|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
288-693 |
2.01e-71 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 235.41 E-value: 2.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 288 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgfacsrh 367
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 368 pglssglsggaskgrNMELIQPREPSSPYSSLCHELHTLFQVMWSGEW-ALVSPFAMLHSVWKLIPAFRGYAQQDAQEFL 446
Cdd:pfam00443 31 ---------------RISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 447 CELLDKIQRELEttgtklpaliptsqRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPErYQCSGK 526
Cdd:pfam00443 96 LFLLDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-DSAELK 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 527 DAASQPCLVtdmlgKFTETEALEGKI-YVCDHCNSKrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSgRNNREK 605
Cdd:pfam00443 161 TASLQICFL-----QFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN-RSTWEK 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 606 IGVHVVFEETLNMEPYCCSEtLNALRPECFIYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTME-EVL 684
Cdd:pfam00443 224 LNTEVEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVL 301
|
....*....
gi 1958789268 685 RAQAYILFY 693
Cdd:pfam00443 302 SSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
289-694 |
6.85e-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: 221.09 E-value: 6.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarSYKHSAVTDAataaahqlnegqekekgfacsrhp 368
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 glssglsggaskgrnmeliqprepSSPYSSLCHELHTLFQVMW-SGEWALVSPFAMLHSVWKLIPAFRGYAQQDAQEFLC 447
Cdd:cd02660 41 ------------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 448 ELLDKIQRELetTGTKLPALIPTSQRRLIEQvlnvvnnIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPERYQCSGKD 527
Cdd:cd02660 97 FLLDQLHTHY--GGDKNEANDESHCNCIIHQ-------TFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 528 AAS----QPCLvTDMLGKFTETEALEGKIYVCDHCNSKRrkfsskpvvltEAQKQLMICHLPQVLRLHLKRFRWSGRNNR 603
Cdd:cd02660 168 GESgvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKTS 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 604 EKIGVHVVFEETLNMEPYCCSET----LNALRPECFIYNLSAVVIHHGKgFGSGHYTAYCYNsEGGFWVHCNDSKLSMCT 679
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVS 313
|
410
....*....|....*
gi 1958789268 680 MEEVLRAQAYILFYT 694
Cdd:cd02660 314 EEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
439-693 |
4.73e-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: 200.40 E-value: 4.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 439 QQDAQEFLCELLDKIQRELETTGTKlpaliptsqRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFP 518
Cdd:cd02257 22 QQDAHEFLLFLLDKLHEELKKSSKR---------TSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 519 ERyqcsgkdaASQPCLVTDMLGKFTETEALEGkiYVCDHCNSKRrkfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWS 598
Cdd:cd02257 93 VK--------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLKRFSFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 599 GRNNREKIGVHVVFEETLNMEPYC-CSETLNALRPECFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSM 677
Cdd:cd02257 154 EDGTKEKLNTKVSFPLELDLSPYLsEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTE 233
|
250 260
....*....|....*....|.
gi 1958789268 678 CTMEEVLR-----AQAYILFY 693
Cdd:cd02257 234 VSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
288-693 |
2.97e-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: 186.33 E-value: 2.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 288 TGLRNLGNTCYMNSVLQVLSHllifrqcflkldlnqwlAVAASDKARSYKHSAVtdaataaahqlnegqekekgfaCSRH 367
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH-----------------TPPLANYLLSREHSKD----------------------CCNE 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 368 pglssglsgGASKGRNME--LIQPREPSSPYSslchelhtlfqvmwsgewALVSPFAMLHSVWKlipAFRGYAQQDAQEF 445
Cdd:cd02661 43 ---------GFCMMCALEahVERALASSGPGS------------------APRIFSSNLKQISK---HFRIGRQEDAHEF 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 446 LCELLDKIQRelettgTKLPALIPTSQRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFperyqcsg 525
Cdd:cd02661 93 LRYLLDAMQK------ACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI-------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 526 KDAASqpclVTDMLGKFTETEALEGK-IYVCDHCNSKrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFrwsGRNNRE 604
Cdd:cd02661 159 KGADS----LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 605 KIGVHVVFEETLNMEPYCCSETLNALrpecfIYNLSAVVIHHGKGFGSGHYTAYCYNSEgGFWVHCNDSKLSMCTMEEVL 684
Cdd:cd02661 221 KINKQISFPETLDLSPYMSQPNDGPL-----KYKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDDSKVSPVSIETVL 294
|
....*....
gi 1958789268 685 RAQAYILFY 693
Cdd:cd02661 295 SQKAYILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-694 |
6.38e-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: 163.61 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 439 QQDAQEFLCELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFP 518
Cdd:cd02674 22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 519 ERYQCSGKdaasqpCLVTDMLGKFTETEALEGKIYV-CDHCNSKRRkfsskpvvlteAQKQLMICHLPQVLRLHLKRFRW 597
Cdd:cd02674 76 SGSGDAPK------VTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLKRFSF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 598 SGRNnREKIGVHVVFE-ETLNMEPYCcsetLNALRPECFIYNLSAVVIHHGKGFGsGHYTAYCYNSEGGFWVHCNDSKLS 676
Cdd:cd02674 139 SRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDDSRVT 212
|
250
....*....|....*...
gi 1958789268 677 MCTMEEVLRAQAYILFYT 694
Cdd:cd02674 213 KVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
398-693 |
1.00e-45 |
|
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: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 398 SLCHELHTLFQVmwsgewalvSPFAMLHSVWKLIPAFRGYAQQDAQEFLCELLDKIQrelettgtklpaliptsqrrlie 477
Cdd:cd02667 19 SQTPALRELLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR----------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 478 qvlNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLefPEryqcsgKDAASQPCLVTDMLGKFTETEALEGK-IYVCD 556
Cdd:cd02667 67 ---TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL--PR------SDEIKSECSIESCLKQFTEVEILEGNnKFACE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 557 HCnskrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMEPYCCSETLNALRPECFI 636
Cdd:cd02667 136 NC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVL 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789268 637 YNLSAVVIHHGkGFGSGHYTAYCY------------------NSEG---GFWVHCNDSKLSMCTMEEVLRAQAYILFY 693
Cdd:cd02667 202 YRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
289-693 |
6.46e-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: 152.80 E-value: 6.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWlavAASDKARSYkhsavtdaataaahQLnegqEKEKGFAcsrhp 368
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED---DDDNKSVPL--------------AL----QRLFLFL----- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 glssglsggaskgRNMEliqprepsSPYSSlcHELHTLFQVMWsgewalvspfamlhsvWKLIPAFRgyaQQDAQEFLCE 448
Cdd:cd02659 58 -------------QLSE--------SPVKT--TELTDKTRSFG----------------WDSLNTFE---QHDVQEFFRV 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 449 LLDKIQRELEttGTKLPALIptsqrrlieqvlnvvNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEfperyqcsGKDA 528
Cdd:cd02659 96 LFDKLEEKLK--GTGQEGLI---------------KNLFGGKLVNYIICKECPHESEREEYFLDLQVA--------VKGK 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 529 ASqpclVTDMLGKFTETEALEG-KIYVCDHCNSKRRkfsskpvvlteAQKQLMICHLPQVLRLHLKRFRWSG-RNNREKI 606
Cdd:cd02659 151 KN----LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKI 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 607 GVHVVFEETLNMEPYC------CSETLNALRPECFIYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTM 680
Cdd:cd02659 216 NDRFEFPLELDMEPYTekglakKEGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDP 294
|
410 420 430
....*....|....*....|....*....|....*
gi 1958789268 681 EEVLRAQ----------------------AYILFY 693
Cdd:cd02659 295 NDAEEECfggeetqktydsgprafkrttnAYMLFY 329
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-694 |
9.39e-39 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 145.53 E-value: 9.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 396 YSSLCHELHTLFQVMWSGE--WALVSPFAMLHSVWKLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPALIPTSQR 473
Cdd:cd02663 20 FENLLTCLKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 474 RLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPERYQcsgkdaasqpclVTDMLGKFTETEALEGK-I 552
Cdd:cd02663 100 NNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTS------------ITSCLRQFSATETLCGRnK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 553 YVCDHCNSKRrkfsskpvvltEAQKQLMICHLPQVLRLHLKRFRWSGRNNR-EKIGVHVVFEETLNMepycCSETLNALR 631
Cdd:cd02663 168 FYCDECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFPLELRL----FNTTDDAEN 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789268 632 PeCFIYNLSAVVIHHGKGFGSGHYTAYCYNSegGFWVHCNDSKLSMCTMEEVLR--------AQAYILFYT 694
Cdd:cd02663 233 P-DRLYELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
289-676 |
3.12e-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: 136.40 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgFACSRHP 368
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE-------------------------------------------CNSTEDA 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 GLssglsggaskgRNMELIQPREPSSPysslCHELHTLFQVMWSGEWALVSPFAmlhsvwkLIPAFR--GYAQQDAQEFL 446
Cdd:cd02668 38 EL-----------KNMPPDKPHEPQTI----IDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFS 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 447 CELLDKIQRELETTGTKlpaliptsqrrlieQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFperyqcsgK 526
Cdd:cd02668 96 KLFLSLLEAKLSKSKNP--------------DLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--------K 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 527 DAASqpclVTDMLGKFTETEALEG-KIYVCDHCNSKRRkfsskpvvlteAQKQLMICHLPQVLRLHLKRF---RWSGRnn 602
Cdd:cd02668 154 GHKT----LEECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTGA-- 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958789268 603 REKIGVHVVFEETLNMEPYCCSETLNAlrpecFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLS 676
Cdd:cd02668 217 KKKLNASISFPEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVE 285
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
289-693 |
2.18e-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: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLdlnqwlavaasdkarsykhsavtdaataaaHQLNEGQEKEKGFAcsrhp 368
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL------------------------------NLPRLGDSQSVMKK----- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 glssglsggaskgrnmeliqprepsspysslchELHTLFQVMWSGEWALVSPFAMLHSVWKliPAFRGYAQQDAQEFLCE 448
Cdd:cd02664 46 ---------------------------------LQLLQAHLMHTQRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRY 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 449 LLDKIQRelettgtklpaliptsqrrLIEQVlnvvnniFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPeryqcsgkda 528
Cdd:cd02664 91 LLDRLHT-------------------LIEKM-------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 529 asqpcLVTDMLGKFTETEALEGK-IYVCDHCNSkrrkfsskpvvLTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNREKI 606
Cdd:cd02664 135 -----SVQDLLNYFLSPEKLTGDnQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDqKTHVREKI 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 607 GVHVVFEETLNM----------EPYCCSETLNALRPE-CFI---YNLSAVVIHHGKGFGSGHYtaYCY------------ 660
Cdd:cd02664 199 MDNVSINEVLSLpvrvesksseSPLEKKEEESGDDGElVTRqvhYRLYAVVVHSGYSSESGHY--FTYardqtdadstgq 276
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958789268 661 ----------NSEGGFWVHCNDSKLSMCTMEEVLRAQ-------AYILFY 693
Cdd:cd02664 277 ecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
285-693 |
9.93e-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: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 285 PGVTGLRNLGNTCYMNSVLQVLshllifRQCflkldlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgfac 364
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVL------YFC------------------------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 365 srhPGLSSGLSGGASKGRNMELIQprepsspysSLCHELHTLFqvmwSGEWALVSPFAMLHSVWKLIPAFRGYAQQDAQE 444
Cdd:cd02671 47 ---PGFKHGLKHLVSLISSVEQLQ---------SSFLLNPEKY----NDELANQAPRRLLNALREVNPMYEGYLQHDAQE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 445 FLCELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPERYQCS 524
Cdd:cd02671 111 VLQCILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 525 GKDAAS-QPCLVTDM------LGKFTETEALEGK-IYVCDHCNSkrrkfsskpvvLTEAQKQLMICHLPQVLRLHLKRFR 596
Cdd:cd02671 165 SEESSEiSPDPKTEMktlkwaISQFASVERIVGEdKYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 597 WSGRNNR-----EKIGVHVVFEETLNMEPYCCSETLNalrpecfIYNLSAVVIHHGKGFGSGHYTAYCYnseggfWVHCN 671
Cdd:cd02671 234 ANGSEFDcygglSKVNTPLLTPLKLSLEEWSTKPKND-------VYRLFAVVMHSGATISSGHYTAYVR------WLLFD 300
|
410 420 430
....*....|....*....|....*....|.
gi 1958789268 672 DSKLSMCTMEEVLRAQA---------YILFY 693
Cdd:cd02671 301 DSEVKVTEEKDFLEALSpntsststpYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
431-693 |
2.84e-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: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 431 IPAFRGY-----AQQDAQEFLCELLDKIQRELEttgtklpaliptsqrrlieqvlnvvnNIFHGQLLSQVTCLACNNKSN 505
Cdd:cd02662 21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 506 -TIEPFWDLSLEFPERYQCSGkdaasqpCLVTDMLGKFTETEALEGkiYVCDHCnskrrkfsskpvvlteaqkQLMICHL 584
Cdd:cd02662 75 vRYESFTMLSLPVPNQSSGSG-------TTLEHCLDDFLSTEIIDD--YKCDRC-------------------QTVIVRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 585 PQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMepyccsetlnalrpecFIYNLSAVVIHHGkGFGSGHYTAY------ 658
Cdd:cd02662 127 PQILCIHLSRSVFDGRGTSTKNSCKVSFPERLPK----------------VLYRLRAVVVHYG-SHSSGHYVCYrrkplf 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958789268 659 --------------CYNSEGGFWVHCNDSKLSMCTMEEVL-RAQAYILFY 693
Cdd:cd02662 190 skdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
289-693 |
5.99e-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: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlavaasdkarsykhsavtdaataaaHQLNEGQEKEKGFACSRhp 368
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL-------------------------------------------RSVPELRDALKNYNPAR-- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 glssglsggaskgrnmeliqpREPSSPYSSLCHELHTLFQVMWSGEWAlVSPFAMLHSVWKLIPAF------RGYAQQDA 442
Cdd:cd02657 36 ---------------------RGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMAFPQFaekqnqGGYAQQDA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 443 QEFLCELLDKIQRELEttgtklpalIPTSQRRLIEQvlnvvnnIFHGQLLSQVTCLAC-NNKSNTIEPFWDLSLefpery 521
Cdd:cd02657 94 EECWSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESpDEEEVSTESEYKLQC------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 522 QCSGKDAASQpcLVTDMLGKFTETEalegkiyvcdhcnskrRKFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGR- 600
Cdd:cd02657 152 HISITTEVNY--LQDGLKKGLEEEI----------------EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDi 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 601 NNREKIGVHVVFEETLNMEPYCCsetlnalrpECFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTM 680
Cdd:cd02657 214 QKKAKILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTE 284
|
410 420
....*....|....*....|
gi 1958789268 681 EEVLRAQ-------AYILFY 693
Cdd:cd02657 285 EDILKLSgggdwhiAYILLY 304
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
43-104 |
1.15e-21 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 88.86 E-value: 1.15e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789268 43 CMVCNTTESIWACLSCSHVACGQYIQEHALKHFEESSHPVAFEVNDMYVFCYLCNDYVLNDN 104
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
289-695 |
1.52e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.48 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlaVAASDKARSYkhsavtdaataaahqlnegqekekgfacsrhp 368
Cdd:COG5533 1 GLPNLGNTCFMNSVLQIL--------------------ALYLPKLDEL-------------------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 glsSGLSGGASKgrnmELIQPREPSSPYSSLCHELHTLFQVMWSGEWALVSPFAMlhsvwklipafrgYAQQDAQEFLCE 448
Cdd:COG5533 29 ---LDDLSKELK----VLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGWIPPM-------------GSQEDAHELLGK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 449 LLDKIQRELETTGTklpaliptsqrRLIEQVLNvvnnifhgqllsqvtclacNNKSNTIEPFWDLSLEFPerYQCSGKDA 528
Cdd:COG5533 89 LLDELKLDLVNSFT-----------IRIFKTTK-------------------DKKKTSTGDWFDIIIELP--DQTWVNNL 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 529 ASQPCLVTDMlgkftetealegKIYVCDHCNSKRRKFSSKPVVlTEAQKQLMICHLPQVLRLHLKRFRWSGRNnrEKIGV 608
Cdd:COG5533 137 KTLQEFIDNM------------EELVDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLGGN--QKIDT 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 609 HVvfEETLNMePYCCSETLNaLRPEcFIYNLSAVVIHHGkGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMEEVL---R 685
Cdd:COG5533 202 EV--DEKFEL-PVKHDQILN-IVKE-TYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAInekA 273
|
410
....*....|
gi 1958789268 686 AQAYILFYTQ 695
Cdd:COG5533 274 KNAYLYFYER 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
286-696 |
4.14e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 92.25 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 286 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkARSYKHsavtdaataaahQLNEgqekekgfacS 365
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL---------------SDEYEE------------SINE----------E 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 366 RHPGLSSGLSggaskgrnmeliqprepsSPYSSLCHELHTlfqvmwsGEWALVSPFAMLHSVWKLIPAFRGYAQQDAQEF 445
Cdd:COG5560 307 NPLGMHGSVA------------------SAYADLIKQLYD-------GNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 446 LCELLDKIQREL----ETTGTKLPALIPTSQ---RRLIEQVL--------NVVNNIFHGQLLSQVTCLACNNKSNTIEPF 510
Cdd:COG5560 362 IAFLLDGLHEDLnriiKKPYTSKPDLSPGDDvvvKKKAKECWwehlkrndSIITDLFQGMYKSTLTCPGCGSVSITFDPF 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 511 WDLSLEFPERYQCSGK------DAASQPC---------------LVTDMLGKFTETEALEGKIYV--------------- 554
Cdd:COG5560 442 MDLTLPLPVSMVWKHTivvfpeSGRRQPLkieldasstirglkkLVDAEYGKLGCFEIKVMCIYYggnynmlepadkvll 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 555 -----CDHC----------------------------------------------------------------------- 558
Cdd:COG5560 522 qdipqTDFVylyetndngievpvvhlriekgykskrlfgdpflqlnvlikasiydklvkefeellvlvemkktdvdlvse 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 559 ---------------------NSKRRK----------------------------FSSKPVVLTE--------------- 574
Cdd:COG5560 602 qvrllreesspsswlkleteiDTKREEqveeegqmnfndavvisceweekrylslFSYDPLWTIReigaaertitlqdcl 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 575 -------------------------AQKQLMICHLPQVLRLHLKRFRwSGRNNREKIGVHVVFEET-LNMEPYCCSETLN 628
Cdd:COG5560 682 nefskpeqlglsdswycpgckefrqASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789268 629 ALrpecfIYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEVLRAQAYILFYTQR 696
Cdd:COG5560 761 RL-----IYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
289-693 |
4.40e-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: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 289 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVAasDKARSYkhsavtdaataaahqlnEGQekekgFACSRHp 368
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVV--DPANDL-----------------NCQ-----LIKLAD- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 369 GLssgLSGGASKgrnmeliqPREPSSPysslchelHTLFQVmwsGewalVSPFAMLHSVWKLIPAFRGYAQQDAQEFLCE 448
Cdd:cd02658 56 GL---LSGRYSK--------PASLKSE--------NDPYQV---G----IKPSMFKALIGKGHPEFSTMRQQDALEFLLH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 449 LLDKIQRELETTGTKLPaliptsqrrlieqvlnvvNNIFHGQLLSQVTCLACNNKSNTIEPFWDLSLEFPER---YQCSG 525
Cdd:cd02658 110 LIDKLDRESFKNLGLNP------------------NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeatEKEEG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 526 KDAASQPCLVtDMLGKFTETEALEGKiyvCDHCNSKrrkfsskpvvlTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREK 605
Cdd:cd02658 172 ELVYEPVPLE-DCLKAYFAPETIEDF---CSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 606 IGVHVVFEETLNMEPyccsetlnalrpecfiYNLSAVVIHHGKGFGSGHYTAYCY--NSEGGFWVHCNDSKLSMCTMEEV 683
Cdd:cd02658 237 LDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPE 300
|
410
....*....|
gi 1958789268 684 LRAQAYILFY 693
Cdd:cd02658 301 MKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
286-684 |
3.29e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 89.54 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 286 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLdlnqwlavaasdkarsykhsavtdaataaahqlnegqekekgfacs 365
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------------------------------------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 366 rhpglssglsggaskgrnmeliqPREPSSPYSSLCHELHTLFQVMWSGEWALVSPFAMLHSVWKlipAFRGYAQQDAQEF 445
Cdd:COG5077 226 -----------------------PTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWD---SDDSFMQHDIQEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 446 LCELLDKIQRELETTgtklpaliptsqrrlieQVLNVVNNIFHGQLLSQVTCLACNNKSNTIEPFWDLslefperyQCSG 525
Cdd:COG5077 280 NRVLQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDI--------QLNV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 526 KDAASqpclVTDMLGKFTETEALEGKiyvcdhcnskrRKFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNRE 604
Cdd:COG5077 335 KGMKN----LQESFRRYIQVETLDGD-----------NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 605 KIGVHVVFEETLNMEPYCCSETLNALRPECfIYNLSAVVIHHGKgFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEVL 684
Cdd:COG5077 400 KINDRYEFPLEIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVL 477
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
42-88 |
3.08e-12 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 61.61 E-value: 3.08e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958789268 42 FCMVCNTTESIWACLSCSHVACGQYIQEHALKHFEESSHPVAFEVND 88
Cdd:smart00290 1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGT 47
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
288-693 |
7.25e-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: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 288 TGLRNLGNTCYMNSVLQVLSHLLIFRQcfLKLDLNQWLAVAASDKARSYKhsavtdaataaahqlnEGQEKEkgfacsrh 367
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRD--LVLNFDESKAELASDYPTERR----------------IGGREV-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 368 pglssglsggaskgRNMELIQPREpsspyssLCHELHTLFQVMWSGEWALVSPFAMLhsvwklipAFRGYAQQDAQEFLC 447
Cdd:cd02666 56 --------------SRSELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTECID 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 448 ELLDKIQRELETTGTklpALIPTSQRRLIEQVlNVVNNIFHGQLLSQVT-CLACNNKSNTIEPFWDLSLEFPERYQCSGK 526
Cdd:cd02666 107 NVLFQLEVALEPISN---AFAGPDTEDDKEQS-DLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVDVGKKGREI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 527 DAASQPCLVTDMLGKFTETEALEgkiyvcdhcNSKRRKFSSKPVVLTEAQKQLmichlpqvlrlhlkrfrwSGRNNREKI 606
Cdd:cd02666 183 VVLLEPKDLYDALDRYFDYDSLT---------KLPQRSQVQAQLAQPLQRELI------------------SMDRYELPS 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 607 GVHVVFE------ETLNMEPYCCSETLNALRPEC---------FIYNLSAVVIHHGKGfGSGHYTAYCYNSEGGFWVHCN 671
Cdd:cd02666 236 SIDDIDElireaiQSESSLVRQAQNELAELKHEIekqfddlksYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYN 314
|
410 420
....*....|....*....|....*...
gi 1958789268 672 DSKLSMCTMEEVL------RAQAYILFY 693
Cdd:cd02666 315 DETVTVVPASEVFlftlgnTATPYFLVY 342
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
285-693 |
9.28e-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: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 285 PGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarsykhsavtdaataaahqLNEGQEKEKGfac 364
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL----------------------------------LYENYENIKD--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 365 sRHPGLSSGLSggaskgrnmELIqpREPSSPYsslchelhtLFQvmwsgewALVSPFAMLHSVWKLIPA-FRGYAQQDAQ 443
Cdd:cd02669 160 -RKSELVKRLS---------ELI--RKIWNPR---------NFK-------GHVSPHELLQAVSKVSKKkFSITEQSDPV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 444 EFLCELLDKIQRELETTGTKLPALIPTS-QRRLIEQVLNVVNNIFHGQLLSQVTCLACNNKSNTIePFWDLSLEFPER-- 520
Cdd:cd02669 212 EFLSWLLNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPpl 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 521 YQcSGKDAASQP-CLVTDMLGKFTETEalegkiyvCDHCNSKRRKFsskpvvlteaqkqlMICHLPQVLRLHLKRFRwsg 599
Cdd:cd02669 291 FK-DGNEENIIPqVPLKQLLKKYDGKT--------ETELKDSLKRY--------------LISRLPKYLIFHIKRFS--- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 600 RNN--REKIGVHVVFEETLNMEPYCCSETLNALrPECFIYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSM 677
Cdd:cd02669 345 KNNffKEKNPTIVNFPIKNLDLSDYVHFDKPSL-NLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKE 423
|
410
....*....|....*.
gi 1958789268 678 CTMEEVLRAQAYILFY 693
Cdd:cd02669 424 VLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
424-693 |
8.22e-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: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 424 LHSVWKLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPAlIPTSQRRLieqvlNVVNnIFHGQLLSQVTCLACNNK 503
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPP-SNIEIKRL-----NPLE-AFKYTIESSYVCIGCSFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 504 SNTIEPFWDLSLEFPEryqcsgkdaaSQPCLVTDMLGKFTETEALEGKIYVCDHCNSkrrkfSSKPVVLTeaqkqlmich 583
Cdd:cd02673 91 ENVSDVGNFLDVSMID----------NKLDIDELLISNFKTWSPIEKDCSSCKCESA-----ISSERIMT---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 584 LPQVLRLHLKRFRWsgrnnREKIGVHVVFEEtLNMEPYCcSETLNalrpecfiYNLSAVVIHHGKGFGSGHYTAYCYN-S 662
Cdd:cd02673 146 FPECLSINLKRYKL-----RIATSDYLKKNE-EIMKKYC-GTDAK--------YSLVAVICHLGESPYDGHYIAYTKElY 210
|
250 260 270
....*....|....*....|....*....|....
gi 1958789268 663 EGGFWVHCNDSKLSMCTMEEVL---RAQAYILFY 693
Cdd:cd02673 211 NGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
584-693 |
5.62e-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: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789268 584 LPQVLRLHLKRFRWsGRNNREKIGVHVVFEETLNMEPYccsetlnalrpecfiyNLSAVVIHHGKGfGSGHYTAYCYNSE 663
Cdd:cd02665 128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 1958789268 664 GGFWVHCNDSKLSMCTMEEVLR--------AQAYILFY 693
Cdd:cd02665 190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
|
|
| |
