|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-392 |
5.62e-83 |
|
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: 273.75 E-value: 5.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 39 NLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLT 118
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 119 DSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGL 198
Cdd:cd02659 74 RSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 199 EDALWNmYVEEEVFDCDNLYHCGTCDRLVKAAKEEKSK--PDV---NLK----DLQSEEEI---DH---PLMIlkaille 263
Cdd:cd02659 154 EESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKklPPVltlQLKrfefDFETMMRIkinDRfefPLEL------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 264 eenNLIPVdqLGQKLLKKIGISWNK-----KYRkqhgplrkflqLHSqIFLLSSDEST---VRLLKNsslqaesdfQRND 335
Cdd:cd02659 226 ---DMEPY--TEKGLAKKEGDSEKKdsesyIYE-----------LHG-VLVHSGDAHGghyYSYIKD---------RDDG 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835683867 336 QqifkmlppespglnnsiscphWFDINDSKVQPIREKDI-EQQFQGKE----------------SAYMLFYRKS 392
Cdd:cd02659 280 K---------------------WYKFNDDVVTPFDPNDAeEECFGGEEtqktydsgprafkrttNAYMLFYERK 332
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
35-486 |
2.74e-33 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 139.62 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 35 REFTNLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglfeDKDKPDAKvRIIPLQLQRLFAQLLLLDqEAAST 114
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQTGE-EPVDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 115 ADLTDSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKN 194
Cdd:COG5077 257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 195 VSGLEDALWNmYVEEEVFDCDNLYHCgtcdrlvkaakeekskPDVNLKDLQseeeidhplmilKAILLEeenNLIPVDQL 274
Cdd:COG5077 337 MKNLQESFRR-YIQVETLDGDNRYNA----------------EKHGLQDAK------------KGVIFE---SLPPVLHL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 275 GQK-----LLKKIGISWNKKYRkqhgplrkflqlhsqiFLLSSDESTvrLLKNSSLQAESD----------FQRNDQ--- 336
Cdd:COG5077 385 QLKrfeydFERDMMVKINDRYE----------------FPLEIDLLP--FLDRDADKSENSdavyvlygvlVHSGDLheg 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 337 QIFKMLPPESPGlnnsiscpHWFDINDSKVQPIREKDIEQQ-----------------FQGKESAYMLFY-RKSQLQ--- 395
Cdd:COG5077 447 HYYALLKPEKDG--------RWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgIKRFMSAYMLVYlRKSMLDdll 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 396 RPPEARAnprygVPCHLLNEMDAANIELQTKRAECDSANNTFELHLH---LGPQYHFFNGALHPVVSQTESVWDLTFDKR 472
Cdd:COG5077 519 NPVAAVD-----IPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYtidSFIHYHGFDYPDFSSELNDSGLAQFVIKRG 593
|
490
....*....|....
gi 1835683867 473 KTLGDLRQSIFQLL 486
Cdd:COG5077 594 AKISDLRNNIAEHL 607
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
42-231 |
1.08e-30 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 123.71 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSlgpeelGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAA-STADLTDS 120
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 121 FGWTSNE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:pfam00443 76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1835683867 196 SGLE--DALWNMYVE---EEVFDCDNLYHCGTCDRLVKAAK 231
Cdd:pfam00443 156 SAELktASLQICFLQfskLEELDDEEKYYCDKCGCKQDAIK 196
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-231 |
1.44e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 102.88 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLG-PEELGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLTDS 120
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNsTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 121 FGwTSNEEmrQHDVQELNRILFSALETSLVGTSGHDL---IYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG 197
Cdd:cd02668 81 LG-LDTGQ--QQDAQEFSKLFLSLLEAKLSKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
|
170 180 190
....*....|....*....|....*....|....
gi 1835683867 198 LEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAK 231
Cdd:cd02668 158 LEECI-DEFLKEEQLTGDNQYFCESCNSKTDATR 190
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
42-390 |
2.17e-20 |
|
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: 92.16 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHftpefrealfslgpeelglfedkdkpdakvriiplqlqrlfaqlllldqeaastadltdsf 121
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 122 gwtsneeMRQHDVQELNRILFSALETSLVG--------TSGHDLIYRLYHGTIVNQIVCKECK--NVSERQEDFLDLTVA 191
Cdd:cd02257 20 -------SEQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGheSVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 192 VKNVSG--LEDALwNMYVEEEVFDCDNLYHCGtCDRLVKAAKEEKSK--PDV---NLKdLQSEEEIDHPLMILKAILLEE 264
Cdd:cd02257 93 VKGLPQvsLEDCL-EKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKklPPVliiHLK-RFSFNEDGTKEKLNTKVSFPL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 265 ENNLIPVDQLGQKLLKKIGISwnKKYRkqhgplrkflqLHSQIF-LLSSDES---TVRLLKNSSLQaesdfqrndqqifk 340
Cdd:cd02257 170 ELDLSPYLSEGEKDSDSDNGS--YKYE-----------LVAVVVhSGTSADSghyVAYVKDPSDGK-------------- 222
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1835683867 341 mlppespglnnsiscphWFDINDSKVQPIREKDIEQQFQGKESAYMLFYR 390
Cdd:cd02257 223 -----------------WYKFNDDKVTEVSEEEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
41-389 |
1.10e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 88.10 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 41 SGIRNQGGTCYLNSLLQTLHFTPEFREALFSLGpeelglfEDKDKPDAKVRIIpLQLQRLFAQLLLLDQEAASTADLTDS 120
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSRE-------HSKDCCNEGFCMM-CALEAHVERALASSGPGSAPRIFSSN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 121 FGWTSNEEM--RQHDVQELNRILFSALETS----LVGTSGHD-------LIYRLYHGTIVNQIVCKECKNVSERQEDFLD 187
Cdd:cd02661 74 LKQISKHFRigRQEDAHEFLRYLLDAMQKAcldrFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 188 LTVAVKNVSGLEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKE---EKSKP--DVNLKDLQ--SEEEIDhplmilKAI 260
Cdd:cd02661 154 LSLDIKGADSLEDAL-EQFTKPEQLDGENKYKCERCKKKVKASKQltiHRAPNvlTIHLKRFSnfRGGKIN------KQI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 261 LLEEENNLIPVdqlgqkllkkigiswnkKYRKQHGPLRKFLQ---LHSQiFLLSSDE--STVRllknsslqaesdfqrnd 335
Cdd:cd02661 227 SFPETLDLSPY-----------------MSQPNDGPLKYKLYavlVHSG-FSPHSGHyyCYVK----------------- 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1835683867 336 qqifkmlppESPGLnnsiscphWFDINDSKVQPIREKDIEQQfqgkeSAYMLFY 389
Cdd:cd02661 272 ---------SSNGK--------WYNMDDSKVSPVSIETVLSQ-----KAYILFY 303
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-390 |
5.01e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 86.78 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGlfedkdkpdaKVRIIPLQLQRLFAQLLLLDQEAASTAD--LTD 119
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLG----------DSQSVMKKLQLLQAHLMHTQRRAEAPPDyfLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 120 SF--GWTSNeemRQHDVQELNRILFSALetslvgtsgHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVsg 197
Cdd:cd02664 71 SRppWFTPG---SQQDCSEYLRYLLDRL---------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSV-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 198 lEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKEEK--SKPD---VNLKDLQ------SEEEIDHPLMILKAILLEEEN 266
Cdd:cd02664 137 -QDLL-NYFLSPEKLTGDNQYYCEKCASLQDAEKEMKvtGAPEyliLTLLRFSydqkthVREKIMDNVSINEVLSLPVRV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 267 NLIPVDQLGQKLLKKIGISWNKKYRKQHGPLRKFLqLHSQIfllSSDESTVRLLKNSSLQAESDFQrndqqifkMLPPES 346
Cdd:cd02664 215 ESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVV-VHSGY---SSESGHYFTYARDQTDADSTGQ--------ECPEPK 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1835683867 347 PGLNNSISCPhWFDINDSKVQPIREKDIEQ--QFQGKESAYMLFYR 390
Cdd:cd02664 283 DAEENDESKN-WYLFNDSRVTFSSFESVQNvtSRFPKDTPYILFYE 327
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-242 |
5.49e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 71.19 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFtpefrEALFSLGPEelgLFEDKDKPDAKVRIIPLQLqrlFAQLLLLDQEAASTADLTDS- 120
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLTCLKD---LFESISEQKKRTGVISPKK---FITRLKRENELFDNYMHQDAh 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 121 --FGWTSN---EEMRQHDVQELNRILFSALETSlvgTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:cd02663 70 efLNFLLNeiaEILDAERKAEKANRKLNNNNNA---EPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835683867 196 SGLEDALWNMYvEEEVFDCDNLYHCGTCDRLVKAAKEEKSK--PDV---NLK 242
Cdd:cd02663 147 TSITSCLRQFS-ATETLCGRNKFYCDECCSLQEAEKRMKIKklPKIlalHLK 197
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
31-223 |
3.04e-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: 66.07 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 31 PPAPREFTNL---SGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeeLGLFEDKDkpdakvriiplQLQRLFAQLL-L 106
Cdd:cd02671 12 ATSCEKRENLlpfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVE-----------QLQSSFLLNPeK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 107 LDQEAASTA---------DLTDSFgwtsnEEMRQHDVQE-LNRILFSAletslvgtsgHDLIYRLYHGTIVNQIVCKECK 176
Cdd:cd02671 77 YNDELANQAprrllnalrEVNPMY-----EGYLQHDAQEvLQCILGNI----------QELVEKDFQGQLVLRTRCLECE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835683867 177 NVSERQEDFLDLTVAV----------------KNVSGLEDALWNM--YVEEEVFDCDNLYHCGTC 223
Cdd:cd02671 142 TFTERREDFQDISVPVqeselskseesseispDPKTEMKTLKWAIsqFASVERIVGEDKYFCENC 206
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-229 |
3.71e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 65.10 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREaLFSLGPEELglfedkdkpdakvriiplqlqrlFAQLLLLDQEaastadltdsF 121
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSETPKEL-----------------------FSQVCRKAPQ----------F 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 122 gwtsnEEMRQHDVQELNRILFSALETslvgtsghdLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAV----KNVSG 197
Cdd:cd02667 47 -----KGYQQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRsdeiKSECS 112
|
170 180 190
....*....|....*....|....*....|..
gi 1835683867 198 LEDALWNMYVEEEVFDcDNLYHCGTCDRLVKA 229
Cdd:cd02667 113 IESCLKQFTEVEILEG-NNKFACENCTKAKKQ 143
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-231 |
4.17e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 62.78 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGLFEDKDKpdakvrIIPLQLQRLFAQLllldqeaaSTADLTDSF 121
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNS------CLSCAMDEIFQEF--------YYSGDRSPY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 122 G--------WTSNEEM---RQHDVQELNRILFSALETSLVGTSGHD--------LIYRLYHGTIVNQIVCKECKNVSERQ 182
Cdd:cd02660 68 GpinllylsWKHSRNLagySQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcncIIHQTFSGSLQSSVTCQRCGGVSTTV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835683867 183 EDFLDLTVAVKNVSG---------------LEDALWNMYVEEEVfdCDNLYHCGTCDRLVKAAK 231
Cdd:cd02660 148 DPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL--GDFAYKCSGCGSTQEATK 209
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-239 |
5.30e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 58.87 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeELGLFEDKDKPDAKVRIiplQLQRLfAQLLLLDQEAASTADLTDSF 121
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL---ENKFPSDVVDPANDLNC---QLIKL-ADGLLSGRYSKPASLKSEND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 122 GWT--------------SNEE---MRQHDVQELNRILFSALETSLVGTSGHDLIyRLYHGTIVNQIVCKECKNV--SERQ 182
Cdd:cd02658 74 PYQvgikpsmfkaligkGHPEfstMRQQDALEFLLHLIDKLDRESFKNLGLNPN-DLFKFMIEDRLECLSCKKVkyTSEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835683867 183 EDFLDLTV-------------AVKNVSgLEDALwNMYVEEEVFDcdnlYHCGTCDRLVKAAKEE--KSKPDV 239
Cdd:cd02658 153 SEILSLPVpkdeatekeegelVYEPVP-LEDCL-KAYFAPETIE----DFCSTCKEKTTATKTTgfKTFPDY 218
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-390 |
9.94e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 57.30 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLhftpefrealfslgpeelglfedkdkpdakvriiplqlqrlfaqlllldqeaastadltdsf 121
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 122 gwtSNeemRQHDVQELNRILFSALetslvgtsgHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG---- 197
Cdd:cd02674 19 ---SA---DQQDAQEFLLFLLDGL---------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGdapk 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 198 --LEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKEEK-SK-PDVnlkdlqseeeidhpLMIlkailleeennlipvdQ 273
Cdd:cd02674 84 vtLEDCL-RLFTKEETLDGDNAWKCPKCKKKRKATKKLTiSRlPKV--------------LII----------------H 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 274 LgqKLLKKIGISWNKKYRKQHGPLRKFLqlhsqifllssdestvrllknsslqaesdfqrnDQQIFKMLPPESPGLNN-- 351
Cdd:cd02674 133 L--KRFSFSRGSTRKLTTPVTFPLNDLD---------------------------------LTPYVDTRSFTGPFKYDly 177
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835683867 352 -------SISCPH------------WFDINDSKVQPIREKDIEqqfqgKESAYMLFYR 390
Cdd:cd02674 178 avvnhygSLNGGHytaycknnetndWYKFDDSRVTKVSESSVV-----SSSAYILFYE 230
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
41-190 |
2.07e-07 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 54.20 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 41 SGIRNQGGTCYLNSLLQTLHFTPEFRE-ALFSLGPE---------ELG-LF--EDKDKPdakvriIPLQ---LQRLFAQL 104
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATEclkehcllcELGfLFdmLEKAKG------KNCQasnFLRALSSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 105 llldqEAASTADLTDSFGWTSNEEMRQHDVQELNRILFS-----ALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVS 179
Cdd:pfam13423 75 -----PEASALGLLDEDRETNSAISLSSLIQSFNRFLLDqlsseENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHES 149
|
170
....*....|...
gi 1835683867 180 ERQEDF--LDLTV 190
Cdd:pfam13423 150 VRESSThvLDLIY 162
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
42-391 |
4.04e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 52.88 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHF-TPEFREALFSLgPEELGLFED---KDKPDAKVRiiplQLQRLFAQLLLLDQEaastadl 117
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALyLPKLDELLDDL-SKELKVLKNvirKPEPDLNQE----EALKLFTALWSSKEH------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 118 tdSFGWTSNEEmRQHDVQELNRILFSALETSLVGTsghdlIYRLYHGTIVNqivckeckNVSERQEDFLDLTVAVKNVSG 197
Cdd:COG5533 69 --KVGWIPPMG-SQEDAHELLGKLLDELKLDLVNS-----FTIRIFKTTKD--------KKKTSTGDWFDIIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 198 LEDalwnmyveEEVFDC--DNLYHCGTCDRLVKAAKEEKSKPDVNLKDLQSEEEIDHPLMI-LKAILLEEENNLIPvDQL 274
Cdd:COG5533 133 VNN--------LKTLQEfiDNMEELVDDETGVKAKENEELEVQAKQEYEVSFVKLPKILTIqLKRFANLGGNQKID-TEV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 275 GQKLLKKIGISWNKKYRKQHgplrkFLQLHSQIFLLSSDESTvrllknsslQAESDFQRNdqqifkmlppespglnnsis 354
Cdd:COG5533 204 DEKFELPVKHDQILNIVKET-----YYDLVGFVLHQGSLEGG---------HYIAYVKKG-------------------- 249
|
330 340 350
....*....|....*....|....*....|....*..
gi 1835683867 355 cPHWFDINDSKVQPIREKDIEQQFQgkESAYMLFYRK 391
Cdd:COG5533 250 -GKWEKANDSDVTPVSEEEAINEKA--KNAYLYFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-202 |
1.18e-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 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: 51.56 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELG--------------LFEDKDK-PDAKVRIIPLQ-LQRLFAQll 105
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGanqssdnltnalrdLFDTMDKkQEPVPPIEFLQlLRMAFPQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 106 lldqeaastadltdsFGWTSNEEM-RQHDVQELNRILFSALETSLVGTSGH-DLIYRLYHGTIVNQIVCKECKNVSE--- 180
Cdd:cd02657 79 ---------------FAEKQNQGGyAQQDAEECWSQLLSVLSQKLPGAGSKgSFIDQLFGIELETKMKCTESPDEEEvst 143
|
170 180
....*....|....*....|...
gi 1835683867 181 RQEDFLDLTVAVK-NVSGLEDAL 202
Cdd:cd02657 144 ESEYKLQCHISITtEVNYLQDGL 166
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
40-190 |
1.47e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 46.03 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 40 LSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELglfEDKDKPDAkvriIPLQLQRLFAQLL--LLDQEAASTADL 117
Cdd:COG5560 265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEES---INEENPLG----MHGSVASAYADLIkqLYDGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 118 TDSFGWTSNEEM----RQHDVQE------------LNRILFSALETSLVGTSGHD--------------------LIYRL 161
Cdd:COG5560 338 GFKKTIGSFNEEfsgyDQQDSQEfiaflldglhedLNRIIKKPYTSKPDLSPGDDvvvkkkakecwwehlkrndsIITDL 417
|
170 180
....*....|....*....|....*....
gi 1835683867 162 YHGTIVNQIVCKECKNVSERQEDFLDLTV 190
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-190 |
1.62e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 45.17 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGLFEDKDK----PDAKVRIIPL--------QLQRLFAQLLLLDQ 109
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTerriGGREVSRSELqrsnqfvyELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835683867 110 EAAS-TADLTdsfgwtsNEEMRQHDVQE-LNRILFSaLETSLVGTSGH-------------DLIYRLYHGTIVNQIVcKE 174
Cdd:cd02666 83 RSVTpSKELA-------YLALRQQDVTEcIDNVLFQ-LEVALEPISNAfagpdteddkeqsDLIKRLFSGKTKQQLV-PE 153
|
170 180
....*....|....*....|
gi 1835683867 175 CKN----VSERQEDFLDLTV 190
Cdd:cd02666 154 SMGnqpsVRTKTERFLSLLV 173
|
|
| |
