|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
273-706 |
5.04e-64 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 215.77 E-value: 5.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 273 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlamtasektrsckhppvtdtvvyqmnecqekdtgfvcsrqssl 352
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 353 ssglsggaskgrkMELIQPKEPTSQYISLCHELHTLFQVMWSGKW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:pfam00443 32 -------------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 432 LDKIQRELEttgtslpaliptsqRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryqcsgkDIA 511
Cdd:pfam00443 99 LDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-------DSA 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 512 SQPCLV-TEMLAKFTETEALEGKI-YVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNslcilintl 589
Cdd:pfam00443 158 ELKTASlQICFLQFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN--------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 590 lamlrssngkydqqtekitgwsgRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGkGFGSGHYT 669
Cdd:pfam00443 218 -----------------------RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-DYRLVAVVVHSG-SLSSGHYI 272
|
410 420 430
....*....|....*....|....*....|....*...
gi 530400884 670 AYCYNSEGGFWVHCNDSKLSMCTMD-EVCKAQAYILFY 706
Cdd:pfam00443 273 AYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-707 |
6.22e-55 |
|
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: 191.82 E-value: 6.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrSCKHPPVTDTvvyqmnecqekdtgfvcsrqssls 353
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 354 sglsggaskgrkmeliqpkepTSQYISLCHELHTLFQVMW-SGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELL 432
Cdd:cd02660 41 ---------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLL 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 433 DKIQRELettGTSLPALIPTSQRKLIkqvlnvVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIAS 512
Cdd:cd02660 100 DQLHTHY---GGDKNEANDESHCNCI------IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 513 ----QPCLvTEMLAKFTETEALEGKIYVCDQCNSKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFSTNSLCIlint 588
Cdd:cd02660 171 gvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKT---- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 589 llamlrssngkydqqtekitgwsgrnnREKIGVHVGFEEILNMEPYCCRET----LKSLRPECFIYDLSAVVMHHGKgFG 664
Cdd:cd02660 235 ---------------------------SRKIDTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LD 286
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530400884 665 SGHYTAYCYNsEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYT 707
Cdd:cd02660 287 TGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
421-706 |
1.06e-51 |
|
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: 180.37 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 421 QQDAQEFLCELLDKIQRELETTgtslpalipTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 500
Cdd:cd02257 22 QQDAHEFLLFLLDKLHEELKKS---------SKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 501 ERyqcsgkdiASQPCLVTEMLAKFTETEALEGkiYVCDQCNSKRrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFStn 580
Cdd:cd02257 93 VK--------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLKRFS-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 581 slcilintllamlrssngkydqqtekitgWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRP-ECFIYDLSAVVMHH 659
Cdd:cd02257 152 -----------------------------FNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDnGSYKYELVAVVVHS 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 530400884 660 GKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEV-----CKAQAYILFY 706
Cdd:cd02257 203 GTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-706 |
2.00e-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: 175.93 E-value: 2.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 273 TGLRNLGNTCYMNSVLQVLSHLlifrqcflkldlnqwlamtasektrsckhPPVTDTVVYQM--NECQEKDTGFVCsrqs 350
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHT-----------------------------PPLANYLLSREhsKDCCNEGFCMMC---- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 351 slssglsggaskgrkmeliqpkeptsqyislCHELHTLfQVMWSGKWALVSPFamLHSVWRLI-PAFRGYAQQDAQEFLC 429
Cdd:cd02661 49 -------------------------------ALEAHVE-RALASSGPGSAPRI--FSSNLKQIsKHFRIGRQEDAHEFLR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 430 ELLDKIQRelettgTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefperyqcsgkD 509
Cdd:cd02661 95 YLLDAMQK------ACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSL-----------D 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 510 IASQPCLvTEMLAKFTETEALEGK-IYVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNslcilint 588
Cdd:cd02661 158 IKGADSL-EDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRFSNF-------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 589 llamlrssngkydqqtekitgwsgrnNREKIGVHVGFEEILNMEPYCCRETLKSLrpecfIYDLSAVVMHHGKGFGSGHY 668
Cdd:cd02661 218 --------------------------RGGKINKQISFPETLDLSPYMSQPNDGPL-----KYKLYAVLVHSGFSPHSGHY 266
|
410 420 430
....*....|....*....|....*....|....*...
gi 530400884 669 TAYCYNSEGgFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02661 267 YCYVKSSNG-KWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
377-706 |
1.48e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 152.93 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 377 QYISLCHELHTLFQVmwsgkwalvSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQrelettgtslpaliptsqrk 456
Cdd:cd02667 16 QNLSQTPALRELLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 457 likqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefPEryqcsgKDIASQPCLVTEMLAKFTETEALEGK-IY 535
Cdd:cd02667 67 ------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL--PR------SDEIKSECSIESCLKQFTEVEILEGNnKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 536 VCDQCnskrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNSLCILIntllamlrssngkydqqtekitgwsgrnn 615
Cdd:cd02667 133 ACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR----------------------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 616 reKIGVHVGFEEILNMEPYCcreTLKSLRPEC---FIYDLSAVVMHHGkGFGSGHYTAYCY------------------N 674
Cdd:cd02667 170 --KVSRHVSFPEILDLAPFC---DPKCNSSEDkssVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaD 243
|
330 340 350
....*....|....*....|....*....|....*
gi 530400884 675 SEG---GFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02667 244 EAGpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
421-707 |
3.72e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 144.74 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 421 QQDAQEFLCELLDKIQrelettgtslpaliptsqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 500
Cdd:cd02674 22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 501 ERYQCSGKdiasqpCLVTEMLAKFTETEALEGKIYV-CDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFST 579
Cdd:cd02674 76 SGSGDAPK------VTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLKRFSF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 580 NslcilintllamlrssngkydqqtekitgwsgRNNREKIGVHVGFE-EILNMEPYCcretLKSLRPECFIYDLSAVVMH 658
Cdd:cd02674 139 S--------------------------------RGSTRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNH 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 530400884 659 HGKGFGsGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYT 707
Cdd:cd02674 183 YGSLNG-GHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-706 |
1.14e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 143.55 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWlamtasekTRSCKHPPVTDTVVYQMNECQEKDtgfvcsrqssls 353
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED--------DDDNKSVPLALQRLFLFLQLSESP------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 354 sglsggaskgrkmelIQPKEPTSqyislchelhtLFQVMWsgkwalvspfamlhsvWRLIPAFRgyaQQDAQEFLCELLD 433
Cdd:cd02659 64 ---------------VKTTELTD-----------KTRSFG----------------WDSLNTFE---QHDVQEFFRVLFD 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 434 KIQRELEttgtslpaliPTSQRKLIKqvlnvvnNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEfperyqcsGKDIASq 513
Cdd:cd02659 99 KLEEKLK----------GTGQEGLIK-------NLFGGKLVNYIICKECPHESEREEYFLDLQVA--------VKGKKN- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 514 pclVTEMLAKFTETEALEG-KIYVCDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFStnslcilintllam 592
Cdd:cd02659 153 ---LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFE-------------- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 593 lrssngkYDQQTekitgwsgrNNREKIGVHVGFEEILNMEPYCCR------ETLKSLRPECFIYDLSAVVMHHGkGFGSG 666
Cdd:cd02659 205 -------FDFET---------MMRIKINDRFEFPLELDMEPYTEKglakkeGDSEKKDSESYIYELHGVLVHSG-DAHGG 267
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400884 667 HYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQ----------------------AYILFY 706
Cdd:cd02659 268 HYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsgprafkrttnAYMLFY 329
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-689 |
3.75e-34 |
|
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: 133.31 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQwlamTASEKTRSCKHPPVTDTVVYQMnecqekdtgfvcsrqssls 353
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTE----DAELKNMPPDKPHEPQTIIDQL------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 354 sglsggaskgrkmeliqpkeptsQYIslchelhtlFQVMWSGKWALVSPFAmlhsvwrLIPAFR--GYAQQDAQEFLCEL 431
Cdd:cd02668 58 -----------------------QLI---------FAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLF 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 432 LDKIQRELettgtslpaliptsQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFperyqcsgKDIA 511
Cdd:cd02668 99 LSLLEAKL--------------SKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--------KGHK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 512 SqpclVTEMLAKFTETEALEG-KIYVCDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFStnslcilintll 590
Cdd:cd02668 157 T----LEECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFV------------ 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 591 amlrssngkYDQQTEKitgwsgrnnREKIGVHVGFEEILNMEPYCCRETLKSlrpecFIYDLSAVVMHHGKGFGSGHYTA 670
Cdd:cd02668 210 ---------FDRKTGA---------KKKLNASISFPEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIA 266
|
410
....*....|....*....
gi 530400884 671 YCYNSEGGFWVHCNDSKLS 689
Cdd:cd02668 267 HIKDEQTGEWYKFNDEDVE 285
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
385-707 |
1.42e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 125.11 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 385 LHTLFQVMWSGK--WALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVL 462
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 463 NVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQcsgkdiasqpclVTEMLAKFTETEALEGK-IYVCDQCN 541
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTS------------ITSCLRQFSATETLCGRnKFYCDECC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 542 SKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFstnslcilintllamlrssngKYDQQTEKITGWSGRnnrekigv 621
Cdd:cd02663 175 SLQ-----------EAEKRMKIKKLPKILALHLKRF---------------------KYDEQLNRYIKLFYR-------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 622 hVGFEEILNMepycCRETLKSLRPeCFIYDLSAVVMHHGKGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMDEVCK--- 698
Cdd:cd02663 215 -VVFPLELRL----FNTTDDAENP-DRLYELVAVVVHIGGGPNHGHYVSIV--KSHGGWLLFDDETVEKIDENAVEEffg 286
|
330
....*....|....
gi 530400884 699 -----AQAYILFYT 707
Cdd:cd02663 287 dspnqATAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-706 |
1.91e-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: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlamtasektrsckhPPVTDTVVyqmnecqekdTGFVcsrqssls 353
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNL-----------------PRLGDSQS----------VMKK-------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 354 sglsggaskgrkmeliqpkeptsqyislchELHTLFQVMWSGKWALVSPFAMLHSVWRliPAFRGYAQQDAQEFLCELLD 433
Cdd:cd02664 46 ------------------------------LQLLQAHLMHTQRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRYLLD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 434 KIQRELETTgtslpaliptsqrklikqvlnvvnniFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPeryqcsgkdiasq 513
Cdd:cd02664 94 RLHTLIEKM--------------------------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 514 pcLVTEMLAKFTETEALEGK-IYVCDQCNSkrrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFStnslcilintllam 592
Cdd:cd02664 135 --SVQDLLNYFLSPEKLTGDnQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFS-------------- 187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 593 lrssngkYDQQTekitgwsgrNNREKIGVHVGFEEILNMEPYCCRETLKSLRPE-----------CFI---YDLSAVVMH 658
Cdd:cd02664 188 -------YDQKT---------HVREKIMDNVSINEVLSLPVRVESKSSESPLEKkeeesgddgelVTRqvhYRLYAVVVH 251
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400884 659 HGKGFGSGHYtaYCY----------------------NSEGGFWVHCNDSKLSMCTMDEV-------CKAQAYILFY 706
Cdd:cd02664 252 SGYSSESGHY--FTYardqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
29-90 |
5.70e-23 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 92.71 E-value: 5.70e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400884 29 CVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDN 90
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-706 |
1.80e-21 |
|
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: 96.12 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 270 PGVTGLRNLGNTCYMNSVLQVLshllifrqCFlkldlnqwlamtASEKTRSCKHppvtdtvvyqmnecqekdtgfVCSrq 349
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVL--------YF------------CPGFKHGLKH---------------------LVS-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 350 sslssglsggaskgrkmeLIQPKEPTSQYISLCHELHTlfqvmwsGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLC 429
Cdd:cd02671 59 ------------------LISSVEQLQSSFLLNPEKYN-------DELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 430 ELLDKIQrelettgtslpaliptsqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKD 509
Cdd:cd02671 114 CILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 510 IAS-QPCLVTEM------LAKFTETEALEGK-IYVCDQCNSkrrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFSTNS 581
Cdd:cd02671 168 SSEiSPDPKTEMktlkwaISQFASVERIVGEdKYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 582 LCILINTLLamlrssngkydqqtekitgwsgrnnrEKIGVHVGFEEILNMEPYCCRETLKSlrpecfiYDLSAVVMHHGK 661
Cdd:cd02671 237 SEFDCYGGL--------------------------SKVNTPLLTPLKLSLEEWSTKPKNDV-------YRLFAVVMHSGA 283
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 530400884 662 GFGSGHYTAYCYnseggfWVHCNDSKLSMCTMDEVCKAQA---------YILFY 706
Cdd:cd02671 284 TISSGHYTAYVR------WLLFDDSEVKVTEEKDFLEALSpntsststpYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-706 |
1.42e-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 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: 90.08 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlamtasektRSCkhpPVTDTVVYQMNECQEKDTGfvcsrqssls 353
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL---------------------------RSV---PELRDALKNYNPARRGANQ---------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 354 sglsggaskgrkmeliqpkepTSQYISLchELHTLFQVMwSGKWALVSPFAMLHSVWRLIPAF------RGYAQQDAQEF 427
Cdd:cd02657 41 ---------------------SSDNLTN--ALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEEC 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 428 LCELLDKIQRELEttgtslpalIPTSQRKLIKQvlnvvnnIFHGQLLSQVTCLACDN-KSNTIEPFWDLSLefperyQCS 506
Cdd:cd02657 97 WSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESPDeEEVSTESEYKLQC------HIS 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 507 GKDIASQpcLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSkpvvlteaqkqlmichLPQVLRLHLKRFStnslcili 586
Cdd:cd02657 155 ITTEVNY--LQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISR----------------LPKYLTVQFVRFF-------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 587 ntllamlrssngkYDQQTEKitgwsgrnnREKIGVHVGFEEILNMEPYCCretlkslrpECFIYDLSAVVMHHGKGFGSG 666
Cdd:cd02657 209 -------------WKRDIQK---------KAKILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSG 257
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 530400884 667 HYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQ-------AYILFY 706
Cdd:cd02657 258 HYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
274-708 |
9.22e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 84.47 E-value: 9.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLShllifrqcfLKLDLNQWLAMTASEKTRSCKHppvtdtvVYQMNEcqekdtgfvcsrqssls 353
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA---------LYLPKLDELLDDLSKELKVLKN-------VIRKPE----------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 354 sglsggaskgrkmeliqpkEPTSQyislcHELHTLFQVMWSGKwalvspfamlhsVWRLIPAFRGYAQQDAQEFLCELLD 433
Cdd:COG5533 48 -------------------PDLNQ-----EEALKLFTALWSSK------------EHKVGWIPPMGSQEDAHELLGKLLD 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 434 KIQRELETTGTslpaliptsqrKLIKQVLNvvnnifhgqllsqvtclacDNKSNTIEPFWDLSLEFPerYQCSGKDIASQ 513
Cdd:COG5533 92 ELKLDLVNSFT-----------IRIFKTTK-------------------DKKKTSTGDWFDIIIELP--DQTWVNNLKTL 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 514 PCLVTEMlakftetealegKIYVCDQCNSKRRRFSSKPVVlTEAQKQLMICHLPQVLRLHLKRFSTNSlcilintllaml 593
Cdd:COG5533 140 QEFIDNM------------EELVDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLG------------ 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 594 rsSNGKYDQQTEkitgwsgrnnrEKIGVHVGFEEILNMEPYccretlkslrpecFIYDLSAVVMHHGkGFGSGHYTAYCy 673
Cdd:COG5533 195 --GNQKIDTEVD-----------EKFELPVKHDQILNIVKE-------------TYYDLVGFVLHQG-SLEGGHYIAYV- 246
|
410 420 430
....*....|....*....|....*....|....*...
gi 530400884 674 nSEGGFWVHCNDSKLSMCTMDEVCKA---QAYILFYTQ 708
Cdd:COG5533 247 -KKGGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
413-706 |
4.74e-17 |
|
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: 81.26 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 413 IPAFRGY-----AQQDAQEFLCELLDKIQRELEttgtslpaliptsqrklikqvlnvvnNIFHGQLLSQVTCLACDNKSN 487
Cdd:cd02662 21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 488 -TIEPFWDLSLEFPERYQCSGkdiasqpCLVTEMLAKFTETEALEGkiYVCDQCnskrrrfsskpvvlteaqkQLMICHL 566
Cdd:cd02662 75 vRYESFTMLSLPVPNQSSGSG-------TTLEHCLDDFLSTEIIDD--YKCDRC-------------------QTVIVRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 567 PQVLRLHLKRFStnslcilintllamlrssngkydqqtekitgWSGRNNREKIGVHVGFEEILNMepyccretlkslrpe 646
Cdd:cd02662 127 PQILCIHLSRSV-------------------------------FDGRGTSTKNSCKVSFPERLPK--------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 647 cFIYDLSAVVMHHGkGFGSGHYTAY--------------------CYNSEGGFWVHCNDSKLSMCTMDEVC-KAQAYILF 705
Cdd:cd02662 161 -VLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLF 238
|
.
gi 530400884 706 Y 706
Cdd:cd02662 239 Y 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
271-709 |
6.72e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.32 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 271 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrsckhppvTDTVVYQMNEcqekdtgfvcsrqs 350
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------SDEYEESINE-------------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 351 slssglsggaskgrkmeliqpKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCE 430
Cdd:COG5560 306 ---------------------ENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 431 LLDKIQREL----ETTGTSLPALIPTSQRKlIKQVLN------------VVNNIFHGQLLSQVTCLACDNKSNTIEPFWD 494
Cdd:COG5560 365 LLDGLHEDLnriiKKPYTSKPDLSPGDDVV-VKKKAKecwwehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMD 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 495 LSLEFPERYQCSGK------DIASQPCLV------TEMLAKFTETEALE----GKIYVCDQCNSKRRRFSSK-------- 550
Cdd:COG5560 444 LTLPLPVSMVWKHTivvfpeSGRRQPLKIeldassTIRGLKKLVDAEYGklgcFEIKVMCIYYGGNYNMLEPadkvllqd 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 551 -------------------PVVLTEAQKQLMICHL------------PQVLRLHLKRFSTNSLCIL-INTLLAMLRSSNG 598
Cdd:COG5560 524 ipqtdfvylyetndngievPVVHLRIEKGYKSKRLfgdpflqlnvliKASIYDKLVKEFEELLVLVeMKKTDVDLVSEQV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 599 KYDQQTEKITGW-----SGRNNREKIGVHVG------------------------------FEEILNMEP---------- 633
Cdd:COG5560 604 RLLREESSPSSWlkletEIDTKREEQVEEEGqmnfndavvisceweekrylslfsydplwtIREIGAAERtitlqdclne 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 634 -------------YCcrETLKSLRP-----------------------------------------------------EC 647
Cdd:COG5560 684 fskpeqlglsdswYC--PGCKEFRQaskqmelwrlpmiliihlkrfssvrsfrdkiddlveypiddldlsgveymvddPR 761
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400884 648 FIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQR 709
Cdd:COG5560 762 LIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
274-706 |
9.84e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 78.90 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlamtaseKTRSCKHPPVTDTvvyqmnECQ--EKDTGFVCSRqss 351
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEN----------KFPSDVVDPANDL------NCQliKLADGLLSGR--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 352 lssglsggasKGRKMELIQPKEPTSQYIslchelhtlfqvmwsgkwalvSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:cd02658 62 ----------YSKPASLKSENDPYQVGI---------------------KPSMFKALIGKGHPEFSTMRQQDALEFLLHL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 432 LDKIQRELETTGTSLPaliptsqrklikqvlnvvNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPER---YQCSGK 508
Cdd:cd02658 111 IDKLDRESFKNLGLNP------------------NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeatEKEEGE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 509 DIASQPCLVtEMLAKFTETEALEGKiyvCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNSlcilint 588
Cdd:cd02658 173 LVYEPVPLE-DCLKAYFAPETIEDF---CSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQLLE------- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 589 llamlrssngkydqqtekitGWSGRnnreKIGVHVGFEEILNMEPyccretlkslrpecfiYDLSAVVMHHGKGFGSGHY 668
Cdd:cd02658 231 --------------------NWVPK----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHY 270
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 530400884 669 TAYCY--NSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02658 271 VAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
271-696 |
3.82e-15 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 79.91 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 271 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNqwlamtasektrsckHPPVTDTVVYQMNECqekdtgFvcsrqs 350
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTD---------------HPRGRDSVALALQRL------F------ 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 351 slssglsggaskgrkMELIQPKEPTSQyislchelhTLFQVmwSGKWAlvspfamlhsvwrlipAFRGYAQQDAQEFLCE 430
Cdd:COG5077 245 ---------------YNLQTGEEPVDT---------TELTR--SFGWD----------------SDDSFMQHDIQEFNRV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 431 LLDKIQRELETTgtslpaliptsqrklikQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLslefperyQCSGKDI 510
Cdd:COG5077 283 LQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDI--------QLNVKGM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 511 ASqpclVTEMLAKFTETEALEGKiyvcdqcnskrRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFstnslcilintll 590
Cdd:COG5077 338 KN----LQESFRRYIQVETLDGD-----------NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRF------------- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 591 amlrssngKYDQQtekitgwsgRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGKgFGSGHYTA 670
Cdd:COG5077 390 --------EYDFE---------RDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYA 450
|
410 420
....*....|....*....|....*.
gi 530400884 671 YCYNSEGGFWVHCNDSKLSMCTMDEV 696
Cdd:COG5077 451 LLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
28-73 |
1.97e-13 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 65.08 E-value: 1.97e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530400884 28 HCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVN 73
Cdd:smart00290 1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLG 46
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-706 |
2.77e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 60.02 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 270 PGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEktrsckhppvtdtvvyqmnecqekdtgfvcsrq 349
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSE--------------------------------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 350 sslssglsggaskgrkmeliqpkeptsqyisLCHELHTLFQVMWSGKW--ALVSPFAMLHSVWRLIPA-FRGYAQQDAQE 426
Cdd:cd02669 164 -------------------------------LVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKVSKKkFSITEQSDPVE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 427 FLCELLDKIQRELETTGTSLPALIPTS-QRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIePFWDLSLEFPER--Y 503
Cdd:cd02669 213 FLSWLLNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPplF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 504 QCS-GKDIASQPCLvTEMLAKFTETEalegkiyvCDQCNSKRRRFsskpvvlteaqkqlMICHLPQVLRLHLKRFSTNSL 582
Cdd:cd02669 292 KDGnEENIIPQVPL-KQLLKKYDGKT--------ETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 583 cilintllamlrssngkydqqtekitgwsgrnNREKIGVHVGFEEILNMEPYCCRETLKSLrPECFIYDLSAVVMHHGKG 662
Cdd:cd02669 349 --------------------------------FKEKNPTIVNFPIKNLDLSDYVHFDKPSL-NLSTKYNLVANIVHEGTP 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 530400884 663 FGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02669 396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-706 |
8.50e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 51.72 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 273 TGLRNLGNTCYMNSVLQVLSHLLIFRQcfLKLDLNQWLAMTASEKTRSCKHPPvtdtvvyqmnecQEKdtgfvcsrqssl 352
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRD--LVLNFDESKAELASDYPTERRIGG------------REV------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 353 ssglsggaskgRKMELIQPKEptsqyisLCHELHTLFQVMWSGKWALVSPFAMLhsvwrlipAFRGYAQQDAQEflceLL 432
Cdd:cd02666 56 -----------SRSELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE----CI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 433 DKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVT-CLACDNKSNTIEPFWDLSLEFPERYQCSGKDIA 511
Cdd:cd02666 106 DNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVDVGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 512 SQPCLVTEMLAKFTETEALEgkiyvcdqcnskrrrfSSKPVVLTEAQkqlmichLPQVLRLHLKRFSTNSLCILINTLLA 591
Cdd:cd02666 186 LEPKDLYDALDRYFDYDSLT----------------KLPQRSQVQAQ-------LAQPLQRELISMDRYELPSSIDDIDE 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 592 MLRSSNGKYDQQTEKITgWSGRNNREKIgvhvgfEEILnmepyccrETLKSlrpecFIYDLSAVVMHHGKGfGSGHYTAY 671
Cdd:cd02666 243 LIREAIQSESSLVRQAQ-NELAELKHEI------EKQF--------DDLKS-----YGYRLHAVFIHRGEA-SSGHYWVY 301
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 530400884 672 CYNSEGGFWVHCNDSKLSMCTMDEV------CKAQAYILFY 706
Cdd:cd02666 302 IKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
406-706 |
2.98e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 49.06 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 406 LHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIptsqrKLIKQvLNVVNnIFHGQLLSQVTCLACDNK 485
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSN-----IEIKR-LNPLE-AFKYTIESSYVCIGCSFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 486 SNTIEPFWDLSLEFPERYQCSGKDIASQpclvtemLAKFTETEAlegkiyVCDQCNSKRRRFSSKpvvlteaqkqlmICH 565
Cdd:cd02673 91 ENVSDVGNFLDVSMIDNKLDIDELLISN-------FKTWSPIEK------DCSSCKCESAISSER------------IMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400884 566 LPQVLRLHLKRFStnslcilintllamLRSSNGKYDQQTEKItgwsgrnnrekigvhvgfeeilnMEPYCcrETLKSlrp 645
Cdd:cd02673 146 FPECLSINLKRYK--------------LRIATSDYLKKNEEI-----------------------MKKYC--GTDAK--- 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400884 646 ecfiYDLSAVVMHHGKGFGSGHYTAYCYN-SEGGFWVHCNDSKLSMCTMDEVCKA---QAYILFY 706
Cdd:cd02673 184 ----YSLVAVICHLGESPYDGHYIAYTKElYNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| |
