|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
166-546 |
1.47e-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: 466.35 E-value: 1.47e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 166 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 243
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 244 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 323
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 324 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDV 403
Cdd:cd02659 154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 404 EDEKSPQTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGH 483
Cdd:cd02659 234 GLAKKEGDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGH 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722217619 484 YYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 546
Cdd:cd02659 269 YYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
|
|
| USP47_C |
pfam19718 |
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ... |
1103-1342 |
3.00e-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: 3.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 1103 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1181
Cdd:pfam19718 1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 1182 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1261
Cdd:pfam19718 80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 1262 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1341
Cdd:pfam19718 160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239
|
.
gi 1722217619 1342 Y 1342
Cdd:pfam19718 240 Y 240
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
168-541 |
2.85e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 258.14 E-value: 2.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 244
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 245 SE--AWQQHDVQELCRVMFDALEQKWKQ---TEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQA 319
Cdd:pfam00443 81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 320 FASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 399
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 400 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 479
Cdd:pfam00443 239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722217619 480 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 541
Cdd:pfam00443 267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
162-592 |
4.56e-77 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 278.29 E-value: 4.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 162 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 241
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 242 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygSSQAFA 321
Cdd:COG5077 265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL------NVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 322 SVEEALHAFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFI 401
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 402 DVEDEKSpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAG 481
Cdd:COG5077 418 DRDADKS----------------------------------------------------ENSDAVYVLYGVLVHSGDLHE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 482 GHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDE 557
Cdd:COG5077 446 GHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVD 525
|
410 420 430
....*....|....*....|....*....|....*
gi 1722217619 558 YPEHIKNLVQKERELEEQEKRQREIERNTCKIKLF 592
Cdd:COG5077 526 IPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-542 |
1.44e-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: 208.04 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPV---------TSIPYQLQRLFVLLQTSKKRAIETTDVTRS 239
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 240 FGWDSSeawQQHDVQELCRVMFDALEQKWKQTEQADLIN---ELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIrpygs 316
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNivqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 317 sQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELD 396
Cdd:cd02668 153 -KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 397 MSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHS 476
Cdd:cd02668 232 MGEYLAESDE--------------------------------------------------------GSYVYELSGVLIHQ 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722217619 477 G-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIK--KTHGGSSGSRGYYSSAFASSTNAYMLIYR 542
Cdd:cd02668 256 GvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKlgNSEDPAKPRKSEIKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
169-542 |
9.93e-59 |
|
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: 203.10 E-value: 9.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMtpefrnalykwefeeseedpvtsipyqlqrlfvllqtskkraiettdvtrsfgwdsseaw 248
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 249 QQHDVQELCRVMFDALEQKWKQ--------TEQADLINELYQGKLKDYVRCLECGYEG--WRIDTYLDIPLVIRPYGSSq 318
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESvsTEPELFLSLPLPVKGLPQV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 319 afaSVEEALHAFIQPEILDGPNQYFCErCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYtTMHRIKLNDRMTFPEELDMS 398
Cdd:cd02257 100 ---SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 399 TFIDVEDEKSPQtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGS 478
Cdd:cd02257 175 PYLSEGEKDSDS--------------------------------------------------DNGSYKYELVAVVVHSGT 204
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722217619 479 AA-GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssAFASSTNAYMLIYR 542
Cdd:cd02257 205 SAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE--------------FGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-541 |
2.65e-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: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDP----VTSIPYQLQRlfVLLQTSKKRAI-----ETTDVTRS 239
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEgfcmMCALEAHVER--ALASSGPGSAPrifssNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 240 FGWDSseawqQHDVQELCRVMFDALEQ----KWKQTEQAD-------LINELYQGKLKDYVRCLECGYEGWRIDTYLDIP 308
Cdd:cd02661 81 FRIGR-----QEDAHEFLRYLLDAMQKacldRFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 309 LVIRpyGSSqafaSVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttMHriKLNDR 388
Cdd:cd02661 156 LDIK--GAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 389 MTFPEELDMSTFidvedekspqtesctdsgaenegschsdqMSNdfSNDdgvdegicletnsgtekisksglekNSLIYE 468
Cdd:cd02661 226 ISFPETLDLSPY-----------------------------MSQ--PND-------------------------GPLKYK 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722217619 469 LFSVMVHSG-SAAGGHYYACIKSfSDEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIY 541
Cdd:cd02661 250 LYAVLVHSGfSPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETV-------------------LSQKAYILFY 303
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-542 |
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 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKweFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDvtrSFGWDSSEAW 248
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD---YFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 249 ----QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygssqAFASVE 324
Cdd:cd02664 76 ftpgSQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---------SFPSVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 325 EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMStfidVE 404
Cdd:cd02664 138 DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLP----VR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 405 DEkspqTESCTDSGAENEGschsdqmsndfsnDDGVDEGICLETnsgtekisksgleknsLIYELFSVMVHSG-SAAGGH 483
Cdd:cd02664 214 VE----SKSSESPLEKKEE-------------ESGDDGELVTRQ----------------VHYRLYAVVVHSGySSESGH 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722217619 484 YY--------------ACIKSFSDEQ------WYSFNDQHVSRITQEDIKKThggssgsrgyysSAFASSTNAYMLIYR 542
Cdd:cd02664 261 YFtyardqtdadstgqECPEPKDAEEndesknWYLFNDSRVTFSSFESVQNV------------TSRFPKDTPYILFYE 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
249-542 |
1.11e-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: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 249 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASVEEALH 328
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS---------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 329 AFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMhrIKLNDRMTFP-EELDMSTFIDVEDEK 407
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVDTRSFT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 408 SPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknsliYELFSVMVHSGSAAGGHYYAC 487
Cdd:cd02674 170 GPFK-------------------------------------------------------YDLYAVVNHYGSLNGGHYTAY 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1722217619 488 IKSFSDEQWYSFNDQHVSRITQEDIKkthggssgsrgyyssafasSTNAYMLIYR 542
Cdd:cd02674 195 CKNNETNDWYKFDDSRVTKVSESSVV-------------------SSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-541 |
1.30e-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: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALY--KWEFEESEEDPVTSIPYQLQRLFVLLQTSKKRaiettdvtRSFG----- 241
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLsdRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--------SPYGpinll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 242 ---WDSS---EAWQQHDVQELCRVMFDALEQKWK--QTEQAD------LINELYQGKLKDYVRCLECGYEGWRIDTYLDI 307
Cdd:cd02660 74 ylsWKHSrnlAGYSQQDAHEFFQFLLDQLHTHYGgdKNEANDeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 308 PLVIRPYGSS---------QAFASVEEALHAFIQPEILdGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYT 378
Cdd:cd02660 154 SLDIPNKSTPswalgesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 379 TMHRiKLNDRMTFPEELDMSTFIDVedekspqtesctdsgaenegSCHSDQMSNDFSNDdgvdegicletnsgtekisks 458
Cdd:cd02660 233 KTSR-KIDTYVQFPLELNMTPYTSS--------------------SIGDTQDSNSLDPD--------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 459 gleknsLIYELFSVMVHSGSAAGGHYYACIKsFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssafassTNAYM 538
Cdd:cd02660 271 ------YTYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRVSEEEVLK-------------------SQAYL 324
|
...
gi 1722217619 539 LIY 541
Cdd:cd02660 325 LFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-542 |
2.51e-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: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALykwefeesEEDPVTsipyqlqrlfvLLQTSKKRAIETTDvtrsfgwdsseaW 248
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL--------SETPKE-----------LFSQVCRKAPQFKG------------Y 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 249 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAfaSVEEALH 328
Cdd:cd02667 50 QQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSEC--SIESCLK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 329 AFIQPEILDGPNQYFCERCKKkcdARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELDMSTFIDVedeks 408
Cdd:cd02667 119 QFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAPFCDP----- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 409 pqtesctdsgaenegSCHSDQmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYACI 488
Cdd:cd02667 190 ---------------KCNSSE-------------------------------DKSSVLYRLYGVVEHSGTMRSGHYVAYV 223
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722217619 489 KS---------------FSDE------QWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIYR 542
Cdd:cd02667 224 KVrppqqrlsdltkskpAADEagpgsgQWYYISDSDVREVSLEEV-------------------LKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-541 |
1.60e-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: 99.69 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFmtpeFRNALYkwefeeSEEDPVTSIPYQLQRLFVLlqtSKKRAIETTDVTRSFgWDSSeaw 248
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLT------CLKDLFESISEQKKRTGVI---SPKKFITRLKRENEL-FDNY--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 249 QQHDVQE----LCRVMFDALEQKWKQTE-------------QADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 311
Cdd:cd02663 64 MHQDAHEflnfLLNEIAEILDAERKAEKanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 312 RPYgssqafASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTF 391
Cdd:cd02663 144 EQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 392 PEELDMStfidvedekspqteSCTDsgaenegschsdqmsnDFSNDDgvdegicletnsgtekisksgleknsLIYELFS 471
Cdd:cd02663 218 PLELRLF--------------NTTD----------------DAENPD--------------------------RLYELVA 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722217619 472 VMVHSGSAAG-GHYYACIKsfSDEQWYSFNDQHVSRITQEDIKKTHGGSsgsrgyyssafASSTNAYMLIY 541
Cdd:cd02663 242 VVVHIGGGPNhGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFFGDS-----------PNQATAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
167-511 |
3.58e-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: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 167 YVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPVTSIPYQLQRLF--VLLQTSKKRAIETT-DVTRSFgwd 243
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYndELANQAPRRLLNALrEVNPMY--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 244 ssEAWQQHDVQELCRVMFDALEqkwkqteqaDLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASV 323
Cdd:cd02671 101 --EGYLQHDAQEVLQCILGNIQ---------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 324 E-------------EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRI----KLN 386
Cdd:cd02671 170 EispdpktemktlkWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 387 DRMTFPEELdmstfidvedekspqtesctdsgaenegSCH--SDQMSNDfsnddgvdegicletnsgtekisksglekns 464
Cdd:cd02671 250 TPLLTPLKL----------------------------SLEewSTKPKND------------------------------- 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1722217619 465 lIYELFSVMVHSG-SAAGGHYYACIKsfsdeqWYSFNDQHVSRITQED 511
Cdd:cd02671 271 -VYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-516 |
1.46e-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: 91.23 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRL---FVLLQTSKKRAIETTDVT------ 237
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkFPSDVVDPANDLNCQLIKLadgLLSGRYSKPASLKSENDPyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 238 -RSF----GWDSSE--AWQQHDVQELCRVMFDALEQKWKQTEQADlINELYQGKLKDYVRCLECGYEGW--RIDTYLDIP 308
Cdd:cd02658 81 pSMFkaliGKGHPEfsTMRQQDALEFLLHLIDKLDRESFKNLGLN-PNDLFKFMIEDRLECLSCKKVKYtsELSEILSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 309 LVIRPYGSSQAFASV------EEALHAFIQPEildgPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDF--DYTtm 380
Cdd:cd02658 160 VPKDEATEKEEGELVyepvplEDCLKAYFAPE----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 381 hriklndrmtfPEELDMStfIDVEDEKSPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgl 460
Cdd:cd02658 234 -----------PKKLDVP--IDVPEELGPGK------------------------------------------------- 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1722217619 461 eknsliYELFSVMVHSG-SAAGGHYYACIKSFSDE--QWYSFNDQHVSRITQEDIKKTH 516
Cdd:cd02658 252 ------YELIAFISHKGtSVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKL 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-515 |
1.32e-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: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRNAL--YKWEFEESEE--DPVTSipyQLQRLFVLLQTSKKRA--IETTDVTR---- 238
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQssDNLTN---ALRDLFDTMDKKQEPVppIEFLQLLRmafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 239 SFGWDSSEA-WQQHDVQELCRVMFDALEQKWK-QTEQADLINELYQGKLKDYVRCLEcgyegwridtyldIPLVIRPYGS 316
Cdd:cd02657 78 QFAEKQNQGgYAQQDAEECWSQLLSVLSQKLPgAGSKGSFIDQLFGIELETKMKCTE-------------SPDEEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 317 SQAFASveeaLHAFIQPEI---LDGPNQYFCERCKKKCDAR-------KGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLN 386
Cdd:cd02657 145 SEYKLQ----CHISITTEVnylQDGLKKGLEEEIEKHSPTLgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 387 DRMTFPEELDMSTFidvedekspqtesCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknslI 466
Cdd:cd02657 221 RKVKFPFELDLYEL-------------CTPSG-----------------------------------------------Y 240
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1722217619 467 YELFSVMVHSG-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKT 515
Cdd:cd02657 241 YELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKL 290
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-541 |
6.22e-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: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTLFMTPEFRnalykwEFeeseedpvtsipyqLQRLFvllqtskkraiettdvtrsfgwdsseaw 248
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLI------EY--------------LEEFL---------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 249 QQHDVQELCRVMFDALEQKWKQteqadlineLYQGKLKDYVRCLECGY-EGWRIDTYLDIPLVIrPYGSSQAFASVEEAL 327
Cdd:cd02662 33 EQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGEsSKVRYESFTMLSLPV-PNQSSGSGTTLEHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 328 HAFIQPEILDGpnqYFCERCKKKcdarkglrFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELdmstfidvedek 407
Cdd:cd02662 103 DDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRGTST-KNSCKVSFPERL------------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 408 spqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHSGSAAGGHY--- 484
Cdd:cd02662 159 -------------------------------------------------------PKVLYRLRAVVVHYGSHSSGHYvcy 183
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722217619 485 --------YACIKSFS---------DEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafASSTNAYMLIY 541
Cdd:cd02662 184 rrkplfskDKEPGSFVrmregpsstSHPWWRISDTTVKEVSESEV------------------LEQKSAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
168-512 |
5.96e-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: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYkwEFEESEEDPVTSIP----------------------YQLQRLFVLLQT 225
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPterriggrevsrselqrsnqfvYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 226 SKKRAIETTDVTrsfgwdSSEAWQQHDVQELCRVMFDALE-------------QKWKQTEQADLINELYQGKLK-DYVRC 291
Cdd:cd02666 80 SNTRSVTPSKEL------AYLALRQQDVTECIDNVLFQLEvalepisnafagpDTEDDKEQSDLIKRLFSGKTKqQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 292 LECGYEGWRIDTYLDIPLVIrPYGSSQAFASVEEalHAfiqPEILDGPNQYFCERCKKKcdarkglrflhFPYLLTLQLK 371
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLV-DVGKKGREIVVLL--EP---KDLYDALDRYFDYDSLTK-----------LPQRSQVQAQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 372 rfdfdyttmhriklNDRMTFPEELDMSTFidvEDEKSPQTESCTDSGAENEGSCHSDQMSNdfsnddgvdegiclETNSG 451
Cdd:cd02666 217 --------------LAQPLQRELISMDRY---ELPSSIDDIDELIREAIQSESSLVRQAQN--------------ELAEL 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722217619 452 TEKISKSGLEKNSLIYELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDI 512
Cdd:cd02666 266 KHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
322-544 |
3.35e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 74.53 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 322 SVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFP-EELDMSTF 400
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGV 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 401 IdvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGLEKNSLIYELFSVMVHSGSAA 480
Cdd:COG5560 754 E--------------------------------------------------------YMVDDPRLIYDLYAVDNHYGGLS 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722217619 481 GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstnAYMLIYRLK 544
Cdd:COG5560 778 GGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS-------------------AYVLFYRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
169-512 |
2.75e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 62.90 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 169 GLVNQAMTCYLNSLLQTL-FMTPEFRNALYKWEFE--------ESEEDPVTsipyQLQRLFVLlqtskkRAIETTDVTRs 239
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKElkvlknviRKPEPDLN----QEEALKLF------TALWSSKEHK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 240 FGWDSSEAwQQHDVQELCRVMFDALEqkwkqTEQADLINELYQGKLKDYVRclecgyegwriDTYLDIPLVI--RPYGSS 317
Cdd:COG5533 70 VGWIPPMG-SQEDAHELLGKLLDELK-----LDLVNSFTIRIFKTTKDKKK-----------TSTGDWFDIIieLPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 318 -QAFASVEEALHAFiQPEILDGPNQYFCERCKKKCDARKG--LRFLHFPYLLTLQLKRFDFDyttmhriklndrmtfpee 394
Cdd:COG5533 133 vNNLKTLQEFIDNM-EELVDDETGVKAKENEELEVQAKQEyeVSFVKLPKILTIQLKRFANL------------------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 395 ldmSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgVDEGICLetnsgTEKISKSGLEKNSLIYELFSVMV 474
Cdd:COG5533 194 ---GGNQKIDTE---------------------------------VDEKFEL-----PVKHDQILNIVKETYYDLVGFVL 232
|
330 340 350
....*....|....*....|....*....|....*...
gi 1722217619 475 HSGSAAGGHYYACIKsfSDEQWYSFNDQHVSRITQEDI 512
Cdd:COG5533 233 HQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEA 268
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
168-501 |
1.99e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 57.67 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDpvTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFG------ 241
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKE--HCLLCELGFLFDMLEKAKGKNCQASNFLRALSsipeas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 242 ----WDSSEAWQQHD-----VQELCRVMFDALEQKWKQTEQ-----ADLINELYQGKLKDYVRCLECGYEGWR----IDT 303
Cdd:pfam13423 79 alglLDEDRETNSAIslsslIQSFNRFLLDQLSSEENSTPPnpspaESPLEQLFGIDAETTIRCSNCGHESVResstHVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 304 YLDIPLVIRPYGSSQAFASVEEALHAFIQPEILdgpNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttmhri 383
Cdd:pfam13423 159 DLIYPRKPSSNNKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 384 kLNDRMT---FPEELDMSTFIDvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGL 460
Cdd:pfam13423 230 -RQLWKTpgwLPPEIGLTLSDD-------------------------------------------------------LQG 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1722217619 461 EKNSLIYELFSVMVH-SGSAAGGHYYACIKSFSDE-------QWYSFND 501
Cdd:pfam13423 254 DNEIVKYELRGVVVHiGDSGTSGHLVSFVKVADSEledptesQWYLFND 302
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
467-541 |
1.79e-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: 1.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722217619 467 YELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyysSAFASSTN--AYMLIY 541
Cdd:cd02665 164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVER-------------DSFGGGRNpsAYCLMY 227
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
164-311 |
2.90e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 51.81 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 164 ETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEES--EEDP------VTSIPYQL-QRLFvllqTSKKRAIETT 234
Cdd:COG5560 262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESinEENPlgmhgsVASAYADLiKQLY----DGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 235 DVTRSFGWDSSE--AWQQHDVQELCRVMFDALE------QKWKQTEQADL--------------------------INEL 280
Cdd:COG5560 338 GFKKTIGSFNEEfsGYDQQDSQEFIAFLLDGLHedlnriIKKPYTSKPDLspgddvvvkkkakecwwehlkrndsiITDL 417
|
170 180 190
....*....|....*....|....*....|.
gi 1722217619 281 YQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 311
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
813-1004 |
3.20e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 41.82 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 813 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 888
Cdd:NF033609 521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722217619 889 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 967
Cdd:NF033609 597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669
|
170 180 190
....*....|....*....|....*....|....*..
gi 1722217619 968 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 1004
Cdd:NF033609 670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
|
|
| |
