|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
194-473 |
1.66e-34 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 132.95 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 194 RGLINTGNLCFLNATLQALLSCSPFVQLLQRLR-----LRNIPKVGFPtlTAFAEFVSDFDVPSSNpnvkkkdttvleig 268
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplsedSRYNKDINLL--CALRDLFKALQKNSKS-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 269 RPFSPAMFEAVLKSFTPDVPNSisgrpRQEDAQEFLSFIMDQMHNELIKLDGQPSSSIgvrsslvssveddewetvgpkn 348
Cdd:pfam00443 65 SSVSPKMFKKSLGKLNPDFSGY-----KQQDAQEFLLFLLDGLHEDLNGNHSTENESL---------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 349 ksaitrtqsflpseLSDIFGGQLRSVVKARGNKA-SATVQPFLLLHLDIHPEAVLTIE----DALHLFSAPEYLEGYRAS 423
Cdd:pfam00443 118 --------------ITDLFRGQLKSRLKCLSCGEvSETFEPFSDLSLPIPGDSAELKTaslqICFLQFSKLEELDDEEKY 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 508725699 424 TAGKAGV-VTARKSVKIQTLSKIMILHLMRFSYGSQGSTKLHKPVRFPLEL 473
Cdd:pfam00443 184 YCDKCGCkQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLEL 234
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-491 |
8.27e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 130.86 E-value: 8.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 194 RGLINTGNLCFLNATLQALLSCSPFVQ-LLQRLRLRNIPKVGFPTLTAFAEFVsdfdvpssnpnvkkkdTTVLEIGRPFS 272
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANyLLSREHSKDCCNEGFCMMCALEAHV----------------ERALASSGPGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 273 -PAMFEAVLKSFTPDVpnsisGRPRQEDAQEFLSFIMDQMHNelIKLDGQPSSSIGVRSSLVSSVeddewetvgpknksa 351
Cdd:cd02661 66 aPRIFSSNLKQISKHF-----RIGRQEDAHEFLRYLLDAMQK--ACLDRFKKLKAVDPSSQETTL--------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 352 itrtqsflpseLSDIFGGQLRSVVKA-RGNKASATVQPFLLLHLDIHpeAVLTIEDALHLFSAPEYLEG---YRASTAGK 427
Cdd:cd02661 124 -----------VQQIFGGYLRSQVKClNCKHVSNTYDPFLDLSLDIK--GADSLEDALEQFTKPEQLDGenkYKCERCKK 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 508725699 428 agVVTARKSVKIQTLSKIMILHLMRFSYGSQGstKLHKPVRFPLELVLgRELLVSPSTEYFIYR 491
Cdd:cd02661 191 --KVKASKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFPETLDL-SPYMSQPNDGPLKYK 249
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
195-484 |
4.11e-29 |
|
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: 116.04 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLScspfvqllqrlrlrnipkvgfptltafaefvsdfdvpssnpnvkkkdttvleigrpfspa 274
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 275 mfeavlksftpdvpnsisgrpRQEDAQEFLSFIMDQMHNELikldgqpsssigvrsslvssveddewetvgpKNKSAITR 354
Cdd:cd02257 21 ---------------------EQQDAHEFLLFLLDKLHEEL-------------------------------KKSSKRTS 48
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 355 TQSFLPSELSDIFGGQLRSVVK---ARGNKASATVQPFLLLHLDIHPEAVLTIEDALHLFSAPEYLEGYRASTAGKAGVV 431
Cdd:cd02257 49 DSSSLKSLIHDLFGGKLESTIVcleCGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQ 128
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 508725699 432 TARKSVKIQTLSKIMILHLMRFSYGSQGST-KLHKPVRFPLELVLGRELLVSPS 484
Cdd:cd02257 129 EATKRLKIKKLPPVLIIHLKRFSFNEDGTKeKLNTKVSFPLELDLSPYLSEGEK 182
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
296-491 |
1.11e-18 |
|
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: 85.42 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 296 RQEDAQEFLSFIMDQMHnelikldgqpsssigvrsslvssveddewetvgpknkSAITRTqsflpselsdiFGGQLRSVV 375
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH-------------------------------------SIIVDL-----------FQGQLKSRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 376 KARG-NKASATVQPFLLLHLDI----HPEAVLTIEDALHLFSAPEYLEGYRASTAGKAGVVT-ARKSVKIQTLSKIMILH 449
Cdd:cd02674 53 TCLTcGKTSTTFEPFTYLSLPIpsgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRkATKKLTISRLPKVLIIH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 508725699 450 LMRFSYGSQGSTKLHKPVRFPLE-LVLGRELLVSPSTEYFIYR 491
Cdd:cd02674 133 LKRFSFSRGSTRKLTTPVTFPLNdLDLTPYVDTRSFTGPFKYD 175
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-473 |
5.93e-18 |
|
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: 85.12 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 194 RGLINTGNLCFLNATLQALLSCSPFVQLLQRLRLRNIPKVGFPTLT---AFAEFVSDFDVPSSNpnvkkkdttvleigRP 270
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSClscAMDEIFQEFYYSGDR--------------SP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 271 FSPAmfeAVLKSFTPDVPNsISGRpRQEDAQEFLSFIMDQMHNELIKLDGQPSSsigvrsslvssveddewetvgPKNKS 350
Cdd:cd02660 67 YGPI---NLLYLSWKHSRN-LAGY-SQQDAHEFFQFLLDQLHTHYGGDKNEAND---------------------ESHCN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 351 AITRTqsflpselsdIFGGQLRS-VVKARGNKASATVQPFLLLHLDI-------------HPEAVLTIEDALHLFSAPEY 416
Cdd:cd02660 121 CIIHQ----------TFSGSLQSsVTCQRCGGVSTTVDPFLDLSLDIpnkstpswalgesGVSGTPTLSDCLDRFTRPEK 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 508725699 417 LEGYRASTAGKAGVVTARKSVKIQTLSKIMILHLMRFSYGSQG-STKLHKPVRFPLEL 473
Cdd:cd02660 191 LGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtSRKIDTYVQFPLEL 248
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-477 |
1.16e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 75.05 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCSPFVQLLQRLRLRNIPKVGFPTL---TAFAE----FVSDfdvPSSNPNVKKKDTTVLEI 267
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANdlnCQLIKladgLLSG---RYSKPASLKSENDPYQV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 268 GrpFSPAMFEAVLKSFTPDVPNSisgrpRQEDAQEFLSFIMDQMHNELIKLDGQpsssigvrsslvssveddewetvgpk 347
Cdd:cd02658 78 G--IKPSMFKALIGKGHPEFSTM-----RQQDALEFLLHLIDKLDRESFKNLGL-------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 348 nksaitrtqsflpsELSDIFGGQLRSVVKARG-NKASATVQPFLLLHLDI---------HPEAV---LTIEDALHLFSAP 414
Cdd:cd02658 125 --------------NPNDLFKFMIEDRLECLScKKVKYTSELSEILSLPVpkdeatekeEGELVyepVPLEDCLKAYFAP 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 508725699 415 EYLEGYRASTAGKagvVTARKSVKIQTLSKIMILHLMRFSYGSQG-STKLHKPVRFPLELVLGR 477
Cdd:cd02658 191 ETIEDFCSTCKEK---TTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPIDVPEELGPGK 251
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-473 |
1.11e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 66.51 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCSPF-------------------VQLLQRLRLrnipkvgfptLTAFAEfvSDFDVPSSNP 255
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFrnavysippteddddnksvPLALQRLFL----------FLQLSE--SPVKTTELTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 256 NVKKKDTTVLEIGRpfspamfeavlksftpdvpnsisgrprQEDAQEFLSFIMDQMHNELIKLdGQPSSsigvrsslvss 335
Cdd:cd02659 72 KTRSFGWDSLNTFE---------------------------QHDVQEFFRVLFDKLEEKLKGT-GQEGL----------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 336 veddewetvgpknksaitrtqsflpseLSDIFGGQLRSVVKARG-NKASATVQPFLLLHLDIHPEAvlTIEDALHLFSAP 414
Cdd:cd02659 113 ---------------------------IKNLFGGKLVNYIICKEcPHESEREEYFLDLQVAVKGKK--NLEESLDAYVQG 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 508725699 415 EYLEG---YRASTAGKagVVTARKSVKIQTLSKIMILHLMRFSYG--SQGSTKLHKPVRFPLEL 473
Cdd:cd02659 164 ETLEGdnkYFCEKCGK--KVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLEL 225
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
195-396 |
1.67e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 67.22 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCspfvqllqrlrlrnipkvgfPTLTAFaeFVSDF---DVPSSNPN-------------VK 258
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHT--------------------WELRDY--FLSDEyeeSINEENPLgmhgsvasayadlIK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 259 KKDTTVLEigrPFSPAMFEAVLKSFTpdvpNSISGRpRQEDAQEFLSFIMDQMHNELIKLDGQPSSS----IGVRSSLVS 334
Cdd:COG5560 325 QLYDGNLH---AFTPSGFKKTIGSFN----EEFSGY-DQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdlSPGDDVVVK 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508725699 335 SVEDDEWETVGPKNKSAITrtqsflpselsDIFGGQLRSVVKARG-NKASATVQPFLLLHLDI 396
Cdd:COG5560 397 KKAKECWWEHLKRNDSIIT-----------DLFQGMYKSTLTCPGcGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-475 |
2.55e-10 |
|
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: 61.94 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLscspFVQLLQRLRLRnipkvgfptltafaefvsdFDVPSSNpnvkKKDTTVLeigrpfSPA 274
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLTCLKDL-------------------FESISEQ----KKRTGVI------SPK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 275 MFEAVLKSFTPDVPNSIsgrprQEDAQEFLSFIMdqmhNELIKLDGQPSSSIGVRSSLVSSVEDdEWEtvgpknksaitr 354
Cdd:cd02663 48 KFITRLKRENELFDNYM-----HQDAHEFLNFLL----NEIAEILDAERKAEKANRKLNNNNNA-EPQ------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 355 tqsflPSELSDIFGGQLRSVVKA-RGNKASATVQPFLLLHLDIHPEAVLTieDALHLFSAPEYLEG----YRASTAGKAg 429
Cdd:cd02663 106 -----PTWVHEIFQGILTNETRClTCETVSSRDETFLDLSIDVEQNTSIT--SCLRQFSATETLCGrnkfYCDECCSLQ- 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 508725699 430 vvTARKSVKIQTLSKIMILHLMRFSYGSQ--GSTKLHKPVRFPLELVL 475
Cdd:cd02663 178 --EAEKRMKIKKLPKILALHLKRFKYDEQlnRYIKLFYRVVFPLELRL 223
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-476 |
6.66e-10 |
|
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: 60.48 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCspfvQLLQRLRLRNiPKVGFPTLTAFAEFVSDFDvpssnpnvkkkdttvleigrpfspa 274
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQT----PALRELLSET-PKELFSQVCRKAPQFKGYQ------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 275 mfeavlksftpdvpnsisgrprQEDAQEFLSFIMDQMhnelikldgqpsssigvrsslvssveddewetvgpknksaITR 354
Cdd:cd02667 51 ----------------------QQDSHELLRYLLDGL----------------------------------------RTF 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 355 TQSflpselsdIFGGQLRSVVKA-RGNKASATVQPFLLLHLDIHPEAV--LTIEDALHLFSAPEYLEGYRASTAGKAgvV 431
Cdd:cd02667 69 IDS--------IFGGELTSTIMCeSCGTVSLVYEPFLDLSLPRSDEIKseCSIESCLKQFTEVEILEGNNKFACENC--T 138
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 508725699 432 TARKSVKIQTLSKIMILHLMRFSYGSQGST-KLHKPVRFPLELVLG 476
Cdd:cd02667 139 KAKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFPEILDLA 184
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-473 |
2.21e-08 |
|
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: 55.06 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCSPFVQLLQRLRlrnipkvgfptltafaefvsdfdvpssnpnvkkkdttvleigrpfspa 274
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFL------------------------------------------------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 275 mfeavlksftpdvpnsisgrpRQEDAQEFLSFIMDQMHNEL-IKLDGQPSSSIGVRSSlvSSVEDDEWETvgpknksait 353
Cdd:cd02662 33 ---------------------EQQDAHELFQVLLETLEQLLkFPFDGLLASRIVCLQC--GESSKVRYES---------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 354 rtqsflpselsdifggqlrsvvkargnkasatvqpFLLLHLDIHPEAV---LTIEDALHLFSAPEYLEGYRAStagkagv 430
Cdd:cd02662 80 -----------------------------------FTMLSLPVPNQSSgsgTTLEHCLDDFLSTEIIDDYKCD------- 117
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 508725699 431 vtaRKSVKIQTLSKIMILHLMRFSYGSQG-STKLHKPVRFPLEL 473
Cdd:cd02662 118 ---RCQTVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERL 158
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-487 |
3.84e-08 |
|
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: 55.41 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCSPFVQLLqrlrLRNIPKVGFPTLTAFAEFVSdfdvpssnpnVKKKDTTVLEIGRPFSPA 274
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL----KNYNPARRGANQSSDNLTNA----------LRDLFDTMDKKQEPVPPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 275 MFEAVL-KSFTPDVPNSISGRPRQEDAQEFLSFIMDQMHNELIKLDGQPSSsigvrsslvssveddewetvgpknksait 353
Cdd:cd02657 67 EFLQLLrMAFPQFAEKQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF----------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 354 rtqsflpseLSDIFGGQLRSVVK--ARGNKASATVQPFLLLHLDIHPEA-VLTIEDALhLFSAPEYLEGYRASTAGKAgv 430
Cdd:cd02657 118 ---------IDQLFGIELETKMKctESPDEEEVSTESEYKLQCHISITTeVNYLQDGL-KKGLEEEIEKHSPTLGRDA-- 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 508725699 431 vTARKSVKIQTLSKIMILHLMRFSYGSQGSTKLH--KPVRFPLELVLGRelLVSPSTEY 487
Cdd:cd02657 186 -IYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKilRKVKFPFELDLYE--LCTPSGYY 241
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
195-491 |
1.75e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 53.19 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCSPFVQLLQRLrlrNIPkvgfptltafaefvSDFDVPSSNPNVKKKDTTVLE-IGRPFsp 273
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEC---NST--------------EDAELKNMPPDKPHEPQTIIDqLQLIF-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 274 AMFEAVLKSFTpDVPN-----SISGRpRQEDAQEFLSFIMDQMHNELIKLDGQPSSSIgvrsslvssveddewetvgpkn 348
Cdd:cd02668 62 AQLQFGNRSVV-DPSGfvkalGLDTG-QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNI---------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 349 ksaitrtqsflpseLSDIFGGQLRSV-VKARGNKASATVQPFLLLHLDIhpEAVLTIEDALHLFSAPEYLEG---YRAST 424
Cdd:cd02668 118 --------------VQDLFRGEYSYVtQCSKCGRESSLPSKFYELELQL--KGHKTLEECIDEFLKEEQLTGdnqYFCES 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 508725699 425 AGKAgvVTARKSVKIQTLSKIMILHLMRFSYGSQGST--KLHKPVRFPLELVLGrELLVSPSTEYFIYR 491
Cdd:cd02668 182 CNSK--TDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkkKLNASISFPEILDMG-EYLAESDEGSYVYE 247
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
195-490 |
6.47e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 48.26 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLScspfvqllqrlrlrNIPKVGfptltafaefvsdfdvPSSNPNVKKKDTTVLEIGRPFSPA 274
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAL--------------YLPKLD----------------ELLDDLSKELKVLKNVIRKPEPDL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 275 MFEAVLKSFT----PDVPNSISGRP--RQEDAQEFLSFIMDQMHNELIKldgqpssSIGVRSSLvssveddewetVGPKN 348
Cdd:COG5533 51 NQEEALKLFTalwsSKEHKVGWIPPmgSQEDAHELLGKLLDELKLDLVN-------SFTIRIFK-----------TTKDK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 349 KSAITrtqsflpSELSDIFggqlRSVVKARGNKASATVQPFLLLHLDIHPEAV---LTIEDALHLFSAPEYlegyrasta 425
Cdd:COG5533 113 KKTST-------GDWFDII----IELPDQTWVNNLKTLQEFIDNMEELVDDETgvkAKENEELEVQAKQEY--------- 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508725699 426 gkagvvtarkSVKIQTLSKIMILHLMRFSYgSQGSTKLHKPVRFPLELVLGRE--LLVSPSTEY----FIY 490
Cdd:COG5533 173 ----------EVSFVKLPKILTIQLKRFAN-LGGNQKIDTEVDEKFELPVKHDqiLNIVKETYYdlvgFVL 232
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
195-473 |
2.40e-05 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 47.56 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 195 GLINTGNLCFLNATLQALLSCSPFvqllqrlrlRNIPkvgfptltafaefvsdFDVPSSNPnvKKKDTTVLEIGRPF--- 271
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKF---------RKDV----------------YGIPTDHP--RGRDSVALALQRLFynl 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 272 ----SPAMFEAVLKSFTPDVPNSISgrprQEDAQEFLSFIMDqmhnelikldgqpsssigvrsSLVSSVEDDEWEtvgpk 347
Cdd:COG5077 248 qtgeEPVDTTELTRSFGWDSDDSFM----QHDIQEFNRVLQD---------------------NLEKSMRGTVVE----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508725699 348 nksaitrtqsflpSELSDIFGGQLRSVVKA-RGNKASATVQPFLLLHLDIhpEAVLTIEDALHLFSAPEYLEGYRASTAG 426
Cdd:COG5077 298 -------------NALNGIFVGKMKSYIKCvNVNYESARVEDFWDIQLNV--KGMKNLQESFRRYIQVETLDGDNRYNAE 362
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 508725699 427 KAGVVTARKSVKIQTLSKIMILHLMRFSYG--SQGSTKLHKPVRFPLEL 473
Cdd:COG5077 363 KHGLQDAKKGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLEI 411
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
402-471 |
2.52e-03 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 41.02 E-value: 2.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508725699 402 LTIEDALHLFSAPEYL-EGYRASTAGKAGVVTARKSVKIQTLSKIMILHLMRFSYGSQGSTKLHKPVRFPL 471
Cdd:COG5560 675 ITLQDCLNEFSKPEQLgLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
|
|
| |
