|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
197-548 |
6.91e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 198.05 E-value: 6.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 197 RGLINAGNLCFLNATLQALLSCSPFVQLLQKI---QLQDIPKADSPTLAAFSEFISELDVPSSSSirnnvtvveagrPFR 273
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplSEDSRYNKDINLLCALRDLFKALQKNSKSS------------SVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 274 PAMFEGVLRNFTPDVLNNMsgrprQEDAQEFLSFIMDQMHDELlklkeqSPKVTASKSSVISSanddgdewetvgpknks 353
Cdd:pfam00443 69 PKMFKKSLGKLNPDFSGYK-----QQDAQEFLLFLLDGLHEDL------NGNHSTENESLITD----------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 354 avtrtqsfvpselseIFGGQLKSVVKAKGTKA-SATVQPYLLLHLDIHPDG----VQGIEDALHLFSAQEDLEGYRASVT 428
Cdd:pfam00443 121 ---------------LFRGQLKSRLKCLSCGEvSETFEPFSDLSLPIPGDSaelkTASLQICFLQFSKLEELDDEEKYYC 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 429 GKTGV-VSASKSIKIQKLSKIMILHLMRFSYGSQGSTKLRKGVKFPLELNLNR---SHLVSLSNESLRYELVATITHHGw 504
Cdd:pfam00443 186 DKCGCkQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRylaEELKPKTNNLQDYRLVAVVVHSG- 264
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 332660425 505 DPSKGHYTTDAR-RKNGQWLRFDDASVTPIGTKL-VLHDQAYVLFY 548
Cdd:pfam00443 265 SLSSGHYIAYIKaYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
196-548 |
6.21e-57 |
|
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: 192.88 E-value: 6.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 196 PRGLINAGNLCFLNATLQALLSCSPFVQ-LLQKIQLQDIPKADSPTLAAFSEFISeldvpssssirnnvTVVEAGRPFR- 273
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANyLLSREHSKDCCNEGFCMMCALEAHVE--------------RALASSGPGSa 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 274 PAMFEGVLRNFTPDVLNNmsgrpRQEDAQEFLSFIMDQMHDELLKLKEQSPKVtaskssvissanddgdewetvgpknkS 353
Cdd:cd02661 67 PRIFSSNLKQISKHFRIG-----RQEDAHEFLRYLLDAMQKACLDRFKKLKAV--------------------------D 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 354 AVTRTQSFVpselSEIFGGQLKSVVKAKGTKA-SATVQPYLLLHLDIHpdGVQGIEDALHLFSAQEDLEG---YRASVTG 429
Cdd:cd02661 116 PSSQETTLV----QQIFGGYLRSQVKCLNCKHvSNTYDPFLDLSLDIK--GADSLEDALEQFTKPEQLDGenkYKCERCK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 430 KtgVVSASKSIKIQKLSKIMILHLMRFSYGSQGstKLRKGVKFPLELNLnRSHLVSLSNESLRYELVATITHHGWDPSKG 509
Cdd:cd02661 190 K--KVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFPETLDL-SPYMSQPNDGPLKYKLYAVLVHSGFSPHSG 264
|
330 340 350
....*....|....*....|....*....|....*....
gi 332660425 510 HYTTDARRKNGQWLRFDDASVTPIGTKLVLHDQAYVLFY 548
Cdd:cd02661 265 HYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
198-549 |
1.72e-50 |
|
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: 174.21 E-value: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLScspfvqllqkiqlqdipkadsptlaafsefiseldvpssssirnnvtvveagrpfrpamf 277
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 egvlrnftpdvlnnmsgrpRQEDAQEFLSFIMDQMHDELLKLkeqspkvtaskssvissanddgdewetvgpknkSAVTR 357
Cdd:cd02257 21 -------------------EQQDAHEFLLFLLDKLHEELKKS---------------------------------SKRTS 48
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 358 TQSFVPSELSEIFGGQLKSVVK---AKGTKASATVQPYLLLHLDIHPDGVQGIEDALHLFSAQEDLEGYRASVTGKTGVV 434
Cdd:cd02257 49 DSSSLKSLIHDLFGGKLESTIVcleCGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQ 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 435 SASKSIKIQKLSKIMILHLMRFSYGSQGST-KLRKGVKFPLELNLNRSHLVSL-----SNESLRYELVATITHHGWDPSK 508
Cdd:cd02257 129 EATKRLKIKKLPPVLIIHLKRFSFNEDGTKeKLNTKVSFPLELDLSPYLSEGEkdsdsDNGSYKYELVAVVVHSGTSADS 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 332660425 509 GHYTTDAR-RKNGQWLRFDDASVTPIGTKLVL-----HDQAYVLFYK 549
Cdd:cd02257 209 GHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
197-549 |
8.69e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 139.04 E-value: 8.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 197 RGLINAGNLCFLNATLQALLSCSPFVQLLQKIQLQDIPKADSPTLA---AFSEFISELDVPSSSSirnnvtvveagrPFR 273
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSClscAMDEIFQEFYYSGDRS------------PYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 274 PAmfegvlrnftpDVLN-------NMSGRpRQEDAQEFLSFIMDQMHDELLKLKEqsPKVTASKSSVIssanddgdewet 346
Cdd:cd02660 69 PI-----------NLLYlswkhsrNLAGY-SQQDAHEFFQFLLDQLHTHYGGDKN--EANDESHCNCI------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 347 vgpknksavtrtqsfvpseLSEIFGGQLKSVVKAKG-TKASATVQPYLLLHLDI-------------HPDGVQGIEDALH 412
Cdd:cd02660 123 -------------------IHQTFSGSLQSSVTCQRcGGVSTTVDPFLDLSLDIpnkstpswalgesGVSGTPTLSDCLD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 413 LFSAQEDLEGYRASVTGKTGVVSASKSIKIQKLSKIMILHLMRFSYGSQG-STKLRKGVKFPLELNL--------NRSHL 483
Cdd:cd02660 184 RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtSRKIDTYVQFPLELNMtpytsssiGDTQD 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332660425 484 VSLSNESLRYELVATITHHGwDPSKGHYTTDARRKNGQWLRFDDASVTPIGTKLVLHDQAYVLFYK 549
Cdd:cd02660 264 SNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
297-549 |
6.03e-36 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 133.95 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 297 RQEDAQEFLSFIMDQMHdellklkeqspkvtaskssvissanddgdewetvgpknkSAVTRTqsfvpselseiFGGQLKS 376
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------------------------------------SIIVDL-----------FQGQLKS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 377 VVKAKGT-KASATVQPYLLLHLDI-----HPDGVQgIEDALHLFSAQEDLEG-YRASVTGKTGVVSASKSIKIQKLSKIM 449
Cdd:cd02674 51 RLTCLTCgKTSTTFEPFTYLSLPIpsgsgDAPKVT-LEDCLRLFTKEETLDGdNAWKCPKCKKKRKATKKLTISRLPKVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 450 ILHLMRFSYGSQGSTKLRKGVKFPLE-LNLNRSHLVSLSNESLRYELVATITHHGwDPSKGHYTTDARRKN-GQWLRFDD 527
Cdd:cd02674 130 IIHLKRFSFSRGSTRKLTTPVTFPLNdLDLTPYVDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDD 208
|
250 260
....*....|....*....|..
gi 332660425 528 ASVTPIGTKLVLHDQAYVLFYK 549
Cdd:cd02674 209 SRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-551 |
5.22e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 108.88 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQ-LLQKIQLQDIPKADSPTLAAFSEFIsELDVPSSSSIRNNVTvveagrpfrpam 276
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNaVYSIPPTEDDDDNKSVPLALQRLFL-FLQLSESPVKTTELT------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 277 feGVLRNFTPDVLNNMsgrpRQEDAQEFLSFIMDQMHDELLKLKeqspkvtaskssvissanddgdewetvgpknksavt 356
Cdd:cd02659 71 --DKTRSFGWDSLNTF----EQHDVQEFFRVLFDKLEEKLKGTG------------------------------------ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 357 rtqsfVPSELSEIFGGQLKSVVKAKGTKA-SATVQPYLLLHLDIHpdGVQGIEDALHLFSAQEDLEG---YRASVTGKtg 432
Cdd:cd02659 109 -----QEGLIKNLFGGKLVNYIICKECPHeSEREEYFLDLQVAVK--GKKNLEESLDAYVQGETLEGdnkYFCEKCGK-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 433 VVSASKSIKIQKLSKIMILHLMRFSYG--SQGSTKLRKGVKFPLELNLNR----------SHLVSLSNESLRYELVATIT 500
Cdd:cd02659 180 KVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLELDMEPytekglakkeGDSEKKDSESYIYELHGVLV 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332660425 501 HHGwDPSKGHYTTDAR-RKNGQWLRFDDASVTPIGTKLVLHDQ----------------------AYVLFYKQV 551
Cdd:cd02659 260 HSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-549 |
8.67e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 107.40 E-value: 8.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLscspFVQLLQkiQLQDIpkadsptlaaFSEFiseldvpSSSSIRNNVTvveagrpfRPAMF 277
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLT--CLKDL----------FESI-------SEQKKRTGVI--------SPKKF 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 EGVLRNFTPDVLNNMsgrprQEDAQEFLSFIMDQMHDELLKLKEQSPKVTaskssviSSANDDGDEWETvgpknksavtr 357
Cdd:cd02663 50 ITRLKRENELFDNYM-----HQDAHEFLNFLLNEIAEILDAERKAEKANR-------KLNNNNNAEPQP----------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 358 tqSFVpselSEIFGGQLKSVVKAKGTKA-SATVQPYLLLHLDIHPDgvQGIEDALHLFSAQEDLEG----YRASVTGKTg 432
Cdd:cd02663 107 --TWV----HEIFQGILTNETRCLTCETvSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGrnkfYCDECCSLQ- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 433 vvSASKSIKIQKLSKIMILHLMRFSYGSQ--GSTKLRKGVKFPLELNLNRSHLVSLSNESLrYELVATITHHGWDPSKGH 510
Cdd:cd02663 178 --EAEKRMKIKKLPKILALHLKRFKYDEQlnRYIKLFYRVVFPLELRLFNTTDDAENPDRL-YELVAVVVHIGGGPNHGH 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 332660425 511 YTTDARRKNGqWLRFDDASVTPIGTKLVLH--------DQAYVLFYK 549
Cdd:cd02663 255 YVSIVKSHGG-WLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-549 |
4.41e-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: 105.49 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQ--KIQLQDIPKADSPTLAAFSEFISELDvpssssirnnvtvvEAGRPFRPA 275
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnyNPARRGANQSSDNLTNALRDLFDTMD--------------KKQEPVPPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 276 MFEGVLRNFTPDVLN-NMSGRPRQEDAQEFLSFIMDQMHDELlklkeqspKVTASKSSVISsanddgdewetvgpknksa 354
Cdd:cd02657 67 EFLQLLRMAFPQFAEkQNQGGYAQQDAEECWSQLLSVLSQKL--------PGAGSKGSFID------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 355 vtrtqsfvpselsEIFGGQLKSVVKAKGTKASATV--QPYLLLHLDIHPDG-VQGIEDALHLFSAQEDLEgyRASVTGKT 431
Cdd:cd02657 120 -------------QLFGIELETKMKCTESPDEEEVstESEYKLQCHISITTeVNYLQDGLKKGLEEEIEK--HSPTLGRD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 432 GVVSasKSIKIQKLSKIMILHLMRFSYGSQGSTK---LRKgVKFPLELNLnrshlVSLSNESLRYELVATITHHGWDPSK 508
Cdd:cd02657 185 AIYT--KTSRISRLPKYLTVQFVRFFWKRDIQKKakiLRK-VKFPFELDL-----YELCTPSGYYELVAVITHQGRSADS 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 332660425 509 GHYTTDARRKN-GQWLRFDDASVTPIGTKLVLH-------DQAYVLFYK 549
Cdd:cd02657 257 GHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-548 |
4.64e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 96.30 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCspfvqllqkiqlqdipkadsptlAAFSEFISEldvpssssirnnvtvveagrpfRPAMF 277
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQT-----------------------PALRELLSE----------------------TPKEL 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 EGVLRNFTPDVLNNmsgrpRQEDAQEFLSFIMDQMhdellklkeqspkvtaskSSVISSanddgdewetvgpknksavtr 357
Cdd:cd02667 36 FSQVCRKAPQFKGY-----QQQDSHELLRYLLDGL------------------RTFIDS--------------------- 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 358 tqsfvpselseIFGGQLKSVVKAKGTKA-SATVQPYLLLHLDIH--PDGVQGIEDALHLFSAQEDLEGyrasvTGKTGVV 434
Cdd:cd02667 72 -----------IFGGELTSTIMCESCGTvSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEG-----NNKFACE 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 435 SASKSIK---IQKLSKIMILHLMRFSYGSQGST-KLRKGVKFPLELNLNR----SHLVSLSNESLRYELVATITHHGwDP 506
Cdd:cd02667 136 NCTKAKKqylISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFPEILDLAPfcdpKCNSSEDKSSVLYRLYGVVEHSG-TM 214
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332660425 507 SKGHYTTDARRKN----------------------GQWLRFDDASVTPIGTKLVLHDQAYVLFY 548
Cdd:cd02667 215 RSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
407-549 |
1.44e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.56 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 407 IEDALHLFSAQEDL-EGYRASVTGKTGVVSASKSIKIQKLSKIMILHLMRFSYGSQGSTKLRKGVKFPL-ELNLNRsHLV 484
Cdd:COG5560 677 LQDCLNEFSKPEQLgLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIdDLDLSG-VEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332660425 485 SLSNESLRYELVATITHHGWdPSKGHYTTDARR-KNGQWLRFDDASVTPIGTKLVLHDQAYVLFYK 549
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARNfANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-549 |
1.64e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 83.53 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQKI-QLQDIPKADsPTLAAFSEFISELDVPSSSSIRNNVTVVEAGRPF---- 272
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLeNKFPSDVVD-PANDLNCQLIKLADGLLSGRYSKPASLKSENDPYqvgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 273 RPAMFEGVLRNFTPDVLNNmsgrpRQEDAQEFLSFIMDQMHDELLKLKEQSPkvTASKSSVIssanddGDEWETvgpKNK 352
Cdd:cd02658 80 KPSMFKALIGKGHPEFSTM-----RQQDALEFLLHLIDKLDRESFKNLGLNP--NDLFKFMI------EDRLEC---LSC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 353 SAVTRTqsfvpSELSEIFGGQLKSVVKAKGTKASatvqpylLLHLDIHpdgvqgIEDALHLFSAQEDLEGYRASVTGKTG 432
Cdd:cd02658 144 KKVKYT-----SELSEILSLPVPKDEATEKEEGE-------LVYEPVP------LEDCLKAYFAPETIEDFCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 433 vvsASKSIKIQKLSKIMILHLMRFSYGSQG-STKLRKGVKFPLELNlnrshlvslsneSLRYELVATITHHGWDPSKGHY 511
Cdd:cd02658 206 ---ATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPIDVPEELG------------PGKYELIAFISHKGTSVHSGHY 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 332660425 512 TTDARRK---NGQWLRFDD----ASVTPIGTKlvlhDQAYVLFYK 549
Cdd:cd02658 271 VAHIKKEidgEGKWVLFNDekvvASQDPPEMK----KLGYIYFYQ 311
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-536 |
2.39e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 83.24 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQKIQLQDIPkadsptlaafsefisELDVPSSSSIRNNVTVVEAGRPFRPAMF 277
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDA---------------ELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 EGVLRNFTPDVLNNMSG--RPRQEDAQEFLSFIMDQMHDELLKLKeqspkvtaskssvissanddgdewetvgpkNKSAV 355
Cdd:cd02668 66 FGNRSVVDPSGFVKALGldTGQQQDAQEFSKLFLSLLEAKLSKSK------------------------------NPDLK 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 356 TRTQsfvpselsEIFGGQLKSV-VKAKGTKASATVQPYLLLHLDIHpdGVQGIEDALHLFSAQEDLEG---YRASVTGKT 431
Cdd:cd02668 116 NIVQ--------DLFRGEYSYVtQCSKCGRESSLPSKFYELELQLK--GHKTLEECIDEFLKEEQLTGdnqYFCESCNSK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 432 gvVSASKSIKIQKLSKIMILHLMRFSYGSQGST--KLRKGVKFPLELNLNRsHLVSLSNESLRYELVATITHHGWDPSKG 509
Cdd:cd02668 186 --TDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkkKLNASISFPEILDMGE-YLAESDEGSYVYELSGVLIHQGVSAYSG 262
|
330 340
....*....|....*....|....*...
gi 332660425 510 HYTTDAR-RKNGQWLRFDDASVTPIGTK 536
Cdd:cd02668 263 HYIAHIKdEQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-548 |
5.56e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 77.41 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQKIQlqdipkadsptlaafsefiseldvpssssirnnvtvveagrpfrpamf 277
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFL------------------------------------------------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 egvlrnftpdvlnnmsgrpRQEDAQEFLSFIMDQMHDELLKLKEqspkvtaskssvissanddgdewetvGPKNKSAVTR 357
Cdd:cd02662 33 -------------------EQQDAHELFQVLLETLEQLLKFPFD--------------------------GLLASRIVCL 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 358 TQSFVPSELSEIFGGQLKSVVKAKGtkasatVQPYLLLHLdihpdgvqgiedaLHLFSAQEDLEGYRasvtgktgvvSAS 437
Cdd:cd02662 68 QCGESSKVRYESFTMLSLPVPNQSS------GSGTTLEHC-------------LDDFLSTEIIDDYK----------CDR 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 438 KSIKIQKLSKIMILHLMRFSYGSQG-STKLRKGVKFPLELNlnrshlvslsneSLRYELVATITHHGwDPSKGHYTTdAR 516
Cdd:cd02662 119 CQTVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERLP------------KVLYRLRAVVVHYG-SHSSGHYVC-YR 184
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 332660425 517 RKN----------------------GQWLRFDDASVTPIGTKLVLHD-QAYVLFY 548
Cdd:cd02662 185 RKPlfskdkepgsfvrmregpsstsHPWWRISDTTVKEVSESEVLEQkSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
198-550 |
8.96e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.92 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQallscspfvqllqkiqlqdipkadspTLAAFSEFISELDVPSSSSIRNNVTVVEAGRPfrPAMF 277
Cdd:COG5533 1 GLPNLGNTCFMNSVLQ--------------------------ILALYLPKLDELLDDLSKELKVLKNVIRKPEP--DLNQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 EGVLRNFTPDV---------LNNMSGrprQEDAQEFLSFIMDqmHDELLKLKEQSPKVTASKSSVISSANDDgdeWETVg 348
Cdd:COG5533 53 EEALKLFTALWsskehkvgwIPPMGS---QEDAHELLGKLLD--ELKLDLVNSFTIRIFKTTKDKKKTSTGD---WFDI- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 349 pkNKSAVTRTQSFVPSELSEIFGGQLKSVVKAKGTKASatvqpylllhldihpdgvqgIEDALHLFSAQEDlegyrasvt 428
Cdd:COG5533 124 --IIELPDQTWVNNLKTLQEFIDNMEELVDDETGVKAK--------------------ENEELEVQAKQEY--------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 429 gktgvvsaskSIKIQKLSKIMILHLMRFSYgSQGSTKLRKGVKFPLELNLNRSHlVSLSNESLRYELVATITHHGwDPSK 508
Cdd:COG5533 173 ----------EVSFVKLPKILTIQLKRFAN-LGGNQKIDTEVDEKFELPVKHDQ-ILNIVKETYYDLVGFVLHQG-SLEG 239
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 332660425 509 GHYTTDARrKNGQWLRFDDASVTPI---GTKLVLHDQAYVLFYKQ 550
Cdd:COG5533 240 GHYIAYVK-KGGKWEKANDSDVTPVseeEAINEKAKNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-549 |
4.58e-14 |
|
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: 74.28 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSP---FVQLLQKIQLQDIPKadSPTLAAFSEFISELdvPSSSSIRNNVTVVEagrpfrp 274
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPirnFFLLYENYENIKDRK--SELVKRLSELIRKI--WNPRNFKGHVSPHE------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 275 amfegvLRNFTPDVLNNMSGRPRQEDAQEFLSFIMDQMHdellklkEQSPKVTASKSSVISSANDdgdewetvGPKNKsa 354
Cdd:cd02669 190 ------LLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLH-------KDLGGSKKPNSSIIHDCFQ--------GKVQI-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 355 vtRTQSFVPSELSEIFGGQLKSVVKAKGTKasatVQPYLLLHLDIHP-----DGVQgiEDALHLFSAQEDLEGYrasvTG 429
Cdd:cd02669 247 --ETQKIKPHAEEEGSKDKFFKDSRVKKTS----VSPFLLLTLDLPPpplfkDGNE--ENIIPQVPLKQLLKKY----DG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 430 KTgVVSASKSIK---IQKLSKIMILHLMRFSYGSQGSTKLRKGVKFPLELNLNRSHL---VSLSNESLRYELVATITHHG 503
Cdd:cd02669 315 KT-ETELKDSLKrylISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVhfdKPSLNLSTKYNLVANIVHEG 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 332660425 504 WDPSKGHYTTDARRK-NGQWLRFDDASVTPIGTKLVLHDQAYVLFYK 549
Cdd:cd02669 394 TPQEDGTWRVQLRHKsTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
198-541 |
1.78e-12 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 70.28 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQKIQlQDIPKADSPTLAAFSEFISELDVpssssIRNNVTVVEAGRPFRPAMF 277
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-TDHPRGRDSVALALQRLFYNLQT-----GEEPVDTTELTRSFGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 EGVLrnftpdvlnnmsgrprQEDAQEFLSFIMDQMhdellklkEQSPKVTAskssvissanddgdewetvgpknksavtr 357
Cdd:COG5077 269 DSFM----------------QHDIQEFNRVLQDNL--------EKSMRGTV----------------------------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 358 tqsfVPSELSEIFGGQLKSVVKA-KGTKASATVQPYLLLHLDIhpDGVQGIEDALHLFSAQEDLEGYRASVTGKTGVVSA 436
Cdd:COG5077 296 ----VENALNGIFVGKMKSYIKCvNVNYESARVEDFWDIQLNV--KGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 437 SKSIKIQKLSKIMILHLMRFSYG--SQGSTKLRKGVKFPLELNLnrshLVSLSNESLR-------YELVATITHHGwDPS 507
Cdd:COG5077 370 KKGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLEIDL----LPFLDRDADKsensdavYVLYGVLVHSG-DLH 444
|
330 340 350
....*....|....*....|....*....|....*
gi 332660425 508 KGHYTTDAR-RKNGQWLRFDDASVTPIGTKLVLHD 541
Cdd:COG5077 445 EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEE 479
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-549 |
4.77e-12 |
|
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: 67.13 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQKIQLQdIPKADSPTLAAFSEFISELDVPSSSSIRNNVTVVEAGRPfrPAmf 277
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLP-RLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRP--PW-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 278 egvlrnFTPDvlnnmsgrpRQEDAQEFLSFIMDQMHdellklkeqspkvtaskssvissanddgdewetvgpknksavtr 357
Cdd:cd02664 76 ------FTPG---------SQQDCSEYLRYLLDRLH-------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 358 tqsfvpSELSEIFGGQLKSVVK-AKGTKASATVQPYLLLHLdihpdGVQGIEDALHLFSAQEDLEG---YRASVTGKtgV 433
Cdd:cd02664 97 ------TLIEKMFGGKLSTTIRcLNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGdnqYYCEKCAS--L 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 434 VSASKSIKIQKLSKIMILHLMRFSY--GSQGSTKLRKGVKFPLELNLN-RSHLVSLSN-----------------ESLRY 493
Cdd:cd02664 164 QDAEKEMKVTGAPEYLILTLLRFSYdqKTHVREKIMDNVSINEVLSLPvRVESKSSESplekkeeesgddgelvtRQVHY 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 494 ELVATITHHGWDPSKGHYTTDAR---------------------RKNGQWLRFDDASVTPIGTKLVL-------HDQAYV 545
Cdd:cd02664 244 RLYAVVVHSGYSSESGHYFTYARdqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYI 323
|
....
gi 332660425 546 LFYK 549
Cdd:cd02664 324 LFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-549 |
2.68e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 64.91 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSPFVQLLQ--------KIQLQdipkadSPTLAAFSEFISELDVPSSSSIRNNVTVVEAg 269
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKhlvslissVEQLQ------SSFLLNPEKYNDELANQAPRRLLNALREVNP- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 270 rpfrpaMFEGVLrnftpdvlnnmsgrprQEDAQEFLSFIMDQMHDELLKLKEqspKVTASKSSVISSanddgdewETVgp 349
Cdd:cd02671 99 ------MYEGYL----------------QHDAQEVLQCILGNIQELVEKDFQ---GQLVLRTRCLEC--------ETF-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 350 knksaVTRTQSF----VPSELSEIFGGQLKSVVKAKGTKASATVQpylllhldihpdgvqgieDALHLFSAQEDLEG--- 422
Cdd:cd02671 144 -----TERREDFqdisVPVQESELSKSEESSEISPDPKTEMKTLK------------------WAISQFASVERIVGedk 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 423 YRASVTgkTGVVSASKSIKIQKLSKIMILHLMRFSYGSQ------GSTKLRKGVKFPLELNLnrsHLVSLSNESLRYELV 496
Cdd:cd02671 201 YFCENC--HHYTEAERSLLFDKLPEVITIHLKCFAANGSefdcygGLSKVNTPLLTPLKLSL---EEWSTKPKNDVYRLF 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332660425 497 ATITHHGWDPSKGHYTTDARrkngqWLRFDDASVTPIGTKLVLH---------DQAYVLFYK 549
Cdd:cd02671 276 AVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFYK 332
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
198-399 |
5.26e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 62.21 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 198 GLINAGNLCFLNATLQALLSCSP----FVQLLQKIQL-QDIPKADSPTLA-AFSEFISELDVPSSSSirnnvtvveagrp 271
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWElrdyFLSDEYEESInEENPLGMHGSVAsAYADLIKQLYDGNLHA------------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 272 FRPAMFEGVLRNFTPDVLNNMsgrprQEDAQEFLSFIMDQMHDEL--LKLKEQSPKVTASKSSVISSANDDGDEWETVGP 349
Cdd:COG5560 334 FTPSGFKKTIGSFNEEFSGYD-----QQDSQEFIAFLLDGLHEDLnrIIKKPYTSKPDLSPGDDVVVKKKAKECWWEHLK 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 332660425 350 KNKSAVTrtqsfvpselsEIFGGQLKSVVKAKGT-KASATVQPYLLLHLDI 399
Cdd:COG5560 409 RNDSIIT-----------DLFQGMYKSTLTCPGCgSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
435-548 |
4.48e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 51.38 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 435 SASKSIKIQKLSKIMILHLMRFsygsqgstKLRKGVKfpLELNLNRSHLVSLSNESLRYELVATITHHGWDPSKGHYTTD 514
Cdd:cd02673 136 SAISSERIMTFPECLSINLKRY--------KLRIATS--DYLKKNEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAY 205
|
90 100 110
....*....|....*....|....*....|....*....
gi 332660425 515 ARR--KNGQWLRFDDASVTPIGTKLVLHD---QAYVLFY 548
Cdd:cd02673 206 TKElyNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
196-531 |
6.77e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 48.26 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 196 PRGLINAGNLCFLNATLQALLSCSPfvqlLQKIQLQ-DIPKADSPTLAAFSEFISELDVPSSSSIRNNVTVVEAGRPFRp 274
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKP----LRDLVLNfDESKAELASDYPTERRIGGREVSRSELQRSNQFVYELRSLFN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 275 AMFEGVLRNFTPD-VLNNMSgrPRQEDAQEFLSFIMDQMHDELlklkeqspkVTASKSSVISSANDDGDEWETVgpKNKS 353
Cdd:cd02666 76 DLIHSNTRSVTPSkELAYLA--LRQQDVTECIDNVLFQLEVAL---------EPISNAFAGPDTEDDKEQSDLI--KRLF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 354 AVTRTQSFVPselsEIFGGQLKsvVKAKGTKASATVQPYLLLHLDIHP-DGVQGIEDAL-------HLFSAQEDLEGYRA 425
Cdd:cd02666 143 SGKTKQQLVP----ESMGNQPS--VRTKTERFLSLLVDVGKKGREIVVlLEPKDLYDALdryfdydSLTKLPQRSQVQAQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 426 SVTGKTGVVSASKSIKIQKLSK---IMILHLMRfsygsQGSTKLRKGVKFPLELNLNRSHLVSlSNESLRYELVATITHH 502
Cdd:cd02666 217 LAQPLQRELISMDRYELPSSIDdidELIREAIQ-----SESSLVRQAQNELAELKHEIEKQFD-DLKSYGYRLHAVFIHR 290
|
330 340 350
....*....|....*....|....*....|
gi 332660425 503 GwDPSKGHYTTDAR-RKNGQWLRFDDASVT 531
Cdd:cd02666 291 G-EASSGHYWVYIKdFEENVWRKYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
402-548 |
1.94e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 42.93 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 402 DGVQGIEDALHLFSAQEDLEGYRASVTGKTGVVSASksikiQKLSKIMILHLMRFSYGSQGSTKLRKGVKFPLELNlnrs 481
Cdd:cd02665 90 NGYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWF-----TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQIIQ---- 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332660425 482 hlvslsneSLRYELVATITHHGwDPSKGHYTTDARRKNGQ-WLRFDDASVTPIGTKLVLHD--------QAYVLFY 548
Cdd:cd02665 161 --------QVPYELHAVLVHEG-QANAGHYWAYIYKQSRQeWEKYNDISVTESSWEEVERDsfgggrnpSAYCLMY 227
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
442-530 |
2.21e-03 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 40.33 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660425 442 IQKLSKIMILHLMRFSygsQGSTKLRKGVKF-PLELNLNRSHLVSLSNESLRYELVATITHHGWDPSKGHY--------T 512
Cdd:pfam13423 211 VRNLPPVLSLNAALTN---EEWRQLWKTPGWlPPEIGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLvsfvkvadS 287
|
90
....*....|....*...
gi 332660425 513 TDARRKNGQWLRFDDASV 530
Cdd:pfam13423 288 ELEDPTESQWYLFNDFLV 305
|
|
| |
