|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
273-675 |
6.09e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 228.48 E-value: 6.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 273 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlamtasektrsckhppvtdtvvyqmnecqekdtgfvcsrqssl 352
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 353 ssglsggaskgrkMELIQPKEPTSQYISLCHELHTLFQVMWSGKW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:pfam00443 32 -------------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 432 LDKIQRELEttgtslpaliptsqRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryqcsgkDIA 511
Cdd:pfam00443 99 LDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-------DSA 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 512 SQPCLV-TEMLAKFTETEALEGKI-YVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSgRNNREKIG 589
Cdd:pfam00443 158 ELKTASlQICFLQFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLN 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 590 VHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMD-EVCKA 668
Cdd:pfam00443 226 TEVEFPLELDLSRYLAEELKPKTNNLQ-DYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSS 303
|
....*..
gi 109134334 669 QAYILFY 675
Cdd:pfam00443 304 SAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-676 |
3.14e-61 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 208.38 E-value: 3.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrSCKHPPVTDTvvyqmnecqekdtgfvcsrqssls 353
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggaskgrkmeliqpkepTSQYISLCHELHTLFQVMW-SGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELL 432
Cdd:cd02660 41 ---------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLL 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 433 DKIQRELettGTSLPALIPTSQRKLIkqvlnvVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIAS 512
Cdd:cd02660 100 DQLHTHY---GGDKNEANDESHCNCI------IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 513 ----QPCLvTEMLAKFTETEALEGKIYVCDQCNSKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKI 588
Cdd:cd02660 171 gvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 589 GVHVGFEEILNMEPYCCRET----LKSLRPECFIYDLSAVVMHHGKgFGSGHYTAYCYNsEGGFWVHCNDSKLSMCTMDE 664
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEE 316
|
410
....*....|..
gi 109134334 665 VCKAQAYILFYT 676
Cdd:cd02660 317 VLKSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
421-675 |
3.20e-57 |
|
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: 195.01 E-value: 3.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 421 QQDAQEFLCELLDKIQRELETTgtslpalipTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 500
Cdd:cd02257 22 QQDAHEFLLFLLDKLHEELKKS---------SKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 501 ERyqcsgkdiASQPCLVTEMLAKFTETEALEGkiYVCDQCNSKRrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWS 580
Cdd:cd02257 93 VK--------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLKRFSFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 581 GRNNREKIGVHVGFEEILNMEPYCCRETLKSLRP-ECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSM 659
Cdd:cd02257 154 EDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTE 233
|
250 260
....*....|....*....|.
gi 109134334 660 CTMDEV-----CKAQAYILFY 675
Cdd:cd02257 234 VSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-675 |
6.43e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 184.79 E-value: 6.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 273 TGLRNLGNTCYMNSVLQVLSHLlifrqcflkldlnqwlamtasektrsckhPPVTDTVVYQM--NECQEKDTGFVCsrqs 350
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHT-----------------------------PPLANYLLSREhsKDCCNEGFCMMC---- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 351 slssglsggaskgrkmeliqpkeptsqyislCHELHTLfQVMWSGKWALVSPFamLHSVWRLI-PAFRGYAQQDAQEFLC 429
Cdd:cd02661 49 -------------------------------ALEAHVE-RALASSGPGSAPRI--FSSNLKQIsKHFRIGRQEDAHEFLR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 430 ELLDKIQRelettgTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefperyqcsgkD 509
Cdd:cd02661 95 YLLDAMQK------ACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSL-----------D 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 510 IASQPCLvTEMLAKFTETEALEGK-IYVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFrwsGRNNREKI 588
Cdd:cd02661 158 IKGADSL-EDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGKI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 589 GVHVGFEEILNMEPYCCRETLKSLrpecfIYDLSAVVMHHGKGFGSGHYTAYCYNSEgGFWVHCNDSKLSMCTMDEVCKA 668
Cdd:cd02661 223 NKQISFPETLDLSPYMSQPNDGPL-----KYKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDDSKVSPVSIETVLSQ 296
|
....*..
gi 109134334 669 QAYILFY 675
Cdd:cd02661 297 KAYILFY 303
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
377-675 |
7.88e-46 |
|
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: 164.87 E-value: 7.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 377 QYISLCHELHTLFQVmwsgkwalvSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQrelettgtslpaliptsqrk 456
Cdd:cd02667 16 QNLSQTPALRELLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 457 likqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefPEryqcsgKDIASQPCLVTEMLAKFTETEALEGK-IY 535
Cdd:cd02667 67 ------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL--PR------SDEIKSECSIESCLKQFTEVEILEGNnKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 536 VCDQCnskrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCcreTLKSLRPE 615
Cdd:cd02667 133 ACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFC---DPKCNSSE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 616 C---FIYDLSAVVMHHGkGFGSGHYTAYCY------------------NSEG---GFWVHCNDSKLSMCTMDEVCKAQAY 671
Cdd:cd02667 196 DkssVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAY 274
|
....
gi 109134334 672 ILFY 675
Cdd:cd02667 275 LLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
421-676 |
3.47e-43 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 155.52 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 421 QQDAQEFLCELLDKIQrelettgtslpaliptsqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 500
Cdd:cd02674 22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 501 ERYQCSGKdiasqpCLVTEMLAKFTETEALEGKIYV-CDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFRW 579
Cdd:cd02674 76 SGSGDAPK------VTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLKRFSF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 580 SGRNnREKIGVHVGFE-EILNMEPYCcretLKSLRPECFIYDLSAVVMHHGKGFGsGHYTAYCYNSEGGFWVHCNDSKLS 658
Cdd:cd02674 139 SRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDDSRVT 212
|
250
....*....|....*...
gi 109134334 659 MCTMDEVCKAQAYILFYT 676
Cdd:cd02674 213 KVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-675 |
2.58e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 150.87 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWlamtasekTRSCKHPPVTDTVVYQMNECQEKDtgfvcsrqssls 353
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED--------DDDNKSVPLALQRLFLFLQLSESP------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggaskgrkmelIQPKEPTSqyislchelhtLFQVMWsgkwalvspfamlhsvWRLIPAFRgyaQQDAQEFLCELLD 433
Cdd:cd02659 64 ---------------VKTTELTD-----------KTRSFG----------------WDSLNTFE---QHDVQEFFRVLFD 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 434 KIQRELEttgtslpaliPTSQRKLIKqvlnvvnNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEfperyqcsGKDIASq 513
Cdd:cd02659 99 KLEEKLK----------GTGQEGLIK-------NLFGGKLVNYIICKECPHESEREEYFLDLQVA--------VKGKKN- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 514 pclVTEMLAKFTETEALEG-KIYVCDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFRWSG-RNNREKIGVH 591
Cdd:cd02659 153 ---LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKINDR 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 592 VGFEEILNMEPYCCR------ETLKSLRPECFIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEV 665
Cdd:cd02659 219 FEFPLELDMEPYTEKglakkeGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDA 297
|
410 420 430
....*....|....*....|....*....|..
gi 109134334 666 CKAQ----------------------AYILFY 675
Cdd:cd02659 298 EEECfggeetqktydsgprafkrttnAYMLFY 329
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-658 |
3.74e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 138.71 E-value: 3.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQwlamTASEKTRSCKHPPVTDTVVYQMnecqekdtgfvcsrqssls 353
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTE----DAELKNMPPDKPHEPQTIIDQL------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggaskgrkmeliqpkeptsQYIslchelhtlFQVMWSGKWALVSPFAmlhsvwrLIPAFR--GYAQQDAQEFLCEL 431
Cdd:cd02668 58 -----------------------QLI---------FAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLF 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 432 LDKIQRELettgtslpaliptsQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFperyqcsgKDIA 511
Cdd:cd02668 99 LSLLEAKL--------------SKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--------KGHK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 512 SqpclVTEMLAKFTETEALEG-KIYVCDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRF---RWSGRnnREK 587
Cdd:cd02668 157 T----LEECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTGA--KKK 219
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109134334 588 IGVHVGFEEILNMEPYCCRETLKSlrpecFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLS 658
Cdd:cd02668 220 LNASISFPEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVE 285
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
385-676 |
5.64e-35 |
|
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: 134.74 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 385 LHTLFQVMWSGK--WALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVL 462
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 463 NVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQcsgkdiasqpclVTEMLAKFTETEALEGK-IYVCDQCN 541
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTS------------ITSCLRQFSATETLCGRnKFYCDECC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 542 SKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFRWSGRNNR-EKIGVHVGFEEILNMepycCRETLKSLRPeCFIYD 620
Cdd:cd02663 175 SLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFPLELRL----FNTTDDAENP-DRLYE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109134334 621 LSAVVMHHGKGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMDEVCK--------AQAYILFYT 676
Cdd:cd02663 239 LVAVVVHIGGGPNHGHYVSIV--KSHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-675 |
1.35e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 111.04 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlamtasektrsckhPPVTDTVVyqmnecqekdTGFVcsrqssls 353
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNL-----------------PRLGDSQS----------VMKK-------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggaskgrkmeliqpkeptsqyislchELHTLFQVMWSGKWALVSPFAMLHSVWRliPAFRGYAQQDAQEFLCELLD 433
Cdd:cd02664 46 ------------------------------LQLLQAHLMHTQRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRYLLD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 434 KIQRELETTgtslpaliptsqrklikqvlnvvnniFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPeryqcsgkdiasq 513
Cdd:cd02664 94 RLHTLIEKM--------------------------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 514 pcLVTEMLAKFTETEALEGK-IYVCDQCNSkrrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNREKIGVH 591
Cdd:cd02664 135 --SVQDLLNYFLSPEKLTGDnQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDqKTHVREKIMDN 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 592 VGFEEILNMEPYCCRETLKSLRPE-----------CFI---YDLSAVVMHHGKGFGSGHYtaYCY--------------- 642
Cdd:cd02664 202 VSINEVLSLPVRVESKSSESPLEKkeeesgddgelVTRqvhYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecp 279
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 109134334 643 -------NSEGGFWVHCNDSKLSMCTMDEV-------CKAQAYILFY 675
Cdd:cd02664 280 epkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-675 |
2.68e-24 |
|
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: 103.95 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlamtasektRSCkhpPVTDTVVYQMNECQEKDTGfvcsrqssls 353
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL---------------------------RSV---PELRDALKNYNPARRGANQ---------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggaskgrkmeliqpkepTSQYISLchELHTLFQVMwSGKWALVSPFAMLHSVWRLIPAF------RGYAQQDAQEF 427
Cdd:cd02657 41 ---------------------SSDNLTN--ALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEEC 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 428 LCELLDKIQRELEttgtslpalIPTSQRKLIKQvlnvvnnIFHGQLLSQVTCLACDN-KSNTIEPFWDLSLefperyQCS 506
Cdd:cd02657 97 WSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESPDeEEVSTESEYKLQC------HIS 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 507 GKDIASQpcLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSkpvvlteaqkqlmichLPQVLRLHLKRFRWSGR-NNR 585
Cdd:cd02657 155 ITTEVNY--LQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISR----------------LPKYLTVQFVRFFWKRDiQKK 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 586 EKIGVHVGFEEILNMEPYCCretlkslrpECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEV 665
Cdd:cd02657 217 AKILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDI 287
|
410
....*....|....*..
gi 109134334 666 CKAQ-------AYILFY 675
Cdd:cd02657 288 LKLSgggdwhiAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-675 |
4.20e-24 |
|
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: 103.82 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 270 PGVTGLRNLGNTCYMNSVLQVLshllifrqCFlkldlnqwlamtASEKTRSCKHppvtdtvvyqmnecqekdtgfVCSrq 349
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVL--------YF------------CPGFKHGLKH---------------------LVS-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 350 sslssglsggaskgrkmeLIQPKEPTSQYISLCHELHTlfqvmwsGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLC 429
Cdd:cd02671 59 ------------------LISSVEQLQSSFLLNPEKYN-------DELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 430 ELLDKIQrelettgtslpaliptsqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKD 509
Cdd:cd02671 114 CILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 510 IAS-QPCLVTEM------LAKFTETEALEGK-IYVCDQCNSkrrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWSG 581
Cdd:cd02671 168 SSEiSPDPKTEMktlkwaISQFASVERIVGEdKYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 582 RNNR-----EKIGVHVGFEEILNMEPYCCRETLKSlrpecfiYDLSAVVMHHGKGFGSGHYTAYCYnseggfWVHCNDSK 656
Cdd:cd02671 237 SEFDcygglSKVNTPLLTPLKLSLEEWSTKPKNDV-------YRLFAVVMHSGATISSGHYTAYVR------WLLFDDSE 303
|
410 420
....*....|....*....|....*...
gi 109134334 657 LSMCTMDEVCKAQA---------YILFY 675
Cdd:cd02671 304 VKVTEEKDFLEALSpntsststpYLLFY 331
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
29-90 |
6.57e-23 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 92.32 E-value: 6.57e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109134334 29 CVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDN 90
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
413-675 |
8.77e-22 |
|
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: 95.13 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 413 IPAFRGY-----AQQDAQEFLCELLDKIQRELEttgtslpaliptsqrklikqvlnvvnNIFHGQLLSQVTCLACDNKSN 487
Cdd:cd02662 21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 488 -TIEPFWDLSLEFPERYQCSGkdiasqpCLVTEMLAKFTETEALEGkiYVCDQCnskrrrfsskpvvlteaqkQLMICHL 566
Cdd:cd02662 75 vRYESFTMLSLPVPNQSSGSG-------TTLEHCLDDFLSTEIIDD--YKCDRC-------------------QTVIVRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 567 PQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMepyccretlkslrpecFIYDLSAVVMHHGkGFGSGHYTAY------ 640
Cdd:cd02662 127 PQILCIHLSRSVFDGRGTSTKNSCKVSFPERLPK----------------VLYRLRAVVVHYG-SHSSGHYVCYrrkplf 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 109134334 641 --------------CYNSEGGFWVHCNDSKLSMCTMDEVC-KAQAYILFY 675
Cdd:cd02662 190 skdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
274-677 |
6.11e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 90.63 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLShllifrqcfLKLDLNQWLAMTASEKTRSCKHppvtdtvVYQMNEcqekdtgfvcsrqssls 353
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA---------LYLPKLDELLDDLSKELKVLKN-------VIRKPE----------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggaskgrkmeliqpkEPTSQyislcHELHTLFQVMWSGKwalvspfamlhsVWRLIPAFRGYAQQDAQEFLCELLD 433
Cdd:COG5533 48 -------------------PDLNQ-----EEALKLFTALWSSK------------EHKVGWIPPMGSQEDAHELLGKLLD 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 434 KIQRELETTGTslpaliptsqrKLIKQVLNvvnnifhgqllsqvtclacDNKSNTIEPFWDLSLEFPerYQCSGKDIASQ 513
Cdd:COG5533 92 ELKLDLVNSFT-----------IRIFKTTK-------------------DKKKTSTGDWFDIIIELP--DQTWVNNLKTL 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 514 PCLVTEMlakftetealegKIYVCDQCNSKRRRFSSKPVVlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNR------EK 587
Cdd:COG5533 140 QEFIDNM------------EELVDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEK 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 588 IGVHVGFEEILNMEPYccretlkslrpecFIYDLSAVVMHHGkGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMDEVCK 667
Cdd:COG5533 207 FELPVKHDQILNIVKE-------------TYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAIN 270
|
410
....*....|...
gi 109134334 668 A---QAYILFYTQ 677
Cdd:COG5533 271 EkakNAYLYFYER 283
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-675 |
2.44e-19 |
|
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: 89.30 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlamtaseKTRSCKHPPVTDTVVyQMNECQekdTGFVCSRqssls 353
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEN----------KFPSDVVDPANDLNC-QLIKLA---DGLLSGR----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 354 sglsggasKGRKMELIQPKEPTSQYISlchelhtlfqvmwsgkwalvsPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLD 433
Cdd:cd02658 62 --------YSKPASLKSENDPYQVGIK---------------------PSMFKALIGKGHPEFSTMRQQDALEFLLHLID 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 434 KIQRELETTGTSLPaliptsqrklikqvlnvvNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPER---YQCSGKDI 510
Cdd:cd02658 113 KLDRESFKNLGLNP------------------NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeatEKEEGELV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 511 ASQPCLVtEMLAKFTETEALEGKiyvCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGV 590
Cdd:cd02658 175 YEPVPLE-DCLKAYFAPETIEDF---CSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 591 HVGFEEILNMEPyccretlkslrpecfiYDLSAVVMHHGKGFGSGHYTAYCY--NSEGGFWVHCNDSKLSMCTMDEVCKA 668
Cdd:cd02658 240 PIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKK 303
|
....*..
gi 109134334 669 QAYILFY 675
Cdd:cd02658 304 LGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
271-665 |
4.51e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 89.16 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 271 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNqwlamtasektrsckHPPVTDTVVYQMNECqekdtgFvcsrqs 350
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTD---------------HPRGRDSVALALQRL------F------ 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 351 slssglsggaskgrkMELIQPKEPTSQyislchelhTLFQVmwSGKWAlvspfamlhsvwrlipAFRGYAQQDAQEFLCE 430
Cdd:COG5077 245 ---------------YNLQTGEEPVDT---------TELTR--SFGWD----------------SDDSFMQHDIQEFNRV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 431 LLDKIQRELETTgtslpaliptsqrklikQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLslefperyQCSGKDI 510
Cdd:COG5077 283 LQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDI--------QLNVKGM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 511 ASqpclVTEMLAKFTETEALEGKiyvcdqcnskrRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNREKIG 589
Cdd:COG5077 338 KN----LQESFRRYIQVETLDGD-----------NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMVKIN 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109134334 590 VHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGKgFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEV 665
Cdd:COG5077 403 DRYEFPLEIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
521-678 |
4.16e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 82.62 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 521 LAKFTETEAL-EGKIYVCDQCNSKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFRwSGRNNREKIGVHVGFE-EIL 598
Cdd:COG5560 681 LNEFSKPEQLgLSDSWYCPGCKEFR-----------QASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYPiDDL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 599 NMEPYccretLKSLRPECFIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQR 678
Cdd:COG5560 749 DLSGV-----EYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
271-500 |
9.34e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 81.47 E-value: 9.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 271 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrsckhppvTDTVVYQMNEcqekdtgfvcsrqs 350
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------SDEYEESINE-------------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 351 slssglsggaskgrkmeliqpKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCE 430
Cdd:COG5560 306 ---------------------ENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 431 LLDKIQREL----ETTGTSLPALIPTSQRKlIKQVLN------------VVNNIFHGQLLSQVTCLACDNKSNTIEPFWD 494
Cdd:COG5560 365 LLDGLHEDLnriiKKPYTSKPDLSPGDDVV-VKKKAKecwwehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMD 443
|
....*.
gi 109134334 495 LSLEFP 500
Cdd:COG5560 444 LTLPLP 449
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
28-73 |
1.98e-13 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 65.08 E-value: 1.98e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 109134334 28 HCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVN 73
Cdd:smart00290 1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLG 46
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-675 |
3.55e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 65.80 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 270 PGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEktrsckhppvtdtvvyqmnecqekdtgfvcsrq 349
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSE--------------------------------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 350 sslssglsggaskgrkmeliqpkeptsqyisLCHELHTLFQVMWSGKW--ALVSPFAMLHSVWRLIPA-FRGYAQQDAQE 426
Cdd:cd02669 164 -------------------------------LVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKVSKKkFSITEQSDPVE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 427 FLCELLDKIQRELETTGTSLPALIPTS-QRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIePFWDLSLEFPER--Y 503
Cdd:cd02669 213 FLSWLLNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPplF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 504 QCS-GKDIASQPCLvTEMLAKFTETEalegkiyvCDQCNSKRRRFsskpvvlteaqkqlMICHLPQVLRLHLKRFRwsgR 582
Cdd:cd02669 292 KDGnEENIIPQVPL-KQLLKKYDGKT--------ETELKDSLKRY--------------LISRLPKYLIFHIKRFS---K 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 583 NN--REKIGVHVGFEEILNMEPYCCRETLKSLrPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMC 660
Cdd:cd02669 346 NNffKEKNPTIVNFPIKNLDLSDYVHFDKPSL-NLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEV 424
|
410
....*....|....*
gi 109134334 661 TMDEVCKAQAYILFY 675
Cdd:cd02669 425 LPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
406-675 |
3.86e-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: 54.84 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 406 LHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIptsqrKLIKQvLNVVNnIFHGQLLSQVTCLACDNK 485
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSN-----IEIKR-LNPLE-AFKYTIESSYVCIGCSFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 486 SNTIEPFWDLSLEFPERYQCSGKDIASQpclvtemLAKFTETEAlegkiyVCDQCNSKRRRFSSKpvvlteaqkqlmICH 565
Cdd:cd02673 91 ENVSDVGNFLDVSMIDNKLDIDELLISN-------FKTWSPIEK------DCSSCKCESAISSER------------IMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 566 LPQVLRLHLKRFRWsgrnnREKIGVHVGFEEiLNMEPYCcrETLKSlrpecfiYDLSAVVMHHGKGFGSGHYTAYCYN-S 644
Cdd:cd02673 146 FPECLSINLKRYKL-----RIATSDYLKKNE-EIMKKYC--GTDAK-------YSLVAVICHLGESPYDGHYIAYTKElY 210
|
250 260 270
....*....|....*....|....*....|....
gi 109134334 645 EGGFWVHCNDSKLSMCTMDEVCKA---QAYILFY 675
Cdd:cd02673 211 NGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-675 |
6.92e-07 |
|
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: 52.11 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 273 TGLRNLGNTCYMNSVLQVLSHLLIFRQcfLKLDLNQWLAMTASEKTRSCKHPPvtdtvvyqmnecQEKdtgfvcsrqssl 352
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRD--LVLNFDESKAELASDYPTERRIGG------------REV------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 353 ssglsggaskgRKMELIQPKEptsqyisLCHELHTLFQVMWSGKWALVSPFAMLhsvwrlipAFRGYAQQDAQEflceLL 432
Cdd:cd02666 56 -----------SRSELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE----CI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 433 DKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVT-CLACDNKSNTIEPFWDLSLEFPERYQCSGKDIA 511
Cdd:cd02666 106 DNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVDVGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 512 SQPCLVTEMLAKFTETEALEG-KIYVCDQCNSKRRRFSSKPVVLTEAQKQL------MICHLPQVLRLHLKRFRWSGRNN 584
Cdd:cd02666 186 LEPKDLYDALDRYFDYDSLTKlPQRSQVQAQLAQPLQRELISMDRYELPSSiddideLIREAIQSESSLVRQAQNELAEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 585 REKIgvhvgfEEILnmepyccrETLKSlrpecFIYDLSAVVMHHGKGfGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDE 664
Cdd:cd02666 266 KHEI------EKQF--------DDLKS-----YGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDETVTVVPASE 325
|
410
....*....|....*..
gi 109134334 665 V------CKAQAYILFY 675
Cdd:cd02666 326 VflftlgNTATPYFLVY 342
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
566-675 |
4.32e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 42.55 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134334 566 LPQVLRLHLKRFRWsGRNNREKIGVHVGFEEILNMEPYccretlkslrpecfiyDLSAVVMHHGKGfGSGHYTAYCYNSE 645
Cdd:cd02665 128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 109134334 646 GGFWVHCNDSKLSMCTMDEVCK--------AQAYILFY 675
Cdd:cd02665 190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| |
