|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-540 |
2.09e-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: 2.09e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 160 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 237
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 238 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 317
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 318 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDV 397
Cdd:cd02659 154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 398 EDEKSPQTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGH 477
Cdd:cd02659 234 GLAKKEGDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGH 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722210838 478 YYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 540
Cdd:cd02659 269 YYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
|
|
| USP47_C |
pfam19718 |
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ... |
1097-1336 |
2.96e-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: 2.96e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 1097 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1175
Cdd:pfam19718 1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 1176 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1255
Cdd:pfam19718 80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 1256 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1335
Cdd:pfam19718 160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239
|
.
gi 1722210838 1336 Y 1336
Cdd:pfam19718 240 Y 240
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
162-535 |
4.23e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 257.76 E-value: 4.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 162 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 238
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 239 SE--AWQQHDVQELCRVMFDALEQKWKQ---TEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQA 313
Cdd:pfam00443 81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 314 FASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 393
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 394 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 473
Cdd:pfam00443 239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722210838 474 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 535
Cdd:pfam00443 267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
156-586 |
5.03e-77 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 277.91 E-value: 5.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 156 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 235
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 236 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygSSQAFA 315
Cdd:COG5077 265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL------NVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 316 SVEEALHAFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFI 395
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 396 DVEDEKSpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAG 475
Cdd:COG5077 418 DRDADKS----------------------------------------------------ENSDAVYVLYGVLVHSGDLHE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 476 GHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDE 551
Cdd:COG5077 446 GHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVD 525
|
410 420 430
....*....|....*....|....*....|....*
gi 1722210838 552 YPEHIKNLVQKERELEEQEKRQREIERNTCKIKLF 586
Cdd:COG5077 526 IPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-536 |
1.86e-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: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPV---------TSIPYQLQRLFVLLQTSKKRAIETTDVTRS 233
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 234 FGWDSSeawQQHDVQELCRVMFDALEQKWKQTEQADLIN---ELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIrpygs 310
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNivqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 311 sQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELD 390
Cdd:cd02668 153 -KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 391 MSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHS 470
Cdd:cd02668 232 MGEYLAESDE--------------------------------------------------------GSYVYELSGVLIHQ 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722210838 471 G-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIK--KTHGGSSGSRGYYSSAFASSTNAYMLIYR 536
Cdd:cd02668 256 GvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKlgNSEDPAKPRKSEIKKGTHSSRTAYMLVYK 324
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
163-536 |
1.44e-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: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMtpefrnalykwefeeseedpvtsipyqlqrlfvllqtskkraiettdvtrsfgwdsseaw 242
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 243 QQHDVQELCRVMFDALEQKWKQ--------TEQADLINELYQGKLKDYVRCLECGYEG--WRIDTYLDIPLVIRPYGSSq 312
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESvsTEPELFLSLPLPVKGLPQV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 313 afaSVEEALHAFIQPEILDGPNQYFCErCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYtTMHRIKLNDRMTFPEELDMS 392
Cdd:cd02257 100 ---SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 393 TFIDVEDEKSPQtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGS 472
Cdd:cd02257 175 PYLSEGEKDSDS--------------------------------------------------DNGSYKYELVAVVVHSGT 204
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722210838 473 AA-GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssAFASSTNAYMLIYR 536
Cdd:cd02257 205 SAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE--------------FGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-535 |
3.19e-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: 174.39 E-value: 3.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDP----VTSIPYQLQRlfVLLQTSKKRAI-----ETTDVTRS 233
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEgfcmMCALEAHVER--ALASSGPGSAPrifssNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 234 FGWDSseawqQHDVQELCRVMFDALEQ----KWKQTEQAD-------LINELYQGKLKDYVRCLECGYEGWRIDTYLDIP 302
Cdd:cd02661 81 FRIGR-----QEDAHEFLRYLLDAMQKacldRFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 303 LVIRpyGSSqafaSVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttMHriKLNDR 382
Cdd:cd02661 156 LDIK--GAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 383 MTFPEELDMSTFidvedekspqtesctdsgaenegschsdqMSNdfSNDdgvdegicletnsgtekisksglekNSLIYE 462
Cdd:cd02661 226 ISFPETLDLSPY-----------------------------MSQ--PND-------------------------GPLKYK 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722210838 463 LFSVMVHSG-SAAGGHYYACIKSfSDEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIY 535
Cdd:cd02661 250 LYAVLVHSGfSPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETV-------------------LSQKAYILFY 303
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-536 |
1.19e-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: 170.75 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKweFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDvtrSFGWDSSEAW 242
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD---YFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 243 ----QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygssqAFASVE 318
Cdd:cd02664 76 ftpgSQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---------SFPSVQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 319 EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMStfidVE 398
Cdd:cd02664 138 DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLP----VR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 399 DEkspqTESCTDSGAENEGschsdqmsndfsnDDGVDEGICLETnsgtekisksgleknsLIYELFSVMVHSG-SAAGGH 477
Cdd:cd02664 214 VE----SKSSESPLEKKEE-------------ESGDDGELVTRQ----------------VHYRLYAVVVHSGySSESGH 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722210838 478 YY--------------ACIKSFSDEQ------WYSFNDQHVSRITQEDIKKThggssgsrgyysSAFASSTNAYMLIYR 536
Cdd:cd02664 261 YFtyardqtdadstgqECPEPKDAEEndesknWYLFNDSRVTFSSFESVQNV------------TSRFPKDTPYILFYE 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
243-536 |
1.30e-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: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 243 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASVEEALH 322
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS---------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 323 AFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMhrIKLNDRMTFP-EELDMSTFIDVEDEK 401
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVDTRSFT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 402 SPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknsliYELFSVMVHSGSAAGGHYYAC 481
Cdd:cd02674 170 GPFK-------------------------------------------------------YDLYAVVNHYGSLNGGHYTAY 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1722210838 482 IKSFSDEQWYSFNDQHVSRITQEDIKkthggssgsrgyyssafasSTNAYMLIYR 536
Cdd:cd02674 195 CKNNETNDWYKFDDSRVTKVSESSVV-------------------SSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-535 |
1.67e-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: 120.94 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNALY--KWEFEESEEDPVTSIPYQLQRLFVLLQTSKKRaiettdvtRSFG----- 235
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLsdRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--------SPYGpinll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 236 ---WDSS---EAWQQHDVQELCRVMFDALEQKWK--QTEQAD------LINELYQGKLKDYVRCLECGYEGWRIDTYLDI 301
Cdd:cd02660 74 ylsWKHSrnlAGYSQQDAHEFFQFLLDQLHTHYGgdKNEANDeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 302 PLVIRPYGSS---------QAFASVEEALHAFIQPEILdGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYT 372
Cdd:cd02660 154 SLDIPNKSTPswalgesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 373 TMHRiKLNDRMTFPEELDMSTFIDVedekspqtesctdsgaenegSCHSDQMSNDFSNDdgvdegicletnsgtekisks 452
Cdd:cd02660 233 KTSR-KIDTYVQFPLELNMTPYTSS--------------------SIGDTQDSNSLDPD--------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 453 gleknsLIYELFSVMVHSGSAAGGHYYACIKsFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssafassTNAYM 532
Cdd:cd02660 271 ------YTYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRVSEEEVLK-------------------SQAYL 324
|
...
gi 1722210838 533 LIY 535
Cdd:cd02660 325 LFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-536 |
2.55e-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: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNALykwefeesEEDPVTsipyqlqrlfvLLQTSKKRAIETTDvtrsfgwdsseaW 242
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL--------SETPKE-----------LFSQVCRKAPQFKG------------Y 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 243 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAfaSVEEALH 322
Cdd:cd02667 50 QQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSEC--SIESCLK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 323 AFIQPEILDGPNQYFCERCKKkcdARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELDMSTFIDVedeks 402
Cdd:cd02667 119 QFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAPFCDP----- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 403 pqtesctdsgaenegSCHSDQmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYACI 482
Cdd:cd02667 190 ---------------KCNSSE-------------------------------DKSSVLYRLYGVVEHSGTMRSGHYVAYV 223
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722210838 483 KS---------------FSDE------QWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIYR 536
Cdd:cd02667 224 KVrppqqrlsdltkskpAADEagpgsgQWYYISDSDVREVSLEEV-------------------LKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-535 |
1.73e-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: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFmtpeFRNALYkwefeeSEEDPVTSIPYQLQRLFVLlqtSKKRAIETTDVTRSFgWDSSeaw 242
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLT------CLKDLFESISEQKKRTGVI---SPKKFITRLKRENEL-FDNY--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 243 QQHDVQE----LCRVMFDALEQKWKQTE-------------QADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 305
Cdd:cd02663 64 MHQDAHEflnfLLNEIAEILDAERKAEKanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 306 RPYgssqafASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTF 385
Cdd:cd02663 144 EQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 386 PEELDMStfidvedekspqteSCTDsgaenegschsdqmsnDFSNDDgvdegicletnsgtekisksgleknsLIYELFS 465
Cdd:cd02663 218 PLELRLF--------------NTTD----------------DAENPD--------------------------RLYELVA 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722210838 466 VMVHSGSAAG-GHYYACIKsfSDEQWYSFNDQHVSRITQEDIKKTHGGSsgsrgyyssafASSTNAYMLIY 535
Cdd:cd02663 242 VVVHIGGGPNhGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFFGDS-----------PNQATAYVLFY 299
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
161-505 |
3.28e-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: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 161 YVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPVTSIPYQLQRLF--VLLQTSKKRAIETT-DVTRSFgwd 237
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYndELANQAPRRLLNALrEVNPMY--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 238 ssEAWQQHDVQELCRVMFDALEqkwkqteqaDLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASV 317
Cdd:cd02671 101 --EGYLQHDAQEVLQCILGNIQ---------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 318 E-------------EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRI----KLN 380
Cdd:cd02671 170 EispdpktemktlkWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 381 DRMTFPEELdmstfidvedekspqtesctdsgaenegSCH--SDQMSNDfsnddgvdegicletnsgtekisksglekns 458
Cdd:cd02671 250 TPLLTPLKL----------------------------SLEewSTKPKND------------------------------- 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1722210838 459 lIYELFSVMVHSG-SAAGGHYYACIKsfsdeqWYSFNDQHVSRITQED 505
Cdd:cd02671 271 -VYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-510 |
1.60e-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: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRL---FVLLQTSKKRAIETTDVT------ 231
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkFPSDVVDPANDLNCQLIKLadgLLSGRYSKPASLKSENDPyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 232 -RSF----GWDSSE--AWQQHDVQELCRVMFDALEQKWKQTEQADlINELYQGKLKDYVRCLECGYEGW--RIDTYLDIP 302
Cdd:cd02658 81 pSMFkaliGKGHPEfsTMRQQDALEFLLHLIDKLDRESFKNLGLN-PNDLFKFMIEDRLECLSCKKVKYtsELSEILSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 303 LVIRPYGSSQAFASV------EEALHAFIQPEildgPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDF--DYTtm 374
Cdd:cd02658 160 VPKDEATEKEEGELVyepvplEDCLKAYFAPE----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 375 hriklndrmtfPEELDMStfIDVEDEKSPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgl 454
Cdd:cd02658 234 -----------PKKLDVP--IDVPEELGPGK------------------------------------------------- 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1722210838 455 eknsliYELFSVMVHSG-SAAGGHYYACIKSFSDE--QWYSFNDQHVSRITQEDIKKTH 510
Cdd:cd02658 252 ------YELIAFISHKGtSVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKL 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-509 |
1.47e-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: 81.99 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRNAL--YKWEFEESEE--DPVTSipyQLQRLFVLLQTSKKRA--IETTDVTR---- 232
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQssDNLTN---ALRDLFDTMDKKQEPVppIEFLQLLRmafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 233 SFGWDSSEA-WQQHDVQELCRVMFDALEQKWK-QTEQADLINELYQGKLKDYVRCLEcgyegwridtyldIPLVIRPYGS 310
Cdd:cd02657 78 QFAEKQNQGgYAQQDAEECWSQLLSVLSQKLPgAGSKGSFIDQLFGIELETKMKCTE-------------SPDEEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 311 SQAFASveeaLHAFIQPEI---LDGPNQYFCERCKKKCDAR-------KGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLN 380
Cdd:cd02657 145 SEYKLQ----CHISITTEVnylQDGLKKGLEEEIEKHSPTLgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 381 DRMTFPEELDMSTFidvedekspqtesCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknslI 460
Cdd:cd02657 221 RKVKFPFELDLYEL-------------CTPSG-----------------------------------------------Y 240
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1722210838 461 YELFSVMVHSG-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKT 509
Cdd:cd02657 241 YELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKL 290
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-535 |
6.42e-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: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTLFMTPEFRnalykwEFeeseedpvtsipyqLQRLFvllqtskkraiettdvtrsfgwdsseaw 242
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLI------EY--------------LEEFL---------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 243 QQHDVQELCRVMFDALEQKWKQteqadlineLYQGKLKDYVRCLECGY-EGWRIDTYLDIPLVIrPYGSSQAFASVEEAL 321
Cdd:cd02662 33 EQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGEsSKVRYESFTMLSLPV-PNQSSGSGTTLEHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 322 HAFIQPEILDGpnqYFCERCKKKcdarkglrFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELdmstfidvedek 401
Cdd:cd02662 103 DDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRGTST-KNSCKVSFPERL------------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 402 spqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHSGSAAGGHY--- 478
Cdd:cd02662 159 -------------------------------------------------------PKVLYRLRAVVVHYGSHSSGHYvcy 183
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722210838 479 --------YACIKSFS---------DEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafASSTNAYMLIY 535
Cdd:cd02662 184 rrkplfskDKEPGSFVrmregpsstSHPWWRISDTTVKEVSESEV------------------LEQKSAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
162-506 |
6.04e-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: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 162 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYkwEFEESEEDPVTSIP----------------------YQLQRLFVLLQT 219
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPterriggrevsrselqrsnqfvYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 220 SKKRAIETTDVTrsfgwdSSEAWQQHDVQELCRVMFDALE-------------QKWKQTEQADLINELYQGKLK-DYVRC 285
Cdd:cd02666 80 SNTRSVTPSKEL------AYLALRQQDVTECIDNVLFQLEvalepisnafagpDTEDDKEQSDLIKRLFSGKTKqQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 286 LECGYEGWRIDTYLDIPLVIrPYGSSQAFASVEEalHAfiqPEILDGPNQYFCERCKKKcdarkglrflhFPYLLTLQLK 365
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLV-DVGKKGREIVVLL--EP---KDLYDALDRYFDYDSLTK-----------LPQRSQVQAQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 366 rfdfdyttmhriklNDRMTFPEELDMSTFidvEDEKSPQTESCTDSGAENEGSCHSDQMSNdfsnddgvdegiclETNSG 445
Cdd:cd02666 217 --------------LAQPLQRELISMDRY---ELPSSIDDIDELIREAIQSESSLVRQAQN--------------ELAEL 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722210838 446 TEKISKSGLEKNSLIYELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDI 506
Cdd:cd02666 266 KHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
316-538 |
3.33e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 74.53 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 316 SVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFP-EELDMSTF 394
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGV 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 395 IdvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGLEKNSLIYELFSVMVHSGSAA 474
Cdd:COG5560 754 E--------------------------------------------------------YMVDDPRLIYDLYAVDNHYGGLS 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722210838 475 GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstnAYMLIYRLK 538
Cdd:COG5560 778 GGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS-------------------AYVLFYRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
163-506 |
2.64e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 62.90 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 163 GLVNQAMTCYLNSLLQTL-FMTPEFRNALYKWEFE--------ESEEDPVTsipyQLQRLFVLlqtskkRAIETTDVTRs 233
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKElkvlknviRKPEPDLN----QEEALKLF------TALWSSKEHK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 234 FGWDSSEAwQQHDVQELCRVMFDALEqkwkqTEQADLINELYQGKLKDYVRclecgyegwriDTYLDIPLVI--RPYGSS 311
Cdd:COG5533 70 VGWIPPMG-SQEDAHELLGKLLDELK-----LDLVNSFTIRIFKTTKDKKK-----------TSTGDWFDIIieLPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 312 -QAFASVEEALHAFiQPEILDGPNQYFCERCKKKCDARKG--LRFLHFPYLLTLQLKRFDFDyttmhriklndrmtfpee 388
Cdd:COG5533 133 vNNLKTLQEFIDNM-EELVDDETGVKAKENEELEVQAKQEyeVSFVKLPKILTIQLKRFANL------------------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 389 ldmSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgVDEGICLetnsgTEKISKSGLEKNSLIYELFSVMV 468
Cdd:COG5533 194 ---GGNQKIDTE---------------------------------VDEKFEL-----PVKHDQILNIVKETYYDLVGFVL 232
|
330 340 350
....*....|....*....|....*....|....*...
gi 1722210838 469 HSGSAAGGHYYACIKsfSDEQWYSFNDQHVSRITQEDI 506
Cdd:COG5533 233 HQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEA 268
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
162-495 |
2.01e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 57.28 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 162 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDpvTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFG------ 235
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKE--HCLLCELGFLFDMLEKAKGKNCQASNFLRALSsipeas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 236 ----WDSSEAWQQHD-----VQELCRVMFDALEQKWKQTEQ-----ADLINELYQGKLKDYVRCLECGYEGWR----IDT 297
Cdd:pfam13423 79 alglLDEDRETNSAIslsslIQSFNRFLLDQLSSEENSTPPnpspaESPLEQLFGIDAETTIRCSNCGHESVResstHVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 298 YLDIPLVIRPYGSSQAFASVEEALHAFIQPEILdgpNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttmhri 377
Cdd:pfam13423 159 DLIYPRKPSSNNKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 378 kLNDRMT---FPEELDMSTFIDvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGL 454
Cdd:pfam13423 230 -RQLWKTpgwLPPEIGLTLSDD-------------------------------------------------------LQG 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1722210838 455 EKNSLIYELFSVMVH-SGSAAGGHYYACIKSFSDE-------QWYSFND 495
Cdd:pfam13423 254 DNEIVKYELRGVVVHiGDSGTSGHLVSFVKVADSEledptesQWYLFND 302
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
461-535 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722210838 461 YELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyysSAFASSTN--AYMLIY 535
Cdd:cd02665 164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVER-------------DSFGGGRNpsAYCLMY 227
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
158-305 |
2.86e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 51.81 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 158 ETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEES--EEDP------VTSIPYQL-QRLFvllqTSKKRAIETT 228
Cdd:COG5560 262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESinEENPlgmhgsVASAYADLiKQLY----DGNLHAFTPS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 229 DVTRSFGWDSSE--AWQQHDVQELCRVMFDALE------QKWKQTEQADL--------------------------INEL 274
Cdd:COG5560 338 GFKKTIGSFNEEfsGYDQQDSQEFIAFLLDGLHedlnriIKKPYTSKPDLspgddvvvkkkakecwwehlkrndsiITDL 417
|
170 180 190
....*....|....*....|....*....|.
gi 1722210838 275 YQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 305
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
807-998 |
3.21e-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: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 807 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 882
Cdd:NF033609 521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722210838 883 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 961
Cdd:NF033609 597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669
|
170 180 190
....*....|....*....|....*....|....*..
gi 1722210838 962 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 998
Cdd:NF033609 670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
|
|
| |
