPFCNCETFG------------QYPLQVNGYG----NLHECLEAAMFEGEVELL----------PSDHSVKSG 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 453 VQR----FPRILVLHLNRFSTSRGSIKKSSVGVDFP--LQRLSlgdfasdkagspvYQLYALCNHSGSVHYGHYTA--LC 524
Cdd:cd02665 121 QERwfteLPPVLTFELSRFEFNQGRPEKIHDKLEFPqiIQQVP-------------YELHAVLVHEGQANAGHYWAyiYK 187
|
330 340
....*....|....*....|....
gi 224809307 525 RCQTGWHVYNDSRVSPVSENQVAS 548
Cdd:cd02665 188 QSRQEWEKYNDISVTESSWEEVER 211
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
369-557 |
9.47e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 44.43 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 369 SKIVDLFVGQLKSCLKCQACGY-------RSTTFEVF-CDLSLPIPKKGFAGgkvSLRDCFSLFTkeeELESENAPVCDR 440
Cdd:cd02672 66 STLIQNFTRFLLETISQDQLGTpfscgtsRNSVSLLYtLSLPLGSTKTSKES---TFLQLLKRSL---DLEKVTKAWCDT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809307 441 CRQKTRSTKKLTVQRFP----RILVLHLNRFSTSRGSIKKSSV-------GVDFPLQRLSLGDFASDKAGSPVYQLYA-L 508
Cdd:cd02672 140 CCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVVLPsgkvmqnKVSPKAIDHDKLVKNRGQESIYKYELVGyV 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224809307 509 CNHSGSVHYGHYTALCR------CQTGWHVYNDSRVSPVSEnqVAssegYVLFYQ 557
Cdd:cd02672 220 CEINDSSRGQHNVVFVIkvneesTHGRWYLFNDFLVTPVSE--LA----YILLYQ 268
|
|
| |
