|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
4.54e-108 |
|
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: 324.63 E-value: 4.54e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlghtssahtalmeefakliqtiwtsspndvvspsefktqiqrya 360
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 prfvgyNQQDAQEFLRFLLDGLHnevnrvaarpkpspesldhlpdeekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 440
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 441 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRF 518
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 519 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSS 596
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 1958794344 597 SQVRTSDAYLLFYE 610
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
280-609 |
3.16e-107 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 325.55 E-value: 3.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 280 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRL-YMRDLGHTSSAHtaLMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQR 358
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISpLSEDSRYNKDIN--LLCALRDLFKALQKNSKSSSVSPKMFKKSLGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 359 YAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVAARPKPSPesldhlpdeekgrqmwrkyleredsrIGDLFVGQLKSSLTC 438
Cdd:pfam00443 79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESL--------------------------ITDLFRGQLKSRLKC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 439 TDCGYCSTVFDPFWDLSLPIAKRGYPEVT--LMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLK 516
Cdd:pfam00443 133 LSCGEVSETFEPFSDLSLPIPGDSAELKTasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 517 RFSESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSV 591
Cdd:pfam00443 213 RFSYNRSTWEKLNTEVEFPL-ELDLSRYLAEELkpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKV 291
|
330
....*....|....*....
gi 1958794344 592 TPMS-SSQVRTSDAYLLFY 609
Cdd:pfam00443 292 TEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
281-610 |
5.22e-76 |
|
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: 242.77 E-value: 5.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlghtssahtalmeefakliqtiwtsspndvvspsefktqiqrya 360
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 prfvgyNQQDAQEFLRFLLDGLHNEVNRVAARpkpspesldhlpdeekgrqmwRKYLEREDSRIGDLFVGQLKSSLTCTD 440
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 441 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKpTCCRCRARKRCIKKFSVQRFPKILVLHLKRFS- 519
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNC-YKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 520 ESRIRTSKLTTFVNFPLRdLDLREFASENT-------NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPVTGEWHTFNDSSV 591
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLE-LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKV 231
|
330 340
....*....|....*....|....
gi 1958794344 592 TPMSSSQV-----RTSDAYLLFYE 610
Cdd:cd02257 232 TEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
280-609 |
5.45e-73 |
|
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: 236.79 E-value: 5.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 280 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKliQTIWTSSPNDVvsPSEFKTQIQRY 359
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSA--PRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 360 APRFVGYNQQDAQEFLRFLLDGLHNEvnrvaarpkpspeSLDHLPDEEKGRQmwrkyLEREDSRIGDLFVGQLKSSLTCT 439
Cdd:cd02661 78 SKHFRIGRQEDAHEFLRYLLDAMQKA-------------CLDRFKKLKAVDP-----SSQETTLVQQIFGGYLRSQVKCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 440 DCGYCSTVFDPFWDLSLPIAKRGypevTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFS 519
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 520 EsrIRTSKLTTFVNFPLRdLDLREFASENT-NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPvTGEWHTFNDSSVTPMSSS 597
Cdd:cd02661 216 N--FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIE 291
|
330
....*....|..
gi 1958794344 598 QVRTSDAYLLFY 609
Cdd:cd02661 292 TVLSQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-609 |
3.99e-62 |
|
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: 208.77 E-value: 3.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDlGHTSSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYA 360
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCT-CLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 PRFVGYNQQDAQEFLRFLLDGLHNEvnrvAARPKPSPESLDHLPdeekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 440
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTH----YGGDKNEANDESHCN-----------------CIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 441 CGYCSTVFDPFWDLSLPI-----------AKRGYPEVTLMDCMRLFTKEDVLdGDEKPTCCRCRARKRCIKKFSVQRFPK 509
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 510 ILVLHLKRFSESRIRTS-KLTTFVNFPLRdLDLREFAS----------ENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSP 578
Cdd:cd02660 219 VLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTSssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG 297
|
330 340 350
....*....|....*....|....*....|.
gi 1958794344 579 vTGEWHTFNDSSVTPMSSSQVRTSDAYLLFY 609
Cdd:cd02660 298 -DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
2.23e-58 |
|
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: 197.22 E-value: 2.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELRDyclqrlymrdlghtssahtaLMEEfakliqtiwtsspndvvSPSEFKTQIQRYA 360
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE--------------------LLSE-----------------TPKELFSQVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVaarpkpspesldhlpdeekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 440
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 441 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKptcCRCRARKRCIKKFSVQRFPKILVLHLKRFS- 519
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 520 ESRIRTSKLTTFVNFPLRdLDLREFASENTNHA------VYNLYAVSNHSGTTMGGHYTAYCRS---------------- 577
Cdd:cd02667 163 PRSANLRKVSRHVSFPEI-LDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958794344 578 -----PVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 610
Cdd:cd02667 242 adeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
278-458 |
2.97e-48 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 180.85 E-value: 2.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 278 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTS--SAHTALMEEFAKLIQTIWTSSpNDVVSPSEFKTQ 355
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplGMHGSVASAYADLIKQLYDGN-LHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 356 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVAARP---KPSPESLDHLPDEEKGRQMWRKYLEREDSRIGDLFVGQL 432
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytsKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
|
170 180
....*....|....*....|....*.
gi 1958794344 433 KSSLTCTDCGYCSTVFDPFWDLSLPI 458
Cdd:COG5560 423 KSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
278-614 |
5.15e-44 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 160.12 E-value: 5.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 278 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLiQTiwtsSPNDVVSPSEFKTQiq 357
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLALQRLFLFL-QL----SESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 358 ryapRFVG------YNQQDAQEFLRFLLDGLhnevnrvaarpkpspesldhlpdEEKgrqMwrKYLEREDSrIGDLFVGQ 431
Cdd:cd02659 74 ----RSFGwdslntFEQHDVQEFFRVLFDKL-----------------------EEK---L--KGTGQEGL-IKNLFGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 432 LKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYpeVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKIL 511
Cdd:cd02659 121 LVNYIICKECPHESEREEYFLDLQVAV--KGK--KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 512 VLHLKRF-----SESRIrtsKLTTFVNFPLRdLDLREFASENTNH------------AVYNLYAVSNHSGTTMGGHYTAY 574
Cdd:cd02659 197 TLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYTEKGLAKkegdsekkdsesYIYELHGVLVHSGDAHGGHYYSY 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794344 575 CRSPVTGEWHTFNDSSVTPMSSSQV----------------------RTSDAYLLFYELASP 614
Cdd:cd02659 273 IKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
2.96e-37 |
|
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: 140.52 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELrdYCLqrlymRDLGHTSSAHTALMeefakliqtiwtsspnDVVSPSEFKTQIQRYA 360
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL--TCL-----KDLFESISEQKKRT----------------GVISPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 PRFVGYNQQDAQEFLRFLLdglhNEVNR-VAARPKPSPESLDHLPDEEKGRQ-MWrkyleredsrIGDLFVGQLKSSLTC 438
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLL----NEIAEiLDAERKAEKANRKLNNNNNAEPQpTW----------VHEIFQGILTNETRC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 439 TDCGYCSTVFDPFWDLSLPIakrgYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRF 518
Cdd:cd02663 124 LTCETVSSRDETFLDLSIDV----EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 519 --SESRIRTSKLTTFVNFPlrdLDLREFASENTNHAV---YNLYAVSNHSGTT-MGGHYTAYCRSpvTGEWHTFNDSSVT 592
Cdd:cd02663 200 kyDEQLNRYIKLFYRVVFP---LELRLFNTTDDAENPdrlYELVAVVVHIGGGpNHGHYVSIVKS--HGGWLLFDDETVE 274
|
330 340
....*....|....*....|....*.
gi 1958794344 593 PMSSSQV-------RTSD-AYLLFYE 610
Cdd:cd02663 275 KIDENAVeeffgdsPNQAtAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
2.23e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 136.01 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLIQ-----TIWTSSPNDVVSPSEFKTq 355
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQlqlifAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 356 iqryAPRFVGYNQQDAQEFLRFLLDGLHNEvnrvaarpkpspesLDHLPDEeKGRQMwrkyleredsrIGDLFVGQLKSS 435
Cdd:cd02668 80 ----ALGLDTGQQQDAQEFSKLFLSLLEAK--------------LSKSKNP-DLKNI-----------VQDLFRGEYSYV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 436 LTCTDCGYCSTVFDPFWDLSLPIAKrgypEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHL 515
Cdd:cd02668 130 TQCSKCGRESSLPSKFYELELQLKG----HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 516 KRFSESRIRTS--KLTTFVNFPLrDLDLREF-ASENTNHAVYNLYAVSNHSGT-TMGGHYTAYCRSPVTGEWHTFNDSSV 591
Cdd:cd02668 206 LRFVFDRKTGAkkKLNASISFPE-ILDMGEYlAESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958794344 592 TPMSSSQVR---------------------TSDAYLLFYE 610
Cdd:cd02668 285 EEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
3.78e-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 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: 132.07 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELRDYCLQrlYMRDLGHTSSAHTALMEEFAKLIQTIWTSSpnDVVSPSEFKTQIQRYA 360
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN--YNPARRGANQSSDNLTNALRDLFDTMDKKQ--EPVPPIEFLQLLRMAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 PRFV------GYNQQDAQEFLRFLLDGLHNEVnrvaarpkpspesldhlpdeekgrqmwrKYLEREDSRIGDLFVGQLKS 434
Cdd:cd02657 77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGIELET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 435 SLTCTDCGYCSTV-FDPFWDLSLPIAkrgypevTLMDCMRLFTK-EDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILV 512
Cdd:cd02657 129 KMKCTESPDEEEVsTESEYKLQCHIS-------ITTEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 513 LHLKRFS--ESRIRTSKLTTFVNFPLrDLDLREFAsenTNHAVYNLYAVSNHSGTTM-GGHYTAYCRSPVTGEWHTFNDS 589
Cdd:cd02657 202 VQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDD 277
|
330 340
....*....|....*....|....*...
gi 1958794344 590 SVTPMSSSQVRTSD-------AYLLFYE 610
Cdd:cd02657 278 KVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
236-610 |
5.26e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 125.89 E-value: 5.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 236 VLSPTYrpsgrytlwekNKGQASGPSRSTSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLqrLYMR 315
Cdd:cd02669 87 VLNPTY-----------TKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--LYEN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 316 DLGHTSSAhTALMEEFAKLIQTIWtsSPND---VVSPSEFKTQIQRYAPRFVGYNQQ-DAQEFLRFLLDGLHNEVNrvaa 391
Cdd:cd02669 154 YENIKDRK-SELVKRLSELIRKIW--NPRNfkgHVSPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLG---- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 392 RPKPSPESLDHlpDEEKG--RQMWRKYLEREDSrigdlfvgqLKSSLTCTDCGYCSTVFD-PFWDLSL-----PIAKRGY 463
Cdd:cd02669 227 GSKKPNSSIIH--DCFQGkvQIETQKIKPHAEE---------EGSKDKFFKDSRVKKTSVsPFLLLTLdlpppPLFKDGN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 464 -----PEVTLMDcmrLFTKedvLDGDEKPTccrcraRKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRD 538
Cdd:cd02669 296 eeniiPQVPLKQ---LLKK---YDGKTETE------LKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKN 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794344 539 LDLREFASENTN----HAVYNLYAVSNHSGTTMG-GHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 610
Cdd:cd02669 364 LDLSDYVHFDKPslnlSTKYNLVANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
260-609 |
7.87e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 120.38 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 260 PSRSTSP-GRDTMNSksaqgLAGLRNLGNTCFMNSILQCLSntrelrdYC------LQRLYmrDLGHTSSAHTALMEEFA 332
Cdd:cd02671 9 PSSATSCeKRENLLP-----FVGLNNLGNTCYLNSVLQVLY-------FCpgfkhgLKHLV--SLISSVEQLQSSFLLNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 333 KLIQTIWTSSPndvvsPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvaarpkpspesldhlpdeekgrqm 412
Cdd:cd02671 75 EKYNDELANQA-----PRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 413 wrkyleredsrigdLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEV---------------TLMDCMRLFTK 477
Cdd:cd02671 126 --------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFAS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 478 EDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRT------SKLTTFVNFPLrDLDLREFASENTNH 551
Cdd:cd02671 192 VERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL-KLSLEEWSTKPKND 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794344 552 aVYNLYAVSNHSGTTMG-GHYTAYCRspvtgeWHTFNDSSVTPM---------SSSQVRTSDAYLLFY 609
Cdd:cd02671 271 -VYRLFAVVMHSGATISsGHYTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
281-610 |
5.58e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 113.74 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLS-NTRELRDYCLQRLY-MRDL--GHTSSAHTALMEEFAKLIQTIWTSspndvvspsefktQI 356
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKeLKVLknVIRKPEPDLNQEEALKLFTALWSS-------------KE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 357 QRYAPRFVGYNQQDAQEFLRFLLDGLHNE-VNRVAARPKPSpesldhLPDEEKgrqmwrkyleredSRIGDLFvgqlksS 435
Cdd:COG5533 68 HKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIRIFKT------TKDKKK-------------TSTGDWF------D 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 436 LTctdcgycstvfdpfwdLSLPIAKRGYPEVTLMDCmrlFTKEDVLDGDEKPTCCRCRARKRCIKK----FSVQRFPKIL 511
Cdd:COG5533 123 II----------------IELPDQTWVNNLKTLQEF---IDNMEELVDDETGVKAKENEELEVQAKqeyeVSFVKLPKIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 512 VLHLKRFSESrIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRspVTGEWHTFNDSSV 591
Cdd:COG5533 184 TIQLKRFANL-GGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDV 260
|
330 340
....*....|....*....|..
gi 1958794344 592 TPMSSSQVRTSD---AYLLFYE 610
Cdd:COG5533 261 TPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
5.68e-28 |
|
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: 114.34 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELrdyclQRLYMRDLGHTSSA----HTALMEEFAKLIQTIWT---SSPNDVVS----- 348
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSF-----QWRYDDLENKFPSDvvdpANDLNCQLIKLADGLLSgrySKPASLKSendpy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 349 -----PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvaarpkpspesldhlpdeekgrqmwrkyleREDSR 423
Cdd:cd02658 76 qvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK------------------------------NLGLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 424 IGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPI----------AKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR 493
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 494 ArkrcIKKFSVQRFPKILVLHLKRFsesrirtsklTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT-TMGGHYT 572
Cdd:cd02658 206 A----TKTTGFKTFPDYLVINMKRF----------QLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTsVHSGHYV 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958794344 573 AYCRSPVTGE--WHTFNDSSVTPMSSSQVRTSDAYLLFYE 610
Cdd:cd02658 272 AHIKKEIDGEgkWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
5.01e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 109.76 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYmrdlghtssahtalmeefakliqtiwtsspndvvspsefktqiqrya 360
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-LEEFL----------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 361 prfvgyNQQDAQEFLRFLLDGLHNEVnrvaarpkpspesldhlpdeekgrqmwrkyleredsriGDLFVGQLKSSLTCTD 440
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------------------------------------KFPFDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 441 CGYCSTV-FDPFWDLSLPI-AKRGYPEVTLMDCMRLFTKEDVLDGdekptccrcraRKRCIKKFSVQRFPKILVLHLKRF 518
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD-----------YKCDRCQTVIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 519 SESRIRTS-KLTTFVNFPLRdldlrefasenTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPV------------------ 579
Cdd:cd02662 138 VFDGRGTStKNSCKVSFPER-----------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLfskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 1958794344 580 --TGEWHTFNDSSVTPMSSSQVR-TSDAYLLFYE 610
Cdd:cd02662 207 stSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
1.27e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 111.04 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 281 GLRNLGNTCFMNSILQCLSNTRELRdYCLQRLYMRDLGHTSSAHTALMEEFAKLIQT--IWTSSPNDVVSPSefktqiqr 358
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFR-RQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTqrRAEAPPDYFLEAS-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 359 YAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVaarpkpspesldhlpdeekgrqmwrkyleredsrigdlFVGQLKSSLTC 438
Cdd:cd02664 72 RPPWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRC 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 439 TDCGYCSTVFD--PFWDLSLPiakrgypevTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLK 516
Cdd:cd02664 114 LNCNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 517 RFS---ESRIRTsKLTTFVNFPLrDLDL--------------------REFASENTNHAVYNLYAVSNHSGTTM-GGHYT 572
Cdd:cd02664 185 RFSydqKTHVRE-KIMDNVSINE-VLSLpvrveskssesplekkeeesGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYF 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794344 573 AYCRSPVTGE--------------------WHTFNDSSVTPMSSSQV-------RTSDAYLLFYE 610
Cdd:cd02664 263 TYARDQTDADstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
272-599 |
6.82e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 110.35 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 272 NSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHtALMEEFAKLiQTIwtsspNDVVSPSE 351
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVAL-ALQRLFYNL-QTG-----EEPVDTTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 352 FKTQIQRYAprFVGYNQQDAQEFLRFLLDGLHNEvnrvaarpkpspesldhlpdeekgrqmwRKYLEREDSrIGDLFVGQ 431
Cdd:COG5077 259 LTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKS----------------------------MRGTVVENA-LNGIFVGK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 432 LKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYPevTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCiKKFSVQRFPKIL 511
Cdd:COG5077 308 MKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGDNRYNAEKHGLQDAK-KGVIFESLPPVL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 512 VLHLKRFSESRIRTS--KLTTFVNFPLrDLDLREF------ASENTNHaVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEW 583
Cdd:COG5077 383 HLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFldrdadKSENSDA-VYVLYGVLVHSGDLHEGHYYALLKPEKDGRW 460
|
330
....*....|....*.
gi 1958794344 584 HTFNDSSVTPMSSSQV 599
Cdd:COG5077 461 YKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-610 |
2.92e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 72.95 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 282 LRNLGNTCFMNSILQCLSNTRELRdyclqrlymrdlghtssahtalmEEFAkliqtiwtsspNDvvspsefktqiqryap 361
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKIN-----------------------TEFD-----------ND---------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 362 rfvgyNQQDAQEFLRFLLDGLHNEVNRVAARPKPSPESLDHLPDEEKgrqmwrkyleredsrigdlFVGQLKSSLTCTDC 441
Cdd:cd02673 32 -----DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEA-------------------FKYTIESSYVCIGC 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 442 GYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDvldgdEKPTCCRCRARKRCIKKFSvqRFPKILVLHLKRFsES 521
Cdd:cd02673 88 SFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EKDCSSCKCESAISSERIM--TFPECLSINLKRY-KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 522 RIRTSKLttfvnfpLRD--LDLREFASEntnHAVYNLYAVSNHSG-TTMGGHYTAYCRSPVTG-EWHTFNDSSVTPMSSS 597
Cdd:cd02673 160 RIATSDY-------LKKneEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
|
330
....*....|....*.
gi 1958794344 598 QVR---TSDAYLLFYE 610
Cdd:cd02673 230 DVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
280-609 |
1.55e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 62.89 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 280 AGLRNLGNTCFMNSILQCLSNTRELRDYCL---------------------QRLYMRDLGHTSSAHTALMEEFAKLIqti 338
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLnfdeskaelasdypterriggREVSRSELQRSNQFVYELRSLFNDLI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 339 wtSSPNDVVSPSefktqiQRYAprFVGYNQQDAQEFLRFLLDGLH-NEVNRVAARPKPSPESLDHLPDEEKGrqmwrkyl 417
Cdd:cd02666 79 --HSNTRSVTPS------KELA--YLALRQQDVTECIDNVLFQLEvALEPISNAFAGPDTEDDKEQSDLIKR-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 418 eredsrigdLFVGQLKSSLTCTDCGYCSTVFDP---FWDLSLPIAKRGYPEVT------LMDCM-RLFTKEDVLDGDEKP 487
Cdd:cd02666 141 ---------LFSGKTKQQLVPESMGNQPSVRTKterFLSLLVDVGKKGREIVVllepkdLYDALdRYFDYDSLTKLPQRS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 488 TCCRCRARKRCIKKFSVQRF-PKILVLHLKRFSESRIRT-SKLTTFVNFPLRDLD-LREFASENTNHAVYNLYAVSNHSG 564
Cdd:cd02666 212 QVQAQLAQPLQRELISMDRYeLPSSIDDIDELIREAIQSeSSLVRQAQNELAELKhEIEKQFDDLKSYGYRLHAVFIHRG 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958794344 565 TTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQV----RTSDA--YLLFY 609
Cdd:cd02666 292 EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftLGNTAtpYFLVY 342
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
368-609 |
1.59e-09 |
|
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: 58.34 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 368 QQDAQEFLRFLLDGLHNEVNRVAARPKPSPESLDHLPDEEKGRQMWRKYLERedsrigdlfvgqlKSSLTCTDCGycstv 447
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG-------------KPFCNCETFG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 448 fdpfwdlSLPIAKRGYPEvtLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKkfsvqrFPKILVLHLKRFSESRIRTSK 527
Cdd:cd02665 84 -------QYPLQVNGYGN--LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 528 LTTFVNFPlrdldlREFASENtnhavYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQV-------- 599
Cdd:cd02665 149 IHDKLEFP------QIIQQVP-----YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfggg 217
|
250
....*....|
gi 1958794344 600 RTSDAYLLFY 609
Cdd:cd02665 218 RNPSAYCLMY 227
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
280-591 |
2.03e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 59.21 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 280 AGLRNLGNTCFMNSILQCLSNTRELR-------------DYCL--QRLY---M---------------RDLGHTSSAHT- 325
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCLlcELGFlfdMlekakgkncqasnflRALSSIPEASAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 326 ALMEEFAkliqtiwtsSPNDVVSPSefkTQIQRyaprfvgynqqdaqeFLRFLLDGLHNEVNRVAARPKPSPESLDhlpd 405
Cdd:pfam13423 81 GLLDEDR---------ETNSAISLS---SLIQS---------------FNRFLLDQLSSEENSTPPNPSPAESPLE---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 406 eekgrqmwrkyleredsrigDLFVGQLKSSLTCTDCGYCST------VFDpfwdLSLPIAK----RGYPEVTLMDCMRLF 475
Cdd:pfam13423 130 --------------------QLFGIDAETTIRCSNCGHESVressthVLD----LIYPRKPssnnKKPPNQTFSSILKSS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 476 TKEDVLdgdEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFvnFPLR-DLDLREFASENTNHAVY 554
Cdd:pfam13423 186 LERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEiGLTLSDDLQGDNEIVKY 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958794344 555 NLYA-VSNHSGTTMGGHYTAYCR-------SPVTGEWHTFNDSSV 591
Cdd:pfam13423 261 ELRGvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
501-610 |
2.91e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 45.97 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794344 501 KFSVQRFPKI----LVLHLKRFSESR-------IRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYA-VSNHSGTTMG 568
Cdd:cd02672 149 TTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGyVCEINDSSRG 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958794344 569 GHYTA----YCRSPVTGEWHTFNDSSVTPMSssqvrtSDAYLLFYE 610
Cdd:cd02672 229 QHNVVfvikVNEESTHGRWYLFNDFLVTPVS------ELAYILLYQ 268
|
|
| |
