|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
166-566 |
4.53e-150 |
|
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: 457.49 E-value: 4.53e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 166 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEDSEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 243
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 244 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 323
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 324 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMSFPEELDMSTFIDI 403
Cdd:cd02659 154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 404 EDEKSPQTESCTDSGaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfqlgepn 483
Cdd:cd02659 234 GLAKKEGDSEKKDSE----------------------------------------------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 484 SLMYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLI 560
Cdd:cd02659 249 SYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLF 328
|
....*.
gi 1276346074 561 YRLKDP 566
Cdd:cd02659 329 YERKSP 334
|
|
| USP47_C |
pfam19718 |
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ... |
1125-1364 |
5.21e-101 |
|
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of Ubiquitin carboxyl-terminal hydrolase 47 (USP47), a ubiquitin-specific protease involved in deubiquitinating of monoubiquitinated DNA polymerase beta (Polbeta), being required for its stability and, therefore, plays a role in DNA base excision repair (BER). The C-terminal domains in USPs mediate protein- protein interactions.
Pssm-ID: 466158 Cd Length: 240 Bit Score: 322.09 E-value: 5.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 1125 RVKVCQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLDLSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1203
Cdd:pfam19718 1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 1204 SSNWEVFLEVLDGVEKMKSMSQLAILTRRWRPAEMKLDPFQELVLESNSVDELREKLSEISGIPLEDIEFAKGRGTFPCD 1283
Cdd:pfam19718 80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 1284 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDRTEEVMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1363
Cdd:pfam19718 160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239
|
.
gi 1276346074 1364 Y 1364
Cdd:pfam19718 240 Y 240
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
168-561 |
9.29e-76 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 253.90 E-value: 9.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEDSEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 244
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 245 SE--AWQQHDVQELCRVMFDALEQKWKQ---TEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQA 319
Cdd:pfam00443 81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 320 FASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMSFPEELDMST 399
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 400 FIDIEDEKspqtesctdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfql 479
Cdd:pfam00443 239 YLAEELKP------------------------------------------------------------------------ 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 480 GEPNSLMYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYML 559
Cdd:pfam00443 247 KTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYIL 308
|
..
gi 1276346074 560 IY 561
Cdd:pfam00443 309 FY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
162-612 |
3.45e-74 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 269.43 E-value: 3.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 162 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEDseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 241
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 242 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygSSQAFA 321
Cdd:COG5077 265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL------NVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 322 SVEEALHAFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMSFPEELDMSTFI 401
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 402 DiEDEKSPQTESCTdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfqlge 481
Cdd:COG5077 418 D-RDADKSENSDAV------------------------------------------------------------------ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 482 pnslmYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYM 558
Cdd:COG5077 431 -----YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYM 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1276346074 559 LIYRLKDPTRN-AKFLEVDEYPEHIKNLVQKERELEEQEKRQREIERNTCKIKLF 612
Cdd:COG5077 506 LVYLRKSMLDDlLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-562 |
2.49e-57 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 201.50 E-value: 2.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEF-EDSEEDPV--------TSIPYQLQRLFVLLQTSKKRAIETTDVTRS 239
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNStEDAELKNMppdkphepQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 240 FGWDSSeawQQHDVQELCRVMFDALEQKWKQTEQADLIN---ELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIrpygs 316
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNivqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 317 sQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMSFPEELD 396
Cdd:cd02668 153 -KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 397 MSTFIDIEDEkspqtesctdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiq 476
Cdd:cd02668 232 MGEYLAESDE---------------------------------------------------------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 477 fqlgepNSLMYELFSVMVHSG-SAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIK--KTHGGSSGSRGYYSSAFASS 553
Cdd:cd02668 242 ------GSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKlgNSEDPAKPRKSEIKKGTHSS 315
|
....*....
gi 1276346074 554 TNAYMLIYR 562
Cdd:cd02668 316 RTAYMLVYK 324
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
169-562 |
2.14e-56 |
|
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: 196.16 E-value: 2.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMtpefrnalykwefedseedpvtsipyqlqrlfvllqtskkraiettdvtrsfgwdsseaw 248
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 249 QQHDVQELCRVMFDALEQKWKQ--------TEQADLINELYQGKLKDYVRCLECGYEG--WRIDTYLDIPLVIRPYGSSq 318
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESvsTEPELFLSLPLPVKGLPQV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 319 afaSVEEALHAFIQPEILDGPNQYFCErCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYtTMHRIKLNDRMSFPEELDMS 398
Cdd:cd02257 100 ---SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 399 TFIDIEDEKSPqtesctdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfq 478
Cdd:cd02257 175 PYLSEGEKDSD--------------------------------------------------------------------- 185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 479 lGEPNSLMYELFSVMVHSGSAA-GGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKthggssgsrgyyssAFASSTNAY 557
Cdd:cd02257 186 -SDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE--------------FGSLSSSAY 250
|
....*
gi 1276346074 558 MLIYR 562
Cdd:cd02257 251 ILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-561 |
2.82e-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: 165.91 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNAL----YKWEFEDSEEDPVTSIPYQLQRlfVLLQTSKKRAI-----ETTDVTRS 239
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLlsreHSKDCCNEGFCMMCALEAHVER--ALASSGPGSAPrifssNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 240 FGWDSseawqQHDVQELCRVMFDALEQ----KWKQTEQAD-------LINELYQGKLKDYVRCLECGYEGWRIDTYLDIP 308
Cdd:cd02661 81 FRIGR-----QEDAHEFLRYLLDAMQKacldRFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 309 LVIRpyGSSqafaSVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttMHriKLNDR 388
Cdd:cd02661 156 LDIK--GAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 389 MSFPEELDMSTFidiedekspqtesctdsgaenegschsdqMSNdfSTDdavdegiclesssgsekiskpglekvemaet 468
Cdd:cd02661 226 ISFPETLDLSPY-----------------------------MSQ--PND------------------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 469 dqrkdpiqfqlgepNSLMYELFSVMVHSG-SAAGGHYYACIKSfSDDQWYSFNDQHVSRITQEDIkkthggssgsrgyys 547
Cdd:cd02661 244 --------------GPLKYKLYAVLVHSGfSPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETV--------------- 293
|
410
....*....|....
gi 1276346074 548 safaSSTNAYMLIY 561
Cdd:cd02661 294 ----LSQKAYILFY 303
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-562 |
7.72e-43 |
|
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: 159.96 E-value: 7.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKweFEDSEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDvtrSFGWDSSEAW 248
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD---YFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 249 ----QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygssqAFASVE 324
Cdd:cd02664 76 ftpgSQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---------SFPSVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 325 EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMSFPEELDMSTFIDIE 404
Cdd:cd02664 138 DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 405 DEKSPQTESCTDSGaENEGSCHSdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfqlgepnS 484
Cdd:cd02664 218 SSESPLEKKEEESG-DDGELVTR--------------------------------------------------------Q 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 485 LMYELFSVMVHSG-SAAGGHYYACIKSFSD--------------------DQWYSFNDQHVSRITQEDIKKThggssgsr 543
Cdd:cd02664 241 VHYRLYAVVVHSGySSESGHYFTYARDQTDadstgqecpepkdaeendesKNWYLFNDSRVTFSSFESVQNV-------- 312
|
410
....*....|....*....
gi 1276346074 544 gyysSAFASSTNAYMLIYR 562
Cdd:cd02664 313 ----TSRFPKDTPYILFYE 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
249-562 |
4.79e-32 |
|
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: 125.48 E-value: 4.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 249 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASVEEALH 328
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS---------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 329 AFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMhrIKLNDRMSFP-EELDMSTFIDIEDEK 407
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVDTRSFT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 408 SPQTesctdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfqlgepnslmY 487
Cdd:cd02674 170 GPFK---------------------------------------------------------------------------Y 174
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276346074 488 ELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKkthggssgsrgyyssafasSTNAYMLIYR 562
Cdd:cd02674 175 DLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV-------------------SSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-561 |
2.47e-27 |
|
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: 114.39 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALY--KWEFEDSEEDPVTSIPYQLQRLFVLLQTSKKRaiettdvtRSFG----- 241
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLsdRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--------SPYGpinll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 242 ---WDSS---EAWQQHDVQELCRVMFDALEQKWK--QTEQAD------LINELYQGKLKDYVRCLECGYEGWRIDTYLDI 307
Cdd:cd02660 74 ylsWKHSrnlAGYSQQDAHEFFQFLLDQLHTHYGgdKNEANDeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 308 PLVIRPYGSS---------QAFASVEEALHAFIQPEILdGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYT 378
Cdd:cd02660 154 SLDIPNKSTPswalgesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 379 TMHRiKLNDRMSFPEELDMSTFIDiedekspqtesctdsgaenegschsdqmsndfstddavdegicleSSSGSEKISKP 458
Cdd:cd02660 233 KTSR-KIDTYVQFPLELNMTPYTS---------------------------------------------SSIGDTQDSNS 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 459 glekvemaetdqrkdpiqfqlgEPNSLMYELFSVMVHSGSAAGGHYYACIKsFSDDQWYSFNDQHVSRITQEDIKKthgg 538
Cdd:cd02660 267 ----------------------LDPDYTYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRVSEEEVLK---- 319
|
410 420
....*....|....*....|...
gi 1276346074 539 ssgsrgyyssafassTNAYMLIY 561
Cdd:cd02660 320 ---------------SQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-562 |
1.07e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 105.55 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALykwefedsEEDPVTsipyqlqrlfvLLQTSKKRAIETTDvtrsfgwdsseaW 248
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL--------SETPKE-----------LFSQVCRKAPQFKG------------Y 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 249 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAfaSVEEALH 328
Cdd:cd02667 50 QQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSEC--SIESCLK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 329 AFIQPEILDGPNQYFCERCKKkcdARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMSFPEELDMSTFIDiedeks 408
Cdd:cd02667 119 QFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAPFCD------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 409 PQTESCTDSgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfqlgepNSLMYE 488
Cdd:cd02667 189 PKCNSSEDK-----------------------------------------------------------------SSVLYR 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 489 LFSVMVHSGSAAGGHYYACIKS---------------------FSDDQWYSFNDQHVSRITQEDIkkthggssgsrgyys 547
Cdd:cd02667 204 LYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEV--------------- 268
|
410
....*....|....*
gi 1276346074 548 safaSSTNAYMLIYR 562
Cdd:cd02667 269 ----LKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-561 |
3.52e-21 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 95.84 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFmtpeFRNALYkwefedSEEDPVTSIPYQLQRLFVLlqtSKKRAIETTDVTRSFgWDSSeaw 248
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLT------CLKDLFESISEQKKRTGVI---SPKKFITRLKRENEL-FDNY--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 249 QQHDVQE----LCRVMFDALEQKWKQTE-------------QADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 311
Cdd:cd02663 64 MHQDAHEflnfLLNEIAEILDAERKAEKanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 312 RPYgssqafASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMSF 391
Cdd:cd02663 144 EQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 392 PEELDMSTfidiedekspqtesctdsgaenegschsdqmsndfSTDDAVDEgiclesssgsekiskpglekvemaetDQr 471
Cdd:cd02663 218 PLELRLFN-----------------------------------TTDDAENP--------------------------DR- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 472 kdpiqfqlgepnslMYELFSVMVHSGSAAG-GHYYACIKsfSDDQWYSFNDQHVSRITQEDIKKTHGGSsgsrgyyssaf 550
Cdd:cd02663 236 --------------LYELVAVVVHIGGGPNhGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFFGDS----------- 288
|
410
....*....|.
gi 1276346074 551 ASSTNAYMLIY 561
Cdd:cd02663 289 PNQATAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
167-531 |
5.25e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 93.03 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 167 YVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEDSEEDPVTSIPYQLQRLF--VLLQTSKKRAIETT-DVTRSFgwd 243
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYndELANQAPRRLLNALrEVNPMY--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 244 ssEAWQQHDVQELCRVMFDALEqkwkqteqaDLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASV 323
Cdd:cd02671 101 --EGYLQHDAQEVLQCILGNIQ---------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 324 E-------------EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFdfdyttmhriklndrms 390
Cdd:cd02671 170 EispdpktemktlkWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCF----------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 391 fpeeldmstfidiedekspqtesctdsgaenegschsdqmsndfstddavdegicleSSSGSEKISKPGLEKVEMAETDQ 470
Cdd:cd02671 233 ---------------------------------------------------------AANGSEFDCYGGLSKVNTPLLTP 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276346074 471 RKDPIqFQLGEPNSL-MYELFSVMVHSG-SAAGGHYYACIKsfsddqWYSFNDQHVSRITQED 531
Cdd:cd02671 256 LKLSL-EEWSTKPKNdVYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-396 |
1.52e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 85.07 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEDSEEDPVTSIPYQLQRL---FVLLQTSKKRAIETTDVT------ 237
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkFPSDVVDPANDLNCQLIKLadgLLSGRYSKPASLKSENDPyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 238 -RSF----GWDSSE--AWQQHDVQELCRVMFDALEQKWKQTEQADlINELYQGKLKDYVRCLECGYEGW--RIDTYLDIP 308
Cdd:cd02658 81 pSMFkaliGKGHPEfsTMRQQDALEFLLHLIDKLDRESFKNLGLN-PNDLFKFMIEDRLECLSCKKVKYtsELSEILSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 309 LVIRPYGSSQAFASV------EEALHAFIQPEildgPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDF--DYTTM 380
Cdd:cd02658 160 VPKDEATEKEEGELVyepvplEDCLKAYFAPE----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWVPK 235
|
250
....*....|....*.
gi 1276346074 381 hriKLNDRMSFPEELD 396
Cdd:cd02658 236 ---KLDVPIDVPEELG 248
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-396 |
7.09e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 78.56 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRnalykwEFedseedpvtsipyqLQRLFvllqtskkraiettdvtrsfgwdsseaw 248
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLI------EY--------------LEEFL---------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 249 QQHDVQELCRVMFDALEQKWKQteqadlineLYQGKLKDYVRCLECGY-EGWRIDTYLDIPLVIrPYGSSQAFASVEEAL 327
Cdd:cd02662 33 EQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGEsSKVRYESFTMLSLPV-PNQSSGSGTTLEHCL 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276346074 328 HAFIQPEILDGpnqYFCERCKKKcdarkglrFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMSFPEELD 396
Cdd:cd02662 103 DDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRGTST-KNSCKVSFPERLP 159
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-535 |
3.70e-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 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: 75.06 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTLFMTPEFRNAL--YKWEFEDSEE--DPVTSipyQLQRLFVLLQTSKKRA--IETTDVTR---- 238
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQssDNLTN---ALRDLFDTMDKKQEPVppIEFLQLLRmafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 239 SFGWDSSEA-WQQHDVQELCRVMFDALEQKWK-QTEQADLINELYQGKLKDYVRCLEcgyegwridtyldIPLVIRPYGS 316
Cdd:cd02657 78 QFAEKQNQGgYAQQDAEECWSQLLSVLSQKLPgAGSKGSFIDQLFGIELETKMKCTE-------------SPDEEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 317 SQAFASveeaLHAFIQPEI---LDGPNQYFCERCKKKCDAR-------KGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLN 386
Cdd:cd02657 145 SEYKLQ----CHISITTEVnylQDGLKKGLEEEIEKHSPTLgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 387 DRMSFPEELDMSTFidiedekspqtesCTDSGaenegschsdqmsndfstddavdegiclesssgsekiskpglekvema 466
Cdd:cd02657 221 RKVKFPFELDLYEL-------------CTPSG------------------------------------------------ 239
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 467 etdqrkdpiqfqlgepnslMYELFSVMVHSG-SAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKT 535
Cdd:cd02657 240 -------------------YYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKL 290
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
168-532 |
1.63e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 67.52 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYkwEFEDSEEDPVTSIP----------------------YQLQRLFVLLQT 225
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPterriggrevsrselqrsnqfvYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 226 SKKRAIETTDVTrsfgwdSSEAWQQHDVQELCRVMFDALE-------------QKWKQTEQADLINELYQGKLK-DYVRC 291
Cdd:cd02666 80 SNTRSVTPSKEL------AYLALRQQDVTECIDNVLFQLEvalepisnafagpDTEDDKEQSDLIKRLFSGKTKqQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 292 LECGYEGWRIDTYLDIPLVIrPYGSSQAFASVEEalHAfiqPEILDGPNQYFCERCKKKcdarkglrflhFPYLLTLQLK 371
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLV-DVGKKGREIVVLL--EP---KDLYDALDRYFDYDSLTK-----------LPQRSQVQAQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 372 rfdfdyttmhriklNDRMSFPEELDMSTFidiedekspqtesctdsgaenegschsDQMSNDFSTDDAVDEGICLESSSG 451
Cdd:cd02666 217 --------------LAQPLQRELISMDRY---------------------------ELPSSIDDIDELIREAIQSESSLV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 452 SEKISKPGLEKVEMAETDQrkDPIQFQlgepnslmYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQED 531
Cdd:cd02666 256 RQAQNELAELKHEIEKQFD--DLKSYG--------YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASE 325
|
.
gi 1276346074 532 I 532
Cdd:cd02666 326 V 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
322-564 |
2.72e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 64.90 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 322 SVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMSFP-EELDMSTF 400
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGV 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 401 IDIEDekSPQtesctdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekvemaetdqrkdpiqfqlg 480
Cdd:COG5560 754 EYMVD--DPR---------------------------------------------------------------------- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 481 epnsLMYELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstnAYMLI 560
Cdd:COG5560 762 ----LIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS-------------------AYVLF 818
|
....
gi 1276346074 561 YRLK 564
Cdd:COG5560 819 YRRK 822
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
168-521 |
3.10e-07 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 53.81 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEDSEEDpvTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFG------ 241
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKE--HCLLCELGFLFDMLEKAKGKNCQASNFLRALSsipeas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 242 ----WDSSEAWQQHD-----VQELCRVMFDALEQKWKQTEQ-----ADLINELYQGKLKDYVRCLECGYEGWR----IDT 303
Cdd:pfam13423 79 alglLDEDRETNSAIslsslIQSFNRFLLDQLSSEENSTPPnpspaESPLEQLFGIDAETTIRCSNCGHESVResstHVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 304 YLDIPLVIRPYGSSQAFASVEEALHAFIQPEILdgpNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDyttmHRI 383
Cdd:pfam13423 159 DLIYPRKPSSNNKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE----WRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 384 KLNDRMSFPEELDMSTFIDIEdekspqtesctdsgaenegschsdqmsndfstddavdegiclesssgsekiskpglekv 463
Cdd:pfam13423 232 LWKTPGWLPPEIGLTLSDDLQ----------------------------------------------------------- 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276346074 464 emaetdqrkdpiqfqlGEPNSLMYELFSVMVH-SGSAAGGHYYACIKSFS-------DDQWYSFND 521
Cdd:pfam13423 253 ----------------GDNEIVKYELRGVVVHiGDSGTSGHLVSFVKVADseledptESQWYLFND 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
169-532 |
4.36e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 53.27 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 169 GLVNQAMTCYLNSLLQTL-FMTPEFRNAL---------YKWEFEDSEEDPVtsipyQLQRLFVLlqtskkRAIETTDVTR 238
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLddlskelkvLKNVIRKPEPDLN-----QEEALKLF------TALWSSKEHK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 239 sFGWDSSEAwQQHDVQELCRVMFDALEqkwkqTEQADLINELYQGKLKDYVRclecgyegwriDTYLDIPLVI--RPYGS 316
Cdd:COG5533 70 -VGWIPPMG-SQEDAHELLGKLLDELK-----LDLVNSFTIRIFKTTKDKKK-----------TSTGDWFDIIieLPDQT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 317 S-QAFASVEEALHAFiQPEILDGPNQYFCERCKKKCDARKG--LRFLHFPYLLTLQLKRFDfdyttmhriklndrmsfpe 393
Cdd:COG5533 132 WvNNLKTLQEFIDNM-EELVDDETGVKAKENEELEVQAKQEyeVSFVKLPKILTIQLKRFA------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346074 394 eldmstfidiedekspqtesctdsgaeNEGschsdqmsndfstddavdegiclesssGSEKISKPGLEKVEMAetdQRKD 473
Cdd:COG5533 192 ---------------------------NLG---------------------------GNQKIDTEVDEKFELP---VKHD 214
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1276346074 474 PIqfqLGEPNSLMYELFSVMVHSGSAAGGHYYACIKsfSDDQWYSFNDQHVSRITQEDI 532
Cdd:COG5533 215 QI---LNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEA 268
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
487-561 |
5.91e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 49.09 E-value: 5.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276346074 487 YELFSVMVHSGSAAGGHYYACIKSFSDDQWYSFNDQHVSRITQEDIKKthggssgsrgyysSAFASSTN--AYMLIY 561
Cdd:cd02665 164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVER-------------DSFGGGRNpsAYCLMY 227
|
|
| |
