|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
272-664 |
2.16e-68 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 226.55 E-value: 2.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 272 TGLRNLGNTCYMNSILQVLSHLLIFRECFLkldlnqtqellataasgktrsssrrssvtastlqanenqekgrgsssvrr 351
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 352 snlssglsggasksrNMELIQPREPSSKHISLCHELHTLFQVMWSGKW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFL 430
Cdd:pfam00443 31 ---------------RISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 431 CELLDKVQQELEttgtrypalipaaqRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYHCNgK 510
Cdd:pfam00443 96 LFLLDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAEL-K 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 511 EMASQypcpltEMLAKFTETEALEGKI-YACDQCNK---AQKQLMVCRLPQVLRLHLKRFRWSgRNHREKIGVHVNFDQI 586
Cdd:pfam00443 161 TASLQ------ICFLQFSKLEELDDEEkYYCDKCGCkqdAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTEVEFPLE 233
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024440830 587 LNMEPYCCREsLKSLLPDCFIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLNMCTME-EVCKAQAYILFY 664
Cdd:pfam00443 234 LDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-664 |
2.38e-61 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 208.38 E-value: 2.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLSHLLIFRECFLKLDLNQTqellataasgktrsssrrssvtastlqanenqekgrgsssvrrs 352
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCT-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 nlssglsggasksrnmeliqPREPSSKHiSLCHELHTLFQVMW-SGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLC 431
Cdd:cd02660 38 --------------------CLSCSPNS-CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 432 ELLDKVQQELettGTRYPALIPAAQRKLIkqvlnvVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPE--RYHCNG 509
Cdd:cd02660 97 FLLDQLHTHY---GGDKNEANDESHCNCI------IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNksTPSWAL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 510 KEMASQYPCPLTEMLAKFTETEALEGKIYACDQCN---KAQKQLMVCRLPQVLRLHLKRFRWSGRNHREKIGVHVNFDQI 586
Cdd:cd02660 168 GESGVSGTPTLSDCLDRFTRPEKLGDFAYKCSGCGstqEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 587 LNMEPYCCRES----LKSLLPDCFIYDLSAVVMHHGKgFGSGHYTAYCYNsEGGFWVHCNDSKLNMCTMEEVCKAQAYIL 662
Cdd:cd02660 248 LNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLL 325
|
..
gi 2024440830 663 FY 664
Cdd:cd02660 326 FY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
423-664 |
1.72e-57 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 195.39 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 423 QQDAQEFLCELLDKVQQELETTGTRYpalipaaqrKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 502
Cdd:cd02257 22 QQDAHEFLLFLLDKLHEELKKSSKRT---------SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 503 ERyhcngkemaSQYPCPLTEMLAKFTETEALEGkiYACDQCNK-----AQKQLMVCRLPQVLRLHLKRFRWSGRNHREKI 577
Cdd:cd02257 93 VK---------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKkkkqeATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 578 GVHVNFDQILNMEPYCCRESLKSLLPD-CFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEV-- 654
Cdd:cd02257 162 NTKVSFPLELDLSPYLSEGEKDSDSDNgSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVle 241
|
250
....*....|...
gi 2024440830 655 ---CKAQAYILFY 664
Cdd:cd02257 242 fgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-665 |
1.63e-49 |
|
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: 175.54 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 272 TGLRNLGNTCYMNSILQVLSHllifrecflkldlnqTQELLATAASGKTRSSSRRSSVTAstLQANENQekgrgsssVRR 351
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH---------------TPPLANYLLSREHSKDCCNEGFCM--MCALEAH--------VER 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 352 SnLSSGLSGGASK--SRNMELIQPRepsskhislchelhtlfqvmwsgkwalvspfamlhsvwrlipaFRGYAQQDAQEF 429
Cdd:cd02661 57 A-LASSGPGSAPRifSSNLKQISKH-------------------------------------------FRIGRQEDAHEF 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 430 LCELLDKVQQELETTGTRYPALIPAAQRKlikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFperyhcng 509
Cdd:cd02661 93 LRYLLDAMQKACLDRFKKLKAVDPSSQET------TLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI-------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 510 KEMASqypcpLTEMLAKFTETEALEGK-IYACDQCNK---AQKQLMVCRLPQVLRLHLKRFrwsGRNHREKIGVHVNFDQ 585
Cdd:cd02661 159 KGADS-----LEDALEQFTKPEQLDGEnKYKCERCKKkvkASKQLTIHRAPNVLTIHLKRF---SNFRGGKINKQISFPE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 586 ILNMEPYCCRESLKSLlpdcfIYDLSAVVMHHGKGFGSGHYTAYCYNSEgGFWVHCNDSKLNMCTMEEVCKAQAYILFYS 665
Cdd:cd02661 231 TLDLSPYMSQPNDGPL-----KYKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
381-664 |
4.19e-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: 165.25 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 381 ISLCHELHTLFQVmwsgkwalvSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKVQqelettgtrypalipaaqrkli 460
Cdd:cd02667 18 LSQTPALRELLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR---------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 461 kqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEfpeRYHCNGKEmasqypCPLTEMLAKFTETEALEGK-IYA 539
Cdd:cd02667 67 ----TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---RSDEIKSE------CSIESCLKQFTEVEILEGNnKFA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 540 CDQCNKAQKQLMVCRLPQVLRLHLKRFRWSGRNHREKIGVHVNFDQILNMEPYC------CRESLKSLlpdcfiYDLSAV 613
Cdd:cd02667 134 CENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCdpkcnsSEDKSSVL------YRLYGV 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024440830 614 VMHHGkGFGSGHYTAYCY------------------NSEG---GFWVHCNDSKLNMCTMEEVCKAQAYILFY 664
Cdd:cd02667 208 VEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
423-665 |
3.45e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 161.30 E-value: 3.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 423 QQDAQEFLCELLDKVQqelettgtrypalipaaqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 502
Cdd:cd02674 22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 503 eryhcngKEMASQYPCPLTEMLAKFTETEALEGKI----YACDQCNKAQKQLMVCRLPQVLRLHLKRFRWSGRNhREKIG 578
Cdd:cd02674 76 -------SGSGDAPKVTLEDCLRLFTKEETLDGDNawkcPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGS-TRKLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 579 VHVNFD-QILNMEPYCCRESLKSLlpdcFIYDLSAVVMHHGKGFGsGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEVCKA 657
Cdd:cd02674 148 TPVTFPlNDLDLTPYVDTRSFTGP----FKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSS 222
|
....*...
gi 2024440830 658 QAYILFYS 665
Cdd:cd02674 223 SAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-670 |
3.27e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 147.79 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLSHLLIFRECFLKLDLNQtqellataasgktrsssrrssvtastlqanenqekgrgsssvrrs 352
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTE--------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 nlssglsggasksrnmeliqpREPSSKHISLchELHTLF---QVMWSGKWA---LVSPFAMLhsvWRLIPAFRgyaQQDA 426
Cdd:cd02659 39 ---------------------DDDDNKSVPL--ALQRLFlflQLSESPVKTtelTDKTRSFG---WDSLNTFE---QHDV 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 427 QEFLCELLDKVQQELETTGtrypalipaaQRKLIKqvlnvvnNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefperyh 506
Cdd:cd02659 90 QEFFRVLFDKLEEKLKGTG----------QEGLIK-------NLFGGKLVNYIICKECPHESEREEYFLDLQV------- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 507 cNGKEMASqypcpLTEMLAKFTETEALEG-KIYACDQCNK---AQKQLMVCRLPQVLRLHLKRFRWSG-RNHREKIGVHV 581
Cdd:cd02659 146 -AVKGKKN-----LEESLDAYVQGETLEGdNKYFCEKCGKkvdAEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKINDRF 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 582 NFDQILNMEPYCCRESLKSLLPDC------FIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEVC 655
Cdd:cd02659 220 EFPLELDMEPYTEKGLAKKEGDSEkkdsesYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAE 298
|
410 420 430
....*....|....*....|....*....|....*..
gi 2024440830 656 KAQ----------------------AYILFYsQRLSQ 670
Cdd:cd02659 299 EECfggeetqktydsgprafkrttnAYMLFY-ERKSP 334
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-665 |
3.58e-37 |
|
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: 141.79 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLSHLLIFRECFLKLDLNQTQELlataasgktrsssrrssvtastlqanenqekgrgsssvrrs 352
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 nlssglsggasksRNMELIQPREPSSkhisLCHELHTLFQVMWSGKWALVSPFAmlhsvwrLIPAFR--GYAQQDAQEFL 430
Cdd:cd02668 40 -------------KNMPPDKPHEPQT----IIDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFS 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 431 CELLDKVQQELettgtrypalipaaQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFperyhcNGK 510
Cdd:cd02668 96 KLFLSLLEAKL--------------SKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL------KGH 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 511 EMasqypcpLTEMLAKFTETEALEG-KIYACDQCNK---AQKQLMVCRLPQVLRLHLKRF---RWSGrnHREKIGVHVNF 583
Cdd:cd02668 156 KT-------LEECIDEFLKEEQLTGdNQYFCESCNSktdATRRIRLTTLPPTLNFQLLRFvfdRKTG--AKKKLNASISF 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 584 DQILNMEPYCCRESLKSllpdcFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKL-NM-------------- 648
Cdd:cd02668 227 PEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVeEMpgkplklgnsedpa 301
|
410 420
....*....|....*....|...
gi 2024440830 649 ------CTMEEVCKAQAYILFYS 665
Cdd:cd02668 302 kprkseIKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
387-665 |
5.14e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 134.74 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 387 LHTLFQVMWSGK--WALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKVQQELETTGTRYPALIPAAQRKLIKQVL 464
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 465 NVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryHCNgkemasqypcpLTEMLAKFTETEALEGK-IYACDQC 543
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ--NTS-----------ITSCLRQFSATETLCGRnKFYCDEC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 544 ---NKAQKQLMVCRLPQVLRLHLKRFRWSGRNHR-EKIGVHVNFDQILNMepycCRESLKSLLPDcFIYDLSAVVMHHGK 619
Cdd:cd02663 174 cslQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFPLELRL----FNTTDDAENPD-RLYELVAVVVHIGG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2024440830 620 GFGSGHYTAYCYNSegGFWVHCNDSKLNMCTMEEVCK--------AQAYILFYS 665
Cdd:cd02663 249 GPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-664 |
4.04e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 115.76 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 269 PGVTGLRNLGNTCYMNSILQVLSHLLIFRecflkldlnqtqellataasgktrsssrrssvtastlqanenqekgrgsss 348
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVLYFCPGFK--------------------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 349 vrrSNLSSGLSGGASKSrnmeliqprepssKHISLCHELHTLFqvmwSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQE 428
Cdd:cd02671 51 ---HGLKHLVSLISSVE-------------QLQSSFLLNPEKY----NDELANQAPRRLLNALREVNPMYEGYLQHDAQE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 429 FLCELLDKVQqelettgtrypalipaaqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYHCN 508
Cdd:cd02671 111 VLQCILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 509 GKEMASQYPCPLTEM------LAKFTETEALEGK-IYACDQCN---KAQKQLMVCRLPQVLRLHLKRFRWSGRNHR---- 574
Cdd:cd02671 165 SEESSEISPDPKTEMktlkwaISQFASVERIVGEdKYFCENCHhytEAERSLLFDKLPEVITIHLKCFAANGSEFDcygg 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 575 -EKIGVHVNFDQILNMEPYCCRESLKSllpdcfiYDLSAVVMHHGKGFGSGHYTAYCYnseggfWVHCNDSKLNMCTMEE 653
Cdd:cd02671 245 lSKVNTPLLTPLKLSLEEWSTKPKNDV-------YRLFAVVMHSGATISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
|
410 420
....*....|....*....|
gi 2024440830 654 VCKAQA---------YILFY 664
Cdd:cd02671 312 FLEALSpntsststpYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-664 |
5.00e-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 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: 105.88 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLshllifRECflkldlnqtQELLataasgktrsssrrssvtastlqanenqekgrgsSSVRRS 352
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL------RSV---------PELR----------------------------------DALKNY 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 NLSSGLSGGASksrnmeliqprepsskhISLCHELHTLFQVMwSGKWALVSPFAMLHSVWRLIPAF------RGYAQQDA 426
Cdd:cd02657 32 NPARRGANQSS-----------------DNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 427 QEFLCELLDKVQQELEttgtrypalIPAAQRKLIKQvlnvvnnIFHGQLLSQVTCLACDN-KSNTIEPFWDLSLefpery 505
Cdd:cd02657 94 EECWSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESPDeEEVSTESEYKLQC------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 506 HCNGKEMASQypcpLTE-MLAKFTETEALEGKIYACDQcnKAQKQLMVCRLPQVLRLHLKRFRWSGR-NHREKIGVHVNF 583
Cdd:cd02657 152 HISITTEVNY----LQDgLKKGLEEEIEKHSPTLGRDA--IYTKTSRISRLPKYLTVQFVRFFWKRDiQKKAKILRKVKF 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 584 DQILNMEPYCCreslksllpDCFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEVCKAQ----- 658
Cdd:cd02657 226 PFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdw 296
|
....*...
gi 2024440830 659 --AYILFY 664
Cdd:cd02657 297 hiAYILLY 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-664 |
1.86e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 104.88 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLSHLLIFRECFLkldlnqtqellataasgktrsssrrssvtastlqaNENQEKGRGSSSVrrs 352
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-----------------------------------SLNLPRLGDSQSV--- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 nlssglsggasksrnmeliqprePSSKHISLCHELHTlfqvmwsGKWALVSPFAMLHSVWRliPAFRGYAQQDAQEFLCE 432
Cdd:cd02664 43 -----------------------MKKLQLLQAHLMHT-------QRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRY 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 433 LLDKVQQELETTgtrypalipaaqrklikqvlnvvnniFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryhcngkem 512
Cdd:cd02664 91 LLDRLHTLIEKM--------------------------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPS--------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 513 asqypcpLTEMLAKFTETEALEGK-IYACDQCNK---AQKQLMVCRLPQVLRLHLKRFRWSGRNH-REKIGVHVNFDQIL 587
Cdd:cd02664 136 -------VQDLLNYFLSPEKLTGDnQYYCEKCASlqdAEKEMKVTGAPEYLILTLLRFSYDQKTHvREKIMDNVSINEVL 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 588 NMEPYCCRESLKSLLPD-----------CFI---YDLSAVVMHHGKGFGSGHYtaYCY---------------------- 631
Cdd:cd02664 209 SLPVRVESKSSESPLEKkeeesgddgelVTRqvhYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecpepkdaee 286
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2024440830 632 NSEGGFWVHCNDSKLNMCTMEEV-------CKAQAYILFY 664
Cdd:cd02664 287 NDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
273-666 |
6.90e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 102.19 E-value: 6.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLshllifrecflKLDLNQTQELlataasgktrsssrrssvtastlqanenqekgrgsssvrrs 352
Cdd:COG5533 1 GLPNLGNTCFMNSVLQIL-----------ALYLPKLDEL----------------------------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 nlsSGLSGGASKSrnmeLIQPREPSSKHISLChELHTLFQVMWSGKwalvspfamlhsVWRLIPAFRGYAQQDAQEFLCE 432
Cdd:COG5533 29 ---LDDLSKELKV----LKNVIRKPEPDLNQE-EALKLFTALWSSK------------EHKVGWIPPMGSQEDAHELLGK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 433 LLDKVQQELETTGTRypalipaaqrkLIKQVLNvvnnifhgqllsqvtclacDNKSNTIEPFWDLSLEFPERYHCNGK-- 510
Cdd:COG5533 89 LLDELKLDLVNSFTI-----------RIFKTTK-------------------DKKKTSTGDWFDIIIELPDQTWVNNLkt 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 511 ------EMASQYPCPLTemlAKFTETEALEGKiyacdqcNKAQKQLMVCRLPQVLRLHLKRFRWSGRNHR------EKIG 578
Cdd:COG5533 139 lqefidNMEELVDDETG---VKAKENEELEVQ-------AKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEKFE 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 579 VHVNFDQILNMEPYccreslksllpdcFIYDLSAVVMHHGkGFGSGHYTAYCynSEGGFWVHCNDSKLNMCTMEEVCKA- 657
Cdd:COG5533 209 LPVKHDQILNIVKE-------------TYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEk 272
|
410
....*....|.
gi 2024440830 658 --QAYILFYSQ 666
Cdd:COG5533 273 akNAYLYFYER 283
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-88 |
9.40e-24 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 94.64 E-value: 9.40e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024440830 26 CVDCNTTESVWACLSCSHVACGRYIEEHALKHFQENGHPVALEVNELYVFCYLCDDYVLNDNA 88
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
415-664 |
3.13e-23 |
|
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: 98.98 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 415 IPAFRGY-----AQQDAQEFLCELLDKVQQELEttgtrypalipaaqrklikqvlnvvnNIFHGQLLSQVTCLACDNKSN 489
Cdd:cd02662 21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 490 -TIEPFWDLSLEFPERyhcngkemASQYPCPLTEMLAKFTETEALEGkiYACDQCnkaqkQLMVCRLPQVLRLHLKRFRW 568
Cdd:cd02662 75 vRYESFTMLSLPVPNQ--------SSGSGTTLEHCLDDFLSTEIIDD--YKCDRC-----QTVIVRLPQILCIHLSRSVF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 569 SGRNHREKIGVHVNFdqilnmepyccreslKSLLPDcFIYDLSAVVMHHGkGFGSGHYTAY------------------- 629
Cdd:cd02662 140 DGRGTSTKNSCKVSF---------------PERLPK-VLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmr 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024440830 630 -CYNSEGGFWVHCNDSKLNMCTMEEVC-KAQAYILFY 664
Cdd:cd02662 203 eGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-664 |
2.35e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 98.16 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLSHLLIFRECFLKLDLNQTQELLATAASGKTRSssrrssvtastlqanenqekgrgsssvrrS 352
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANDLNCQL-----------------------------I 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 353 NLSSGL-SGGASKSRNmeLIQPREPSSKHISlchelhtlfqvmwsgkwalvsPFAMLHSVWRLIPAFRGYAQQDAQEFLC 431
Cdd:cd02658 52 KLADGLlSGRYSKPAS--LKSENDPYQVGIK---------------------PSMFKALIGKGHPEFSTMRQQDALEFLL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 432 ELLDKVQQELETTGTRYPalipaaqrklikqvlnvvNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYHCNGKE 511
Cdd:cd02658 109 HLIDKLDRESFKNLGLNP------------------NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 512 MASQY-PCPLTEMLAKFTETEALEGKIYACDQCNKAQKQLMVCRLPQVLRLHLKRFR----WSGRnhreKIGVHVNFDQI 586
Cdd:cd02658 171 GELVYePVPLEDCLKAYFAPETIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQllenWVPK----KLDVPIDVPEE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 587 LNMEPyccreslksllpdcfiYDLSAVVMHHGKGFGSGHYTAYCY--NSEGGFWVHCNDSKLNMCTMEEVCKAQAYILFY 664
Cdd:cd02658 247 LGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
270-654 |
2.17e-19 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 93.40 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 270 GVTGLRNLGNTCYMNSILQVLSHLLIFRECFLKLdlnqtqellataasgktrsssrrssvtastlqanenqekgrgsssv 349
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------------------------------------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 350 rrsnlssglsggasksrnmeliqPREPSSKHISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRlipAFRGYAQQDAQEF 429
Cdd:COG5077 226 -----------------------PTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWD---SDDSFMQHDIQEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 430 LCELLDKVQQELETTgtrypalipaaqrklikQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefperyhcNG 509
Cdd:COG5077 280 NRVLQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL--------NV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 510 KEMASqypcpLTEMLAKFTETEALEGK-IYACDQ--CNKAQKQLMVCRLPQVLRLHLKRFRWS-GRNHREKIGVHVNFDQ 585
Cdd:COG5077 335 KGMKN-----LQESFRRYIQVETLDGDnRYNAEKhgLQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMVKINDRYEFPL 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024440830 586 ILNMEPYCCRESLKSLLPDCfIYDLSAVVMHHGKgFGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEV 654
Cdd:COG5077 410 EIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
496-667 |
2.62e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 92.64 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 496 DLSLEFPERYHCNG--KEMASQYPCP-LTEMLAKFTETEAL-EGKIYACDQCN---KAQKQLMVCRLPQVLRLHLKRFRw 568
Cdd:COG5560 650 EKRYLSLFSYDPLWtiREIGAAERTItLQDCLNEFSKPEQLgLSDSWYCPGCKefrQASKQMELWRLPMILIIHLKRFS- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 569 SGRNHREKIGVHVNF---DQILNMEPYccreslkSLLPDCFIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSK 645
Cdd:COG5560 729 SVRSFRDKIDDLVEYpidDLDLSGVEY-------MVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSR 800
|
170 180
....*....|....*....|..
gi 2024440830 646 LNMCTMEEVCKAQAYILFYSQR 667
Cdd:COG5560 801 ITEVDPEDSVTSSAYVLFYRRK 822
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
270-502 |
1.23e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 84.16 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 270 GVTGLRNLGNTCYMNSILQVLSHLLIFRECFLkldlnqtqellataasgktrsssrrssvtastlqANENQEkgrgssSV 349
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL----------------------------------SDEYEE------SI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 350 RRSNlssglsggasksrnmeliqprePSSKHISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEF 429
Cdd:COG5560 304 NEEN----------------------PLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 430 LCELLDKVQQEL----ETTGTRYPALIPAAQRKlIKQVLN------------VVNNIFHGQLLSQVTCLACDNKSNTIEP 493
Cdd:COG5560 362 IAFLLDGLHEDLnriiKKPYTSKPDLSPGDDVV-VKKKAKecwwehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDP 440
|
....*....
gi 2024440830 494 FWDLSLEFP 502
Cdd:COG5560 441 FMDLTLPLP 449
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
25-70 |
1.22e-13 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 65.46 E-value: 1.22e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2024440830 25 HCVDCNTTESVWACLSCSHVACGRYIEEHALKHFQENGHPVALEVN 70
Cdd:smart00290 1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLG 46
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-664 |
4.18e-13 |
|
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: 71.97 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 269 PGVTGLRNLGNTCYMNSILQVLSHLLIFRECFLKLDlnqtqellataasgktrsssrrssvtastlqaNENQEKGRGSSS 348
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE--------------------------------NYENIKDRKSEL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 349 VRRsnlssgLSggasksrnmELIQ----PREPSSkHISLcHELhtLFQVM-WSGKwalvsPFAMLHsvwrlipafrgyaQ 423
Cdd:cd02669 165 VKR------LS---------ELIRkiwnPRNFKG-HVSP-HEL--LQAVSkVSKK-----KFSITE-------------Q 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 424 QDAQEFLCELLDKVQQELETTGTRYPALIPAA-QRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIePFWDLSLEFP 502
Cdd:cd02669 208 SDPVEFLSWLLNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 503 ERYHCNGKEMASQYP-CPLTEMLAKFTETEalegkiyaCDQCNKAQKQLMVCRLPQVLRLHLKRFRwsgRNH--REKIGV 579
Cdd:cd02669 287 PPPLFKDGNEENIIPqVPLKQLLKKYDGKT--------ETELKDSLKRYLISRLPKYLIFHIKRFS---KNNffKEKNPT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 580 HVNFDQILNMEPYCCRESLKSLLPdCFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEVCKAQA 659
Cdd:cd02669 356 IVNFPIKNLDLSDYVHFDKPSLNL-STKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSES 434
|
....*
gi 2024440830 660 YILFY 664
Cdd:cd02669 435 YIQIW 439
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-664 |
9.34e-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: 64.05 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 272 TGLRNLGNTCYMNSILQVLSHLLIFRECFLKLDLNQtqellataasgktrsssrrssvtaSTLQANENQEKGRGSSSVRR 351
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESK------------------------AELASDYPTERRIGGREVSR 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 352 snlssglsggasksrnMELIQPREpsskhisLCHELHTLFQVMWSGKWALVSPFAMLhsvwrlipAFRGYAQQDAQEflc 431
Cdd:cd02666 58 ----------------SELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE--- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 432 eLLDKVQQELETTGTRYPALIPAAQRKLIKQVLNVVNNIFHGQLLSQVT-CLACDNKSNTIEPFWDLSLEFPeryhcNGK 510
Cdd:cd02666 104 -CIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVD-----VGK 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 511 EM----ASQYPCPLTEMLAKFTETEALEG-KIYACDQCNKA---QKQLMVCR---LPQVLRLHLKRFRWSGRNHREKIGV 579
Cdd:cd02666 178 KGreivVLLEPKDLYDALDRYFDYDSLTKlPQRSQVQAQLAqplQRELISMDryeLPSSIDDIDELIREAIQSESSLVRQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 580 HVNFDQILNMEpyccRESLKSLLPDcFIYDLSAVVMHHGKGfGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEV----- 654
Cdd:cd02666 258 AQNELAELKHE----IEKQFDDLKS-YGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftl 331
|
410
....*....|.
gi 2024440830 655 -CKAQAYILFY 664
Cdd:cd02666 332 gNTATPYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
408-664 |
2.64e-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: 58.31 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 408 LHSVWRLIPAFRGYAQQDAQEFLCELLDKVQQELETTGTRYPALIPAAQRklikqvLNVVnNIFHGQLLSQVTCLACDNK 487
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKR------LNPL-EAFKYTIESSYVCIGCSFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 488 SNTIEPFWDLSLefperyhcngkEMASQYPCPLTEMLAKFTETEALEGKIYACdQCNKAQKQLMVCRLPQVLRLHLKRFR 567
Cdd:cd02673 91 ENVSDVGNFLDV-----------SMIDNKLDIDELLISNFKTWSPIEKDCSSC-KCESAISSERIMTFPECLSINLKRYK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 568 WsgrnhREKIGVHVNfDQILNMEPYCcreslkSLLPDcfiYDLSAVVMHHGKGFGSGHYTAYCYN-SEGGFWVHCNDSKL 646
Cdd:cd02673 159 L-----RIATSDYLK-KNEEIMKKYC------GTDAK---YSLVAVICHLGESPYDGHYIAYTKElYNGSSWLYCSDDEI 223
|
250 260
....*....|....*....|.
gi 2024440830 647 NMCTMEEVCKA---QAYILFY 664
Cdd:cd02673 224 RPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
423-664 |
2.88e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 49.09 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 423 QQDAQEFLCELLDKVQQELEttgtrypalIPAAQRKLIKQVLNVVNNIFHGQLLSQVtclacdnksntiepfwdlSLEFP 502
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQ---------AAAEAISPGEKSKNPMVQLFYGTFLTEG------------------VLEGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 503 ERYHCngkEMASQYPCPLTEM--LAKFTETEALEGKI--YACDQCNKAQKQLMVCRLPQVLRLHLKRFRWsGRNHREKIG 578
Cdd:cd02665 75 PFCNC---ETFGQYPLQVNGYgnLHECLEAAMFEGEVelLPSDHSVKSGQERWFTELPPVLTFELSRFEF-NQGRPEKIH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 579 VHVNFDQILNMEPYccreslksllpdcfiyDLSAVVMHHGKGfGSGHYTAYCYNSEGGFWVHCNDSKLNMCTMEEVCK-- 656
Cdd:cd02665 151 DKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERds 213
|
250
....*....|....
gi 2024440830 657 ------AQAYILFY 664
Cdd:cd02665 214 fgggrnPSAYCLMY 227
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
273-629 |
1.50e-04 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 44.18 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 273 GLRNLGNTCYMNSILQVLSHLLIFReCFLKldlnqtqellataasgktrsssrrssvtASTLQANENQ------------ 340
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLR-NLAL----------------------------SHLATECLKEhcllcelgflfd 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 341 --EKGRGSSsVRRSNLSSGLSGgASKSRNMELIQPREPSSKHISLCHelhtlfqvmwsgkwalvspfamlhsvwrLIPAF 418
Cdd:pfam13423 53 mlEKAKGKN-CQASNFLRALSS-IPEASALGLLDEDRETNSAISLSS----------------------------LIQSF 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 419 rgyaqqdaQEFLcelLDKVQQELETtgtrypalipaaQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLS 498
Cdd:pfam13423 103 --------NRFL---LDQLSSEENS------------TPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024440830 499 LEFPERYHCNGKEMASQYPCPLTEM-LAKFTETEALegkiyaCDQCNKAQ---KQLMVCRLPQVLRLHLK----RFRWSG 570
Cdd:pfam13423 160 LIYPRKPSSNNKKPPNQTFSSILKSsLERETTTKAW------CEKCKRYQpleSRRTVRNLPPVLSLNAAltneEWRQLW 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024440830 571 RNHR---EKIGVHVNFDQILNmepyccreslksllPDCFIYDLSAVVMHHGKGFGSGHYTAY 629
Cdd:pfam13423 234 KTPGwlpPEIGLTLSDDLQGD--------------NEIVKYELRGVVVHIGDSGTSGHLVSF 281
|
|
| |
