|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
271-676 |
2.50e-71 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 234.64 E-value: 2.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 271 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgfacsrh 350
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 351 pglssglsggaskgrNMELIQPREPSSPYSSLCHELHTLFQVMWSGEW-ALVSPFAMLHSVWKLIPAFRGYAQQDAQEFL 429
Cdd:pfam00443 31 ---------------RISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 430 CELLDKIQRELEttgtklpaliptsqRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPErYQCSGK 509
Cdd:pfam00443 96 LFLLDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-DSAELK 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 510 DAASQPCLVtdmlgKFTETEALEGKI-YVCDHCNSKrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSgRNNREK 588
Cdd:pfam00443 161 TASLQICFL-----QFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN-RSTWEK 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 589 IGVHVVFEETLNMEPYCCSEtLNALRPECFIYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTME-EVL 667
Cdd:pfam00443 224 LNTEVEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVL 301
|
....*....
gi 2020023483 668 RAQAYILFY 676
Cdd:pfam00443 302 SSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-677 |
7.92e-66 |
|
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: 220.71 E-value: 7.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarSYKHSAVTDAataaahqlnegqekekgfacsrhp 351
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 glssglsggaskgrnmeliqprepSSPYSSLCHELHTLFQVMW-SGEWALVSPFAMLHSVWKLIPAFRGYAQQDAQEFLC 430
Cdd:cd02660 41 ------------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 431 ELLDKIQRELetTGTKLPALIPTSQRRLIEQvlnvvnnIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPERYQCSGKD 510
Cdd:cd02660 97 FLLDQLHTHY--GGDKNEANDESHCNCIIHQ-------TFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 511 AAS----QPCLvTDMLGKFTETEALEGKIYVCDHCNSKRrkfsskpvvltEAQKQLMICHLPQVLRLHLKRFRWSGRNNR 586
Cdd:cd02660 168 GESgvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKTS 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 587 EKIGVHVVFEETLNMEPYCCSET----LNALRPECFIYNLSAVVIHHGKgFGSGHYTAYCYNsEGGFWVHCNDSKLSMCT 662
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVS 313
|
410
....*....|....*
gi 2020023483 663 MEEVLRAQAYILFYT 677
Cdd:cd02660 314 EEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
422-676 |
6.53e-59 |
|
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: 199.63 E-value: 6.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 422 QQDAQEFLCELLDKIQRELETTGTKlpaliptsqRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFP 501
Cdd:cd02257 22 QQDAHEFLLFLLDKLHEELKKSSKR---------TSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 502 ERyqcsgkdaASQPCLVTDMLGKFTETEALEGkiYVCDHCNSKRrkfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWS 581
Cdd:cd02257 93 VK--------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLKRFSFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 582 GRNNREKIGVHVVFEETLNMEPYC-CSETLNALRPECFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSM 660
Cdd:cd02257 154 EDGTKEKLNTKVSFPLELDLSPYLsEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTE 233
|
250 260
....*....|....*....|.
gi 2020023483 661 CTMEEVLR-----AQAYILFY 676
Cdd:cd02257 234 VSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
271-676 |
3.54e-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: 185.56 E-value: 3.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 271 TGLRNLGNTCYMNSVLQVLSHllifrqcflkldlnqwlAVAASDKARSYKHSAVtdaataaahqlnegqekekgfaCSRH 350
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH-----------------TPPLANYLLSREHSKD----------------------CCNE 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 351 pglssglsgGASKGRNME--LIQPREPSSPYSslchelhtlfqvmwsgewALVSPFAMLHSVWKlipAFRGYAQQDAQEF 428
Cdd:cd02661 43 ---------GFCMMCALEahVERALASSGPGS------------------APRIFSSNLKQISK---HFRIGRQEDAHEF 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 429 LCELLDKIQRelettgTKLPALIPTSQRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFperyqcsg 508
Cdd:cd02661 93 LRYLLDAMQK------ACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI-------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 509 KDAASqpclVTDMLGKFTETEALEGK-IYVCDHCNSKrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFrwsGRNNRE 587
Cdd:cd02661 159 KGADS----LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 588 KIGVHVVFEETLNMEPYCCSETLNALrpecfIYNLSAVVIHHGKGFGSGHYTAYCYNSEgGFWVHCNDSKLSMCTMEEVL 667
Cdd:cd02661 221 KINKQISFPETLDLSPYMSQPNDGPL-----KYKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDDSKVSPVSIETVL 294
|
....*....
gi 2020023483 668 RAQAYILFY 676
Cdd:cd02661 295 SQKAYILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
422-677 |
6.99e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 163.23 E-value: 6.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 422 QQDAQEFLCELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFP 501
Cdd:cd02674 22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 502 ERYQCSGKdaasqpCLVTDMLGKFTETEALEGKIYV-CDHCNSKRRkfsskpvvlteAQKQLMICHLPQVLRLHLKRFRW 580
Cdd:cd02674 76 SGSGDAPK------VTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLKRFSF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 581 SGRNnREKIGVHVVFE-ETLNMEPYCcsetLNALRPECFIYNLSAVVIHHGKGFGsGHYTAYCYNSEGGFWVHCNDSKLS 659
Cdd:cd02674 139 SRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDDSRVT 212
|
250
....*....|....*...
gi 2020023483 660 MCTMEEVLRAQAYILFYT 677
Cdd:cd02674 213 KVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
381-676 |
9.69e-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: 164.48 E-value: 9.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 381 SLCHELHTLFQVmwsgewalvSPFAMLHSVWKLIPAFRGYAQQDAQEFLCELLDKIQrelettgtklpaliptsqrrlie 460
Cdd:cd02667 19 SQTPALRELLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR----------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 461 qvlNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLefPEryqcsgKDAASQPCLVTDMLGKFTETEALEGK-IYVCD 539
Cdd:cd02667 67 ---TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL--PR------SDEIKSECSIESCLKQFTEVEILEGNnKFACE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 540 HCnskrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMEPYCCSETLNALRPECFI 619
Cdd:cd02667 136 NC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVL 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023483 620 YNLSAVVIHHGkGFGSGHYTAYCY------------------NSEG---GFWVHCNDSKLSMCTMEEVLRAQAYILFY 676
Cdd:cd02667 202 YRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-676 |
7.83e-41 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 152.41 E-value: 7.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWlavAASDKARSYkhsavtdaataaahQLnegqEKEKGFAcsrhp 351
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED---DDDNKSVPL--------------AL----QRLFLFL----- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 glssglsggaskgRNMEliqprepsSPYSSlcHELHTLFQVMWsgewalvspfamlhsvWKLIPAFRgyaQQDAQEFLCE 431
Cdd:cd02659 58 -------------QLSE--------SPVKT--TELTDKTRSFG----------------WDSLNTFE---QHDVQEFFRV 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 432 LLDKIQRELEttGTKLPALIptsqrrlieqvlnvvNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEfperyqcsGKDA 511
Cdd:cd02659 96 LFDKLEEKLK--GTGQEGLI---------------KNLFGGKLVNYIICKECPHESEREEYFLDLQVA--------VKGK 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 512 ASqpclVTDMLGKFTETEALEG-KIYVCDHCNSKRRkfsskpvvlteAQKQLMICHLPQVLRLHLKRFRWSG-RNNREKI 589
Cdd:cd02659 151 KN----LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKI 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 590 GVHVVFEETLNMEPYC------CSETLNALRPECFIYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTM 663
Cdd:cd02659 216 NDRFEFPLELDMEPYTekglakKEGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDP 294
|
410 420 430
....*....|....*....|....*....|....*
gi 2020023483 664 EEVLRAQ----------------------AYILFY 676
Cdd:cd02659 295 NDAEEECfggeetqktydsgprafkrttnAYMLFY 329
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
379-677 |
1.13e-38 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 145.15 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 379 YSSLCHELHTLFQVMWSGE--WALVSPFAMLHSVWKLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPALIPTSQR 456
Cdd:cd02663 20 FENLLTCLKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 457 RLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPERYQcsgkdaasqpclVTDMLGKFTETEALEGK-I 535
Cdd:cd02663 100 NNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTS------------ITSCLRQFSATETLCGRnK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 536 YVCDHCNSKRrkfsskpvvltEAQKQLMICHLPQVLRLHLKRFRWSGRNNR-EKIGVHVVFEETLNMepycCSETLNALR 614
Cdd:cd02663 168 FYCDECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFPLELRL----FNTTDDAEN 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020023483 615 PeCFIYNLSAVVIHHGKGFGSGHYTAYCYNSegGFWVHCNDSKLSMCTMEEVLR--------AQAYILFYT 677
Cdd:cd02663 233 P-DRLYELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-659 |
3.56e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 136.01 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgFACSRHP 351
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE-------------------------------------------CNSTEDA 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 GLssglsggaskgRNMELIQPREPSSPysslCHELHTLFQVMWSGEWALVSPFAmlhsvwkLIPAFR--GYAQQDAQEFL 429
Cdd:cd02668 38 EL-----------KNMPPDKPHEPQTI----IDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFS 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 430 CELLDKIQRELETTGTKlpaliptsqrrlieQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFperyqcsgK 509
Cdd:cd02668 96 KLFLSLLEAKLSKSKNP--------------DLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--------K 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 510 DAASqpclVTDMLGKFTETEALEG-KIYVCDHCNSKRRkfsskpvvlteAQKQLMICHLPQVLRLHLKRF---RWSGRnn 585
Cdd:cd02668 154 GHKT----LEECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTGA-- 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020023483 586 REKIGVHVVFEETLNMEPYCCSETLNAlrpecFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLS 659
Cdd:cd02668 217 KKKLNASISFPEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVE 285
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-676 |
1.81e-27 |
|
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: 113.74 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLdlnqwlavaasdkarsykhsavtdaataaaHQLNEGQEKEKGFAcsrhp 351
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL------------------------------NLPRLGDSQSVMKK----- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 glssglsggaskgrnmeliqprepsspysslchELHTLFQVMWSGEWALVSPFAMLHSVWKliPAFRGYAQQDAQEFLCE 431
Cdd:cd02664 46 ---------------------------------LQLLQAHLMHTQRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRY 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 432 LLDKIQRelettgtklpaliptsqrrLIEQVlnvvnniFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPeryqcsgkda 511
Cdd:cd02664 91 LLDRLHT-------------------LIEKM-------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 512 asqpcLVTDMLGKFTETEALEGK-IYVCDHCNSkrrkfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNREKI 589
Cdd:cd02664 135 -----SVQDLLNYFLSPEKLTGDnQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDqKTHVREKI 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 590 GVHVVFEETLNM----------EPYCCSETLNALRPE-CFI---YNLSAVVIHHGKGFGSGHYtaYCY------------ 643
Cdd:cd02664 199 MDNVSINEVLSLpvrvesksseSPLEKKEEESGDDGElVTRqvhYRLYAVVVHSGYSSESGHY--FTYardqtdadstgq 276
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2020023483 644 ----------NSEGGFWVHCNDSKLSMCTMEEVLRAQ-------AYILFY 676
Cdd:cd02664 277 ecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-676 |
9.02e-27 |
|
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: 111.91 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 268 PGVTGLRNLGNTCYMNSVLQVLshllifRQCflkldlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgfac 347
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVL------YFC------------------------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 348 srhPGLSSGLSGGASKGRNMELIQprepsspysSLCHELHTLFqvmwSGEWALVSPFAMLHSVWKLIPAFRGYAQQDAQE 427
Cdd:cd02671 47 ---PGFKHGLKHLVSLISSVEQLQ---------SSFLLNPEKY----NDELANQAPRRLLNALREVNPMYEGYLQHDAQE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 428 FLCELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPERYQCS 507
Cdd:cd02671 111 VLQCILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 508 GKDAAS-QPCLVTDM------LGKFTETEALEGK-IYVCDHCNSkrrkfsskpvvLTEAQKQLMICHLPQVLRLHLKRFR 579
Cdd:cd02671 165 SEESSEiSPDPKTEMktlkwaISQFASVERIVGEdKYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 580 WSGRNNR-----EKIGVHVVFEETLNMEPYCCSETLNalrpecfIYNLSAVVIHHGKGFGSGHYTAYCYnseggfWVHCN 654
Cdd:cd02671 234 ANGSEFDcygglSKVNTPLLTPLKLSLEEWSTKPKND-------VYRLFAVVMHSGATISSGHYTAYVR------WLLFD 300
|
410 420 430
....*....|....*....|....*....|.
gi 2020023483 655 DSKLSMCTMEEVLRAQA---------YILFY 676
Cdd:cd02671 301 DSEVKVTEEKDFLEALSpntsststpYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
414-676 |
3.12e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 105.14 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 414 IPAFRGY-----AQQDAQEFLCELLDKIQRELEttgtklpaliptsqrrlieqvlnvvnNIFHGQLLSQVTCLACNNKSN 488
Cdd:cd02662 21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 489 -TIEPFWDLSLEFPERYQCSGkdaasqpCLVTDMLGKFTETEALEGkiYVCDHCnskrrkfsskpvvlteaqkQLMICHL 567
Cdd:cd02662 75 vRYESFTMLSLPVPNQSSGSG-------TTLEHCLDDFLSTEIIDD--YKCDRC-------------------QTVIVRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 568 PQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMepyccsetlnalrpecFIYNLSAVVIHHGkGFGSGHYTAY------ 641
Cdd:cd02662 127 PQILCIHLSRSVFDGRGTSTKNSCKVSFPERLPK----------------VLYRLRAVVVHYG-SHSSGHYVCYrrkplf 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2020023483 642 --------------CYNSEGGFWVHCNDSKLSMCTMEEVL-RAQAYILFY 676
Cdd:cd02662 190 skdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-676 |
5.89e-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: 102.79 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlavaasdkarsykhsavtdaataaaHQLNEGQEKEKGFACSRhp 351
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL-------------------------------------------RSVPELRDALKNYNPAR-- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 glssglsggaskgrnmeliqpREPSSPYSSLCHELHTLFQVMWSGEWAlVSPFAMLHSVWKLIPAF------RGYAQQDA 425
Cdd:cd02657 36 ---------------------RGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMAFPQFaekqnqGGYAQQDA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 426 QEFLCELLDKIQRELEttgtklpalIPTSQRRLIEQvlnvvnnIFHGQLLSQVTCLAC-NNKSNTIEPFWDLSLefpery 504
Cdd:cd02657 94 EECWSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESpDEEEVSTESEYKLQC------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 505 QCSGKDAASQpcLVTDMLGKFTETEalegkiyvcdhcnskrRKFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGR- 583
Cdd:cd02657 152 HISITTEVNY--LQDGLKKGLEEEI----------------EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDi 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 584 NNREKIGVHVVFEETLNMEPYCCsetlnalrpECFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTM 663
Cdd:cd02657 214 QKKAKILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTE 284
|
410 420
....*....|....*....|
gi 2020023483 664 EEVLRAQ-------AYILFY 676
Cdd:cd02657 285 EDILKLSgggdwhiAYILLY 304
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-87 |
1.84e-21 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 88.09 E-value: 1.84e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020023483 26 CMVCNTTESIWACLSCSHVACGQYIQEHALKHFEESSHPVAFEVNDMYVFCYLCNDYVLNDN 87
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
272-678 |
1.47e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.48 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlaVAASDKARSYkhsavtdaataaahqlnegqekekgfacsrhp 351
Cdd:COG5533 1 GLPNLGNTCFMNSVLQIL--------------------ALYLPKLDEL-------------------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 glsSGLSGGASKgrnmELIQPREPSSPYSSLCHELHTLFQVMWSGEWALVSPFAMlhsvwklipafrgYAQQDAQEFLCE 431
Cdd:COG5533 29 ---LDDLSKELK----VLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGWIPPM-------------GSQEDAHELLGK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 432 LLDKIQRELETTGTklpaliptsqrRLIEQVLNvvnnifhgqllsqvtclacNNKSNTIEPFWDLSLEFPerYQCSGKDA 511
Cdd:COG5533 89 LLDELKLDLVNSFT-----------IRIFKTTK-------------------DKKKTSTGDWFDIIIELP--DQTWVNNL 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 512 ASQPCLVTDMlgkftetealegKIYVCDHCNSKRRKFSSKPVVlTEAQKQLMICHLPQVLRLHLKRFRWSGRNnrEKIGV 591
Cdd:COG5533 137 KTLQEFIDNM------------EELVDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLGGN--QKIDT 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 592 HVvfEETLNMePYCCSETLNaLRPEcFIYNLSAVVIHHGkGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMEEVL---R 668
Cdd:COG5533 202 EV--DEKFEL-PVKHDQILN-IVKE-TYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAInekA 273
|
410
....*....|
gi 2020023483 669 AQAYILFYTQ 678
Cdd:COG5533 274 KNAYLYFYER 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
269-679 |
3.97e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 92.25 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 269 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkARSYKHsavtdaataaahQLNEgqekekgfacS 348
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL---------------SDEYEE------------SINE----------E 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 349 RHPGLSSGLSggaskgrnmeliqprepsSPYSSLCHELHTlfqvmwsGEWALVSPFAMLHSVWKLIPAFRGYAQQDAQEF 428
Cdd:COG5560 307 NPLGMHGSVA------------------SAYADLIKQLYD-------GNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 429 LCELLDKIQREL----ETTGTKLPALIPTSQ---RRLIEQVL--------NVVNNIFHGQLLSQVTCLACNNKSNTIEPF 493
Cdd:COG5560 362 IAFLLDGLHEDLnriiKKPYTSKPDLSPGDDvvvKKKAKECWwehlkrndSIITDLFQGMYKSTLTCPGCGSVSITFDPF 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 494 WDLSLEFPERYQCSGK------DAASQPC---------------LVTDMLGKFTETEALEGKIYV--------------- 537
Cdd:COG5560 442 MDLTLPLPVSMVWKHTivvfpeSGRRQPLkieldasstirglkkLVDAEYGKLGCFEIKVMCIYYggnynmlepadkvll 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 538 -----CDHC----------------------------------------------------------------------- 541
Cdd:COG5560 522 qdipqTDFVylyetndngievpvvhlriekgykskrlfgdpflqlnvlikasiydklvkefeellvlvemkktdvdlvse 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 542 ---------------------NSKRRK----------------------------FSSKPVVLTE--------------- 557
Cdd:COG5560 602 qvrllreesspsswlkleteiDTKREEqveeegqmnfndavvisceweekrylslFSYDPLWTIReigaaertitlqdcl 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 558 -------------------------AQKQLMICHLPQVLRLHLKRFRwSGRNNREKIGVHVVFEET-LNMEPYCCSETLN 611
Cdd:COG5560 682 nefskpeqlglsdswycpgckefrqASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020023483 612 ALrpecfIYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEVLRAQAYILFYTQR 679
Cdd:COG5560 761 RL-----IYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-676 |
4.58e-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: 88.53 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 272 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVAasDKARSYkhsavtdaataaahqlnEGQekekgFACSRHp 351
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVV--DPANDL-----------------NCQ-----LIKLAD- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 352 GLssgLSGGASKgrnmeliqPREPSSPysslchelHTLFQVmwsGewalVSPFAMLHSVWKLIPAFRGYAQQDAQEFLCE 431
Cdd:cd02658 56 GL---LSGRYSK--------PASLKSE--------NDPYQV---G----IKPSMFKALIGKGHPEFSTMRQQDALEFLLH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 432 LLDKIQRELETTGTKLPaliptsqrrlieqvlnvvNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPER---YQCSG 508
Cdd:cd02658 110 LIDKLDRESFKNLGLNP------------------NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeatEKEEG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 509 KDAASQPCLVtDMLGKFTETEALEGKiyvCDHCNSKrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREK 588
Cdd:cd02658 172 ELVYEPVPLE-DCLKAYFAPETIEDF---CSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 589 IGVHVVFEETLNMEPyccsetlnalrpecfiYNLSAVVIHHGKGFGSGHYTAYCY--NSEGGFWVHCNDSKLSMCTMEEV 666
Cdd:cd02658 237 LDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPE 300
|
410
....*....|
gi 2020023483 667 LRAQAYILFY 676
Cdd:cd02658 301 MKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
269-667 |
3.13e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 89.54 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 269 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLdlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgfacs 348
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------------------------------------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 349 rhpglssglsggaskgrnmeliqPREPSSPYSSLCHELHTLFQVMWSGEWALVSPFAMLHSVWKlipAFRGYAQQDAQEF 428
Cdd:COG5077 226 -----------------------PTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWD---SDDSFMQHDIQEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 429 LCELLDKIQRELETTgtklpaliptsqrrlieQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLslefperyQCSG 508
Cdd:COG5077 280 NRVLQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDI--------QLNV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 509 KDAASqpclVTDMLGKFTETEALEGKiyvcdhcnskrRKFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNRE 587
Cdd:COG5077 335 KGMKN----LQESFRRYIQVETLDGD-----------NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 588 KIGVHVVFEETLNMEPYCCSETLNALRPECfIYNLSAVVIHHGKgFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEVL 667
Cdd:COG5077 400 KINDRYEFPLEIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVL 477
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
25-71 |
3.62e-12 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 61.23 E-value: 3.62e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2020023483 25 FCMVCNTTESIWACLSCSHVACGQYIQEHALKHFEESSHPVAFEVND 71
Cdd:smart00290 1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGT 47
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
271-676 |
7.01e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 64.43 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 271 TGLRNLGNTCYMNSVLQVLSHLLIFRQcfLKLDLNQWLAVAASDKARSYKhsavtdaataaahqlnEGQEKEkgfacsrh 350
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRD--LVLNFDESKAELASDYPTERR----------------IGGREV-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 351 pglssglsggaskgRNMELIQPREpsspyssLCHELHTLFQVMWSGEWALVSPFAMLhsvwklipAFRGYAQQDAQEFLC 430
Cdd:cd02666 56 --------------SRSELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTECID 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 431 ELLDKIQRELETTGTklpALIPTSQRRLIEQVlNVVNNIFHGQLLSQVT-CLACNNKSNTIEPFWDLSLEFPERYQCSGK 509
Cdd:cd02666 107 NVLFQLEVALEPISN---AFAGPDTEDDKEQS-DLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVDVGKKGREI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 510 DAASQPCLVTDMLGKFTETEALEgkiyvcdhcNSKRRKFSSKPVVLTEAQKQLmichlpqvlrlhlkrfrwSGRNNREKI 589
Cdd:cd02666 183 VVLLEPKDLYDALDRYFDYDSLT---------KLPQRSQVQAQLAQPLQRELI------------------SMDRYELPS 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 590 GVHVVFE------ETLNMEPYCCSETLNALRPEC---------FIYNLSAVVIHHGKGfGSGHYTAYCYNSEGGFWVHCN 654
Cdd:cd02666 236 SIDDIDElireaiQSESSLVRQAQNELAELKHEIekqfddlksYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYN 314
|
410 420
....*....|....*....|....*...
gi 2020023483 655 DSKLSMCTMEEVL------RAQAYILFY 676
Cdd:cd02666 315 DETVTVVPASEVFlftlgnTATPYFLVY 342
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
268-676 |
9.36e-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: 64.65 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 268 PGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarsykhsavtdaataaahqLNEGQEKEKGfac 347
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL----------------------------------LYENYENIKD--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 348 sRHPGLSSGLSggaskgrnmELIqpREPSSPYsslchelhtLFQvmwsgewALVSPFAMLHSVWKLIPA-FRGYAQQDAQ 426
Cdd:cd02669 160 -RKSELVKRLS---------ELI--RKIWNPR---------NFK-------GHVSPHELLQAVSKVSKKkFSITEQSDPV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 427 EFLCELLDKIQRELETTGTKLPALIPTS-QRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIePFWDLSLEFPER-- 503
Cdd:cd02669 212 EFLSWLLNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPpl 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 504 YQcSGKDAASQP-CLVTDMLGKFTETEalegkiyvCDHCNSKRRKFsskpvvlteaqkqlMICHLPQVLRLHLKRFRwsg 582
Cdd:cd02669 291 FK-DGNEENIIPqVPLKQLLKKYDGKT--------ETELKDSLKRY--------------LISRLPKYLIFHIKRFS--- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 583 RNN--REKIGVHVVFEETLNMEPYCCSETLNALrPECFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSM 660
Cdd:cd02669 345 KNNffKEKNPTIVNFPIKNLDLSDYVHFDKPSL-NLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKE 423
|
410
....*....|....*.
gi 2020023483 661 CTMEEVLRAQAYILFY 676
Cdd:cd02669 424 VLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
407-676 |
9.69e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 56.77 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 407 LHSVWKLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPAlIPTSQRRLieqvlNVVNnIFHGQLLSQVTCLACNNK 486
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPP-SNIEIKRL-----NPLE-AFKYTIESSYVCIGCSFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 487 SNTIEPFWDLSLEFPEryqcsgkdaaSQPCLVTDMLGKFTETEALEGKIYVCDHCNSkrrkfSSKPVVLTeaqkqlmich 566
Cdd:cd02673 91 ENVSDVGNFLDVSMID----------NKLDIDELLISNFKTWSPIEKDCSSCKCESA-----ISSERIMT---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 567 LPQVLRLHLKRFRWsgrnnREKIGVHVVFEEtLNMEPYCcSETLNalrpecfiYNLSAVVIHHGKGFGSGHYTAYCYN-S 645
Cdd:cd02673 146 FPECLSINLKRYKL-----RIATSDYLKKNE-EIMKKYC-GTDAK--------YSLVAVICHLGESPYDGHYIAYTKElY 210
|
250 260 270
....*....|....*....|....*....|....
gi 2020023483 646 EGGFWVHCNDSKLSMCTMEEVL---RAQAYILFY 676
Cdd:cd02673 211 NGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
567-676 |
5.88e-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: 45.24 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020023483 567 LPQVLRLHLKRFRWsGRNNREKIGVHVVFEETLNMEPYccsetlnalrpecfiyNLSAVVIHHGKGfGSGHYTAYCYNSE 646
Cdd:cd02665 128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 2020023483 647 GGFWVHCNDSKLSMCTMEEVLR--------AQAYILFY 676
Cdd:cd02665 190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| |
