|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-419 |
0e+00 |
|
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: 570.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL--KNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668 79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668 159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668 239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313
|
330
....*....|.
gi 76257392 409 CSRNAYMLVYR 419
Cdd:cd02668 314 SSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
88-419 |
3.54e-84 |
|
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: 262.96 E-value: 3.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdymlgdgiqEEKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELN 242
Cdd:cd02659 70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 243 IQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILD 322
Cdd:cd02659 147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 323 MEPYVEH------------KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659 227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305
|
330 340 350
....*....|....*....|....*....|..
gi 76257392 388 EDLAEPSKSQTRKPKCGkgthcsrNAYMLVYR 419
Cdd:cd02659 306 ETQKTYDSGPRAFKRTT-------NAYMLFYE 330
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
89-418 |
2.29e-63 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 208.07 E-value: 2.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMLGDGIQeekdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443 72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKlqlgie 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET------ 298
|
330 340 350
....*....|....*....|....*....|.
gi 76257392 388 edlaepsksqtrkpkcgkgTHCSRNAYMLVY 418
Cdd:pfam00443 299 -------------------AVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
90-419 |
5.68e-60 |
|
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: 197.32 E-value: 5.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdymlgdgiqeekdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257 1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQ 244
Cdd:cd02257 21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 245 GHKQ----LTDCISEFLKEEKLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEI 320
Cdd:cd02257 93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 321 LDMEPYVEHKG-------GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgiEEDLAEP 393
Cdd:cd02257 171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEF 242
|
330 340
....*....|....*....|....*.
gi 76257392 394 SKSqtrkpkcgkgthcSRNAYMLVYR 419
Cdd:cd02257 243 GSL-------------SSSAYILFYE 255
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
72-458 |
8.09e-49 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 180.45 E-value: 8.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdymlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077 179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077 244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077 320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDI---EKMEGK 380
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQE----KPNTTVQVPAFLQELVDRDNSKFEEWCIEMAE 456
Cdd:COG5077 478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550
|
..
gi 76257392 457 MR 458
Cdd:COG5077 551 IH 552
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
3.11e-45 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 160.13 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVwflnleLRQALYLcpstcSDYMLGDGIQEEKDYE-PQTICEHLQYLFALLQNSnRRYIDPSGF 168
Cdd:cd02661 3 GLQNLGNTCFLNSVLQC------LTHTPPL-----ANYLLSREHSKDCCNEgFCMMCALEAHVERALASS-GPGSAPRIF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 169 VKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQQQFCGEYAYVTVCNQCGRESKLLSK 235
Cdd:cd02661 71 SSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 236 FYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYI 315
Cdd:cd02661 151 FLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 76257392 316 GFSEILDMEPYV-EHKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPqSGEWYKFND 371
Cdd:cd02661 227 SFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-419 |
1.61e-44 |
|
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: 155.91 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 178 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674 21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 252 CISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFS-EILDMEPYV--E 328
Cdd:cd02674 89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 329 HKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 408
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219
|
250
....*....|.
gi 76257392 409 CSRNAYMLVYR 419
Cdd:cd02674 220 VSSSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
1.00e-39 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 146.10 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcsdymLGDGIQEEKDyePQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQV-----------LSLNLPRLGD--SQSVMKKLQLLQAHLMHTQRRAEAPpDYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIqg 245
Cdd:cd02664 68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 246 hKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEP 325
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 326 YVEHKGGSYV--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQSGE-------------------- 365
Cdd:cd02664 213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendeskn 292
|
....*.
gi 76257392 366 WYKFND 371
Cdd:cd02664 293 WYLFND 298
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-371 |
4.23e-38 |
|
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: 141.74 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYMLGDGIQEEKDY--EPQTICEHLQYLFA-LLQNSNRRyidPS 166
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLR-----------NYFLSDRHSCTCLScsPNSCLSCAMDEIFQeFYYSGDRS---PY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 167 GFVKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRES 230
Cdd:cd02660 68 GPINLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 231 KLLSKFYELELNIQGHKQ---------------LTDCISEFLKEEKLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQ 295
Cdd:cd02660 145 TTVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 296 LMRFVFDrQTGHKKKLNTYIGFSEILDMEPYV----------EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDpQSGE 365
Cdd:cd02660 224 LKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQ 300
|
....*.
gi 76257392 366 WYKFND 371
Cdd:cd02660 301 WFKFDD 306
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-379 |
9.58e-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 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: 134.77 E-value: 9.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYMlgdGIQEEKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 170 KALGL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQQQFCGEYAYVTVC-NQCGRESKLLSKF 236
Cdd:cd02657 70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVSTESE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 237 YELELNIqGHKQLTDCISEFLKEeKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIG 316
Cdd:cd02657 147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76257392 317 FSEILDMEPYVEHKGgsyVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFND--------EDIEKMEG 379
Cdd:cd02657 225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-418 |
2.76e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 133.20 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdymlgdgiqeekdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:cd02663 49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663 129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 309 KKLNTYIGFSEIL------DMEPYVEHKggsyvYELSAVLIHRGVSAYSGHYIAHVKdpQSGEWYKFNDEDIEKMEGKKL 382
Cdd:cd02663 209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV 281
|
330 340 350
....*....|....*....|....*....|....*.
gi 76257392 383 qlgieEDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 418
Cdd:cd02663 282 -----EEFFGDSPNQA-------------TAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-401 |
1.74e-30 |
|
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: 120.77 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 78 PNCERRKK-NSFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSD--YMLGDGIQEEkdyEPQTICEHLQYLFal 154
Cdd:cd02671 13 TSCEKRENlLPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGlkHLVSLISSVE---QLQSSFLLNPEKY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 155 lqNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCG-- 227
Cdd:cd02671 78 --NDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECEtf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 228 --------------RESKLLSKFYELELNIQGH---KQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPC 290
Cdd:cd02671 144 terredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 291 TLNLQLMRF----VFDRQTGHKKKLNTYIGFSEILDMEPYVEhKGGSYVYELSAVLIHRGVSAYSGHYIAHVKdpqsgeW 366
Cdd:cd02671 224 VITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR------W 296
|
330 340 350
....*....|....*....|....*....|....*
gi 76257392 367 YKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 401
Cdd:cd02671 297 LLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-372 |
9.13e-30 |
|
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: 118.19 E-value: 9.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWF-------LNLELRQALYLCPS------TCSDYMLGDGIQEEKDYEPQTICEHlqylfallQ 156
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwRYDDLENKFPSDVVdpandlNCQLIKLADGLLSGRYSKPASLKSE--------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 157 NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQQQFCgeyayvtvCNQCG 227
Cdd:cd02658 73 DPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 228 RESKLLSKFYELELNIQGHKQ--------------LTDCISEFLKEEKLEgdnrYFCENCQSKQNATRKIRLLSLPCTLN 293
Cdd:cd02658 145 KVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 294 LQLMRFVFDrQTGHKKKLNTYIGFSEILDMEPYvehkggsyvyELSAVLIHRGVSAYSGHYIAHVK--DPQSGEWYKFND 371
Cdd:cd02658 221 INMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289
|
.
gi 76257392 372 E 372
Cdd:cd02658 290 E 290
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-419 |
1.48e-29 |
|
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: 117.10 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTflqvwflnleLRQALYLCPstcsdyMLGDGIQEEkdyePQTicehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667 1 GLSNLGNTCFFNA----------VMQNLSQTP------ALRELLSET----PKE-------LFSQVCRKAPQFKG----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELEL----NIQG 245
Cdd:cd02667 49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 246 HKQLTDCISEFLKEEKLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSEILDMEP 325
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 326 Y------VEHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGEWYKFNDEDIEkme 378
Cdd:cd02667 186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR--- 261
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 76257392 379 gkklqlgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 419
Cdd:cd02667 262 --------EVSLEEVLKSE---------------AYLLFYE 279
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-377 |
2.42e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 91.02 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgdgIQE-EKDYEPQTICEHLqYLFALLQNSNRRYIDPSGf 168
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVL----KNViRKPEPDLNQEEAL-KLFTALWSSKEHKVGWIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 169 vkalglDTGQQQDAQEFSKLFMSLLEDTLSKQ--------KNPDVRNIVQQQFcgeyaYVTVCNQCGRESKLLSKFyele 240
Cdd:COG5533 75 ------PMGSQEDAHELLGKLLDELKLDLVNSftirifktTKDKKKTSTGDWF-----DIIIELPDQTWVNNLKTL---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 241 lniqghKQLTDCISEFLKEEKL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNTYIGfs 318
Cdd:COG5533 140 ------QEFIDNMEELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76257392 319 EILDMEPYVEHKGG---SYVYELSAVLIHRGvSAYSGHYIAHVKdpQSGEWYKFNDEDIEKM 377
Cdd:COG5533 205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
90-376 |
9.25e-20 |
|
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: 88.19 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdymlgdgiqeekdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqqqFCGEYAYVTVCNQCGRESKL-LSKFYELELNIQGHKQ 248
Cdd:cd02662 33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 249 -----LTDCISEFLKEEKLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEILDm 323
Cdd:cd02662 93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76257392 324 epyvehkggSYVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGE--------------WYKFNDEDIEK 376
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
89-371 |
5.58e-19 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 87.33 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpstcsdymlgdgIQEEKDYEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH------------LATECLKEHCLLCE-LGFLFDMLEKAKGKNCQASNF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:pfam13423 68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 229 ESKLLSKFYELELN------IQGHKQLTDCISEFLKEE-KLEGDNRYFCENCQSKQNATRKIRLLSLPC--TLNLQLMRF 299
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76257392 300 VFDRQTGHKKKLNTYIGfseiLDMEPYVEHKGGSYVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGEWYKFND 371
Cdd:pfam13423 228 EWRQLWKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
220-376 |
1.06e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.56 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 220 VTVCNQCGRESKLLSKFYE-----LELNIQGHKQ---LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCT 291
Cdd:COG5560 640 DAVVISCEWEEKRYLSLFSydplwTIREIGAAERtitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 292 LNLQLMRFVFDRQTghKKKLNTYIGFS-EILDMEPYVEHKGGSYV-YELSAVLIHRGVSAySGHYIAHVKDPQSGEWYKF 369
Cdd:COG5560 720 LIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLF 796
|
....*..
gi 76257392 370 NDEDIEK 376
Cdd:COG5560 797 DDSRITE 803
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-375 |
4.44e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 89 VGLTNLGATCYVNTFLQVWFLNLELRQA--------LYLCPSTCSDYMLGDGIQEEKDYE-PQTICEHLQYLFALLQNSN 159
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnfdeskAELASDYPTERRIGGREVSRSELQrSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 160 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQQQFCGEY----AYVTVCNQ 225
Cdd:cd02666 82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 226 CGRESK---LLSKFYEL-----ELNIQGHKQ-LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKI---------RLLS 287
Cdd:cd02666 159 PSVRTKterFLSLLVDVgkkgrEIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 288 LPCTLNLQLMRFVFDRQTGHKKKLNTYIGfseilDMEPYVEHKGgSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWY 367
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAELKH-----EIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVWR 311
|
....*...
gi 76257392 368 KFNDEDIE 375
Cdd:cd02666 312 KYNDETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-383 |
6.26e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 71.05 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnivqQQFCGEYAYVTVcnqcgRESKLLSK---FYELELNIQ 244
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGV-----LEGKPFCNcetFGQYPLQVN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 245 GHKQLTDCISEFLKEEKLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSEILDME 324
Cdd:cd02665 91 GYGNLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 76257392 325 PYvehkggsyvyELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQ 383
Cdd:cd02665 163 PY----------ELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVE 210
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-378 |
2.13e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 65.80 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 86 NSFVGLTNLGATCYVNTFLQvwflnlelrqALYLCPSTCSDYMLGDGIQEEKDYEPQTIcEHLQYLFALLQNSN--RRYI 163
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQ----------ALSHVKPIRNFFLLYENYENIKDRKSELV-KRLSELIRKIWNPRnfKGHV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 164 DPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNIVQQQFCGEY-----AYVTVCNQCGRESKLL 233
Cdd:cd02669 186 SPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKVqietqKIKPHAEEEGSKDKFF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 234 ----------SKFYELELNIQG-----HKQLTDCISEFLKEEKLegdNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMR 298
Cdd:cd02669 266 kdsrvkktsvSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 299 FvfDRQTGHKKKLNTYIGFS-EILDMEPYVE---HKGGSYV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDED 373
Cdd:cd02669 343 F--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLN 420
|
....*
gi 76257392 374 IEKME 378
Cdd:cd02669 421 VKEVL 425
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-374 |
1.17e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 61.78 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQQQFCGEYAYVT----VCNQCGRESKLLSKFYELELNIQG 245
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 246 HK--QLTDCISEFLKEEKLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfseildM 323
Cdd:cd02673 107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 76257392 324 EPYvEHKGGSYvyELSAVLIHRGVSAYSGHYIAHVKDPQSG-EWYKFNDEDI 374
Cdd:cd02673 175 KKY-CGTDAKY--SLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
75-371 |
2.05e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 49.05 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdymlgdgIQEEKDYEPQTICEhLQYLFAL 154
Cdd:cd02672 2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFST 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 155 LqnsnrryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqqqfcgeyayvtvcNQCGRESKLLS 234
Cdd:cd02672 68 L--------------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 235 KFYELELNIQGHKQLTD-----CISEFLKEEKlegDNRYFCENCQSKQNATRKIRLLSLPCTLNLQL---MRFV------ 300
Cdd:cd02672 100 LLYTLSLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefdd 176
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76257392 301 FDRQTGHKKKLNTYIGFSEILDMEPYVEHKG-GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQS----GEWYKFND 371
Cdd:cd02672 177 INVVLPSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
90-243 |
1.36e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 47.96 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYMLGDGIQEEKDYE-PQTICEHLQYLFA-LLQ---NSNRRYID 164
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELR-----------DYFLSDEYEESINEEnPLGMHGSVASAYAdLIKqlyDGNLHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257392 165 PSGFVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSK--QK----NPDV-----------------------RNIVQ 210
Cdd:COG5560 336 PSGFKKTIGsfneeFSGYDQQDSQEFIAFLLDGLHEDLNRiiKKpytsKPDLspgddvvvkkkakecwwehlkrnDSIIT 415
|
170 180 190
....*....|....*....|....*....|...
gi 76257392 211 QQFCGEYAYVTVCNQCGRESKLLSKFYELELNI 243
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| |
