|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
186-566 |
4.33e-153 |
|
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: 465.58 E-value: 4.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 186 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 263
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 264 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 343
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 344 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDV 423
Cdd:cd02659 154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 424 EDEKSPQTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGH 503
Cdd:cd02659 234 GLAKKEGDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGH 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966986574 504 YYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 566
Cdd:cd02659 269 YYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
|
|
| USP47_C |
pfam19718 |
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ... |
1124-1363 |
3.67e-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: 322.47 E-value: 3.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 1124 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1202
Cdd:pfam19718 1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 1203 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLEDIEFAKGRGTFPCD 1282
Cdd:pfam19718 80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 1283 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1362
Cdd:pfam19718 160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239
|
.
gi 966986574 1363 Y 1363
Cdd:pfam19718 240 Y 240
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
188-561 |
3.81e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 258.14 E-value: 3.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 264
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 265 SE--AWQQHDVQELCRVMFDALEQKWKQ---TEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQA 339
Cdd:pfam00443 81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 340 FASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 419
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 420 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 499
Cdd:pfam00443 239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966986574 500 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 561
Cdd:pfam00443 267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
182-612 |
6.14e-77 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 277.91 E-value: 6.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 182 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 261
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 262 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygSSQAFA 341
Cdd:COG5077 265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL------NVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 342 SVEEALHAFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFI 421
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 422 DVEDEKSpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAG 501
Cdd:COG5077 418 DRDADKS----------------------------------------------------ENSDAVYVLYGVLVHSGDLHE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 502 GHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDE 577
Cdd:COG5077 446 GHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVD 525
|
410 420 430
....*....|....*....|....*....|....*
gi 966986574 578 YPEHIKNLVQKERELEEQEKRQREIERNTCKIKLF 612
Cdd:COG5077 526 IPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-562 |
1.89e-59 |
|
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: 207.66 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPV---------TSIPYQLQRLFVLLQTSKKRAIETTDVTRS 259
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 260 FGWDSSeawQQHDVQELCRVMFDALEQKWKQTEQADLIN---ELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIrpygs 336
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNivqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 337 sQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELD 416
Cdd:cd02668 153 -KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 417 MSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHS 496
Cdd:cd02668 232 MGEYLAESDE--------------------------------------------------------GSYVYELSGVLIHQ 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966986574 497 G-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIK--KTHGGSSGSRGYYSSAFASSTNAYMLIYR 562
Cdd:cd02668 256 GvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKlgNSEDPAKPRKSEIKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
189-562 |
1.40e-58 |
|
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: 202.71 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMtpefrnalykwefeeseedpvtsipyqlqrlfvllqtskkraiettdvtrsfgwdsseaw 268
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 269 QQHDVQELCRVMFDALEQKWKQ--------TEQADLINELYQGKLKDYVRCLECGYEG--WRIDTYLDIPLVIRPYGSSq 338
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESvsTEPELFLSLPLPVKGLPQV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 339 afaSVEEALHAFIQPEILDGPNQYFCErCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYtTMHRIKLNDRMTFPEELDMS 418
Cdd:cd02257 100 ---SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 419 TFIDVEDEKSPQtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGS 498
Cdd:cd02257 175 PYLSEGEKDSDS--------------------------------------------------DNGSYKYELVAVVVHSGT 204
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966986574 499 AA-GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssAFASSTNAYMLIYR 562
Cdd:cd02257 205 SAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE--------------FGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-561 |
3.15e-48 |
|
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: 174.77 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDP----VTSIPYQLQRlfVLLQTSKKRAI-----ETTDVTRS 259
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEgfcmMCALEAHVER--ALASSGPGSAPrifssNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 260 FGWDSseawqQHDVQELCRVMFDALEQ----KWKQTEQAD-------LINELYQGKLKDYVRCLECGYEGWRIDTYLDIP 328
Cdd:cd02661 81 FRIGR-----QEDAHEFLRYLLDAMQKacldRFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 329 LVIRpyGSSqafaSVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttMHriKLNDR 408
Cdd:cd02661 156 LDIK--GAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 409 MTFPEELDMSTFidvedekspqtesctdsgaenegschsdqMSNdfSNDdgvdegicletnsgtekisksglekNSLIYE 488
Cdd:cd02661 226 ISFPETLDLSPY-----------------------------MSQ--PND-------------------------GPLKYK 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966986574 489 LFSVMVHSG-SAAGGHYYACIKSfSDEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIY 561
Cdd:cd02661 250 LYAVLVHSGfSPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETV-------------------LSQKAYILFY 303
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-562 |
1.02e-46 |
|
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: 171.14 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKweFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDvtrSFGWDSSEAW 268
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD---YFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 269 ----QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygssqAFASVE 344
Cdd:cd02664 76 ftpgSQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---------SFPSVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 345 EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMStfidVE 424
Cdd:cd02664 138 DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLP----VR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 425 DEkspqTESCTDSGAENEGschsdqmsndfsnDDGVDEGICLETnsgtekisksgleknsLIYELFSVMVHSG-SAAGGH 503
Cdd:cd02664 214 VE----SKSSESPLEKKEE-------------ESGDDGELVTRQ----------------VHYRLYAVVVHSGySSESGH 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966986574 504 YY--------------ACIKSFSDEQ------WYSFNDQHVSRITQEDIKKThggssgsrgyysSAFASSTNAYMLIYR 562
Cdd:cd02664 261 YFtyardqtdadstgqECPEPKDAEEndesknWYLFNDSRVTFSSFESVQNV------------TSRFPKDTPYILFYE 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-562 |
1.22e-34 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 132.80 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 269 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASVEEALH 348
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS---------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 349 AFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMhrIKLNDRMTFP-EELDMSTFIDVEDEK 427
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVDTRSFT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 428 SPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknsliYELFSVMVHSGSAAGGHYYAC 507
Cdd:cd02674 170 GPFK-------------------------------------------------------YDLYAVVNHYGSLNGGHYTAY 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 966986574 508 IKSFSDEQWYSFNDQHVSRITQEDIKkthggssgsrgyyssafasSTNAYMLIYR 562
Cdd:cd02674 195 CKNNETNDWYKFDDSRVTKVSESSVV-------------------SSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-561 |
1.40e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 121.33 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNALY--KWEFEESEEDPVTSIPYQLQRLFVLLQTSKKRaiettdvtRSFG----- 261
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLsdRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--------SPYGpinll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 262 ---WDSS---EAWQQHDVQELCRVMFDALEQKWK--QTEQAD------LINELYQGKLKDYVRCLECGYEGWRIDTYLDI 327
Cdd:cd02660 74 ylsWKHSrnlAGYSQQDAHEFFQFLLDQLHTHYGgdKNEANDeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 328 PLVIRPYGSS---------QAFASVEEALHAFIQPEILdGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYT 398
Cdd:cd02660 154 SLDIPNKSTPswalgesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 399 TMHRiKLNDRMTFPEELDMSTFIDVedekspqtesctdsgaenegSCHSDQMSNDFSNDdgvdegicletnsgtekisks 478
Cdd:cd02660 233 KTSR-KIDTYVQFPLELNMTPYTSS--------------------SIGDTQDSNSLDPD--------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 479 gleknsLIYELFSVMVHSGSAAGGHYYACIKsFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssafassTNAYM 558
Cdd:cd02660 271 ------YTYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRVSEEEVLK-------------------SQAYL 324
|
...
gi 966986574 559 LIY 561
Cdd:cd02660 325 LFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-562 |
2.61e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 110.17 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNALykwefeesEEDPVTsipyqlqrlfvLLQTSKKRAIETTDvtrsfgwdsseaW 268
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL--------SETPKE-----------LFSQVCRKAPQFKG------------Y 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 269 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAfaSVEEALH 348
Cdd:cd02667 50 QQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSEC--SIESCLK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 349 AFIQPEILDGPNQYFCERCKKkcdARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELDMSTFIDVedeks 428
Cdd:cd02667 119 QFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAPFCDP----- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 429 pqtesctdsgaenegSCHSDQmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYACI 508
Cdd:cd02667 190 ---------------KCNSSE-------------------------------DKSSVLYRLYGVVEHSGTMRSGHYVAYV 223
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966986574 509 KS---------------FSDE------QWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIYR 562
Cdd:cd02667 224 KVrppqqrlsdltkskpAADEagpgsgQWYYISDSDVREVSLEEV-------------------LKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-561 |
1.85e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 99.31 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFmtpeFRNALYkwefeeSEEDPVTSIPYQLQRLFVLlqtSKKRAIETTDVTRSFgWDSSeaw 268
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLT------CLKDLFESISEQKKRTGVI---SPKKFITRLKRENEL-FDNY--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 269 QQHDVQE----LCRVMFDALEQKWKQTE-------------QADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 331
Cdd:cd02663 64 MHQDAHEflnfLLNEIAEILDAERKAEKanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 332 RPYgssqafASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTF 411
Cdd:cd02663 144 EQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 412 PEELDMStfidvedekspqteSCTDsgaenegschsdqmsnDFSNDDgvdegicletnsgtekisksgleknsLIYELFS 491
Cdd:cd02663 218 PLELRLF--------------NTTD----------------DAENPD--------------------------RLYELVA 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966986574 492 VMVHSGSAAG-GHYYACIKsfSDEQWYSFNDQHVSRITQEDIKKTHGGSsgsrgyyssafASSTNAYMLIY 561
Cdd:cd02663 242 VVVHIGGGPNhGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFFGDS-----------PNQATAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-531 |
3.65e-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: 93.42 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 187 YVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPVTSIPYQLQRLF--VLLQTSKKRAIETT-DVTRSFgwd 263
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYndELANQAPRRLLNALrEVNPMY--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 264 ssEAWQQHDVQELCRVMFDALEqkwkqteqaDLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASV 343
Cdd:cd02671 101 --EGYLQHDAQEVLQCILGNIQ---------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 344 E-------------EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRI----KLN 406
Cdd:cd02671 170 EispdpktemktlkWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 407 DRMTFPEELdmstfidvedekspqtesctdsgaenegSCH--SDQMSNDfsnddgvdegicletnsgtekisksglekns 484
Cdd:cd02671 250 TPLLTPLKL----------------------------SLEewSTKPKND------------------------------- 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966986574 485 lIYELFSVMVHSG-SAAGGHYYACIKsfsdeqWYSFNDQHVSRITQED 531
Cdd:cd02671 271 -VYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-536 |
1.72e-19 |
|
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: 90.85 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRL---FVLLQTSKKRAIETTDVT------ 257
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkFPSDVVDPANDLNCQLIKLadgLLSGRYSKPASLKSENDPyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 258 -RSF----GWDSSE--AWQQHDVQELCRVMFDALEQKWKQTEQADlINELYQGKLKDYVRCLECGYEGW--RIDTYLDIP 328
Cdd:cd02658 81 pSMFkaliGKGHPEfsTMRQQDALEFLLHLIDKLDRESFKNLGLN-PNDLFKFMIEDRLECLSCKKVKYtsELSEILSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 329 LVIRPYGSSQAFASV------EEALHAFIQPEildgPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDF--DYTtm 400
Cdd:cd02658 160 VPKDEATEKEEGELVyepvplEDCLKAYFAPE----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 401 hriklndrmtfPEELDMStfIDVEDEKSPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgl 480
Cdd:cd02658 234 -----------PKKLDVP--IDVPEELGPGK------------------------------------------------- 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 966986574 481 eknsliYELFSVMVHSG-SAAGGHYYACIKSFSDE--QWYSFNDQHVSRITQEDIKKTH 536
Cdd:cd02658 252 ------YELIAFISHKGtSVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKL 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-535 |
1.37e-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 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: 82.38 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRNAL--YKWEFEESEE--DPVTSipyQLQRLFVLLQTSKKRA--IETTDVTR---- 258
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQssDNLTN---ALRDLFDTMDKKQEPVppIEFLQLLRmafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 259 SFGWDSSEA-WQQHDVQELCRVMFDALEQKWK-QTEQADLINELYQGKLKDYVRCLEcgyegwridtyldIPLVIRPYGS 336
Cdd:cd02657 78 QFAEKQNQGgYAQQDAEECWSQLLSVLSQKLPgAGSKGSFIDQLFGIELETKMKCTE-------------SPDEEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 337 SQAFASveeaLHAFIQPEI---LDGPNQYFCERCKKKCDAR-------KGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLN 406
Cdd:cd02657 145 SEYKLQ----CHISITTEVnylQDGLKKGLEEEIEKHSPTLgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 407 DRMTFPEELDMSTFidvedekspqtesCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknslI 486
Cdd:cd02657 221 RKVKFPFELDLYEL-------------CTPSG-----------------------------------------------Y 240
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 966986574 487 YELFSVMVHSG-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKT 535
Cdd:cd02657 241 YELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKL 290
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-561 |
6.57e-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: 78.95 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTLFMTPEFRnalykwEFeeseedpvtsipyqLQRLFvllqtskkraiettdvtrsfgwdsseaw 268
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLI------EY--------------LEEFL---------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 269 QQHDVQELCRVMFDALEQKWKQteqadlineLYQGKLKDYVRCLECGY-EGWRIDTYLDIPLVIrPYGSSQAFASVEEAL 347
Cdd:cd02662 33 EQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGEsSKVRYESFTMLSLPV-PNQSSGSGTTLEHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 348 HAFIQPEILDGpnqYFCERCKKKcdarkglrFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELdmstfidvedek 427
Cdd:cd02662 103 DDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRGTST-KNSCKVSFPERL------------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 428 spqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHSGSAAGGHY--- 504
Cdd:cd02662 159 -------------------------------------------------------PKVLYRLRAVVVHYGSHSSGHYvcy 183
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966986574 505 --------YACIKSFS---------DEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafASSTNAYMLIY 561
Cdd:cd02662 184 rrkplfskDKEPGSFVrmregpsstSHPWWRISDTTVKEVSESEV------------------LEQKSAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
188-532 |
6.07e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 74.84 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYkwEFEESEEDPVTSIP----------------------YQLQRLFVLLQT 245
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPterriggrevsrselqrsnqfvYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 246 SKKRAIETTDVTrsfgwdSSEAWQQHDVQELCRVMFDALE-------------QKWKQTEQADLINELYQGKLK-DYVRC 311
Cdd:cd02666 80 SNTRSVTPSKEL------AYLALRQQDVTECIDNVLFQLEvalepisnafagpDTEDDKEQSDLIKRLFSGKTKqQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 312 LECGYEGWRIDTYLDIPLVIrPYGSSQAFASVEEalHAfiqPEILDGPNQYFCERCKKKcdarkglrflhFPYLLTLQLK 391
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLV-DVGKKGREIVVLL--EP---KDLYDALDRYFDYDSLTK-----------LPQRSQVQAQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 392 rfdfdyttmhriklNDRMTFPEELDMSTFidvEDEKSPQTESCTDSGAENEGSCHSDQMSNdfsnddgvdegiclETNSG 471
Cdd:cd02666 217 --------------LAQPLQRELISMDRY---ELPSSIDDIDELIREAIQSESSLVRQAQN--------------ELAEL 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966986574 472 TEKISKSGLEKNSLIYELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDI 532
Cdd:cd02666 266 KHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
342-564 |
3.62e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 74.53 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 342 SVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFP-EELDMSTF 420
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGV 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 421 IdvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGLEKNSLIYELFSVMVHSGSAA 500
Cdd:COG5560 754 E--------------------------------------------------------YMVDDPRLIYDLYAVDNHYGGLS 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966986574 501 GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstnAYMLIYRLK 564
Cdd:COG5560 778 GGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS-------------------AYVLFYRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
189-532 |
2.65e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 62.90 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 189 GLVNQAMTCYLNSLLQTL-FMTPEFRNALYKWEFE--------ESEEDPVTsipyQLQRLFVLlqtskkRAIETTDVTRs 259
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKElkvlknviRKPEPDLN----QEEALKLF------TALWSSKEHK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 260 FGWDSSEAwQQHDVQELCRVMFDALEqkwkqTEQADLINELYQGKLKDYVRclecgyegwriDTYLDIPLVI--RPYGSS 337
Cdd:COG5533 70 VGWIPPMG-SQEDAHELLGKLLDELK-----LDLVNSFTIRIFKTTKDKKK-----------TSTGDWFDIIieLPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 338 -QAFASVEEALHAFiQPEILDGPNQYFCERCKKKCDARKG--LRFLHFPYLLTLQLKRFDFDyttmhriklndrmtfpee 414
Cdd:COG5533 133 vNNLKTLQEFIDNM-EELVDDETGVKAKENEELEVQAKQEyeVSFVKLPKILTIQLKRFANL------------------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 415 ldmSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgVDEGICLetnsgTEKISKSGLEKNSLIYELFSVMV 494
Cdd:COG5533 194 ---GGNQKIDTE---------------------------------VDEKFEL-----PVKHDQILNIVKETYYDLVGFVL 232
|
330 340 350
....*....|....*....|....*....|....*...
gi 966986574 495 HSGSAAGGHYYACIKsfSDEQWYSFNDQHVSRITQEDI 532
Cdd:COG5533 233 HQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEA 268
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
188-521 |
2.08e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 57.28 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDpvTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFG------ 261
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKE--HCLLCELGFLFDMLEKAKGKNCQASNFLRALSsipeas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 262 ----WDSSEAWQQHD-----VQELCRVMFDALEQKWKQTEQ-----ADLINELYQGKLKDYVRCLECGYEGWR----IDT 323
Cdd:pfam13423 79 alglLDEDRETNSAIslsslIQSFNRFLLDQLSSEENSTPPnpspaESPLEQLFGIDAETTIRCSNCGHESVResstHVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 324 YLDIPLVIRPYGSSQAFASVEEALHAFIQPEILdgpNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttmhri 403
Cdd:pfam13423 159 DLIYPRKPSSNNKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 404 kLNDRMT---FPEELDMSTFIDvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGL 480
Cdd:pfam13423 230 -RQLWKTpgwLPPEIGLTLSDD-------------------------------------------------------LQG 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 966986574 481 EKNSLIYELFSVMVH-SGSAAGGHYYACIKSFSDE-------QWYSFND 521
Cdd:pfam13423 254 DNEIVKYELRGVVVHiGDSGTSGHLVSFVKVADSEledptesQWYLFND 302
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
487-561 |
1.92e-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: 50.63 E-value: 1.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966986574 487 YELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyysSAFASSTN--AYMLIY 561
Cdd:cd02665 164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVER-------------DSFGGGRNpsAYCLMY 227
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
184-331 |
3.05e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 51.81 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 184 ETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEES--EEDP------VTSIPYQL-QRLFvllqTSKKRAIETT 254
Cdd:COG5560 262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESinEENPlgmhgsVASAYADLiKQLY----DGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966986574 255 DVTRSFGWDSSE--AWQQHDVQELCRVMFDALE------QKWKQTEQADL--------------------------INEL 300
Cdd:COG5560 338 GFKKTIGSFNEEfsGYDQQDSQEFIAFLLDGLHedlnriIKKPYTSKPDLspgddvvvkkkakecwwehlkrndsiITDL 417
|
170 180 190
....*....|....*....|....*....|.
gi 966986574 301 YQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 331
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| |
