|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
1.74e-107 |
|
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: 323.09 E-value: 1.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlghtssahtalmeefakliqtiwtsspndvvspsefktqiqrya 361
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 prfmgyNQQDAQEFLRFLLDGLHnevnrvaarpkaspetldhlpdeekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 441
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 442 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRF 519
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 520 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSS 597
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 114052502 598 SQVRTSDAYLLFYE 611
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
281-610 |
1.80e-106 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 323.63 E-value: 1.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 281 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRL-YMRDLGHTSSAHtaLMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQR 359
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISpLSEDSRYNKDIN--LLCALRDLFKALQKNSKSSSVSPKMFKKSLGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 360 YAPRFMGYNQQDAQEFLRFLLDGLHNEVNRvaarpkaspetldhlpdeekgrqmwrKYLEREDSRIGDLFVGQLKSSLTC 439
Cdd:pfam00443 79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLKC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 440 TDCGYCSTVFDPFWDLSLPIAKRGYPEVT--LMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLK 517
Cdd:pfam00443 133 LSCGEVSETFEPFSDLSLPIPGDSAELKTasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 518 RFSESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSV 592
Cdd:pfam00443 213 RFSYNRSTWEKLNTEVEFPL-ELDLSRYLAEELkpktnNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKV 291
|
330
....*....|....*....
gi 114052502 593 TPMS-SSQVRTSDAYLLFY 610
Cdd:pfam00443 292 TEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
282-611 |
7.58e-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: 242.39 E-value: 7.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlghtssahtalmeefakliqtiwtsspndvvspsefktqiqrya 361
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 prfmgyNQQDAQEFLRFLLDGLHNEVNRVAARpkaspetldhlpdeekgrqmwRKYLEREDSRIGDLFVGQLKSSLTCTD 441
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 442 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDILDGDEKpTCCRCRARKRCIKKFSVQRFPKILVLHLKRFS- 520
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNC-YKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 521 ESRIRTSKLTTFVNFPLRdLDLREFASENT-------NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPVTGEWHTFNDSSV 592
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLE-LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKV 231
|
330 340
....*....|....*....|....
gi 114052502 593 TPMSSSQV-----RTSDAYLLFYE 611
Cdd:cd02257 232 TEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
6.71e-74 |
|
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: 239.10 E-value: 6.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 281 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKliQTIWTSSPNDVvsPSEFKTQIQRY 360
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSA--PRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 361 APRFMGYNQQDAQEFLRFLLDGLHNevnrvAARPKASPETLDHLPDeekgrqmwrkyleREDSRIGDLFVGQLKSSLTCT 440
Cdd:cd02661 78 SKHFRIGRQEDAHEFLRYLLDAMQK-----ACLDRFKKLKAVDPSS-------------QETTLVQQIFGGYLRSQVKCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 441 DCGYCSTVFDPFWDLSLPIAKRGypevTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFS 520
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 521 EsrIRTSKLTTFVNFPLRdLDLREFASENT-NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPvTGEWHTFNDSSVTPMSSS 598
Cdd:cd02661 216 N--FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIE 291
|
330
....*....|..
gi 114052502 599 QVRTSDAYLLFY 610
Cdd:cd02661 292 TVLSQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-610 |
9.23e-61 |
|
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: 205.30 E-value: 9.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDlGHTSSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYA 361
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCT-CLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 PRFMGYNQQDAQEFLRFLLDGLHNEvnrvAARPKASPETLDHLPdeekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 441
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTH----YGGDKNEANDESHCN-----------------CIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 442 CGYCSTVFDPFWDLSLPI-----------AKRGYPEVTLMDCMRLFTKEDILdGDEKPTCCRCRARKRCIKKFSVQRFPK 510
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 511 ILVLHLKRFSESRIRTS-KLTTFVNFPLRdLDLREFAS----------ENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSP 579
Cdd:cd02660 219 VLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTSssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG 297
|
330 340 350
....*....|....*....|....*....|.
gi 114052502 580 vTGEWHTFNDSSVTPMSSSQVRTSDAYLLFY 610
Cdd:cd02660 298 -DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
7.43e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 198.38 E-value: 7.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELRDyclqrlymrdlghtssahtaLMEEfakliqtiwtsspndvvSPSEFKTQIQRYA 361
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE--------------------LLSE-----------------TPKELFSQVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 PRFMGYNQQDAQEFLRFLLDGLHNEVNRVaarpkaspetldhlpdeekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 441
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 442 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDILDGDEKptcCRCRARKRCIKKFSVQRFPKILVLHLKRFS- 520
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 521 ESRIRTSKLTTFVNFPLRdLDLREFASENTNHA------VYNLYAVSNHSGTTMGGHYTAYCRS---------------- 578
Cdd:cd02667 163 PRSANLRKVSRHVSFPEI-LDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 114052502 579 -----PVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 611
Cdd:cd02667 242 adeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
279-459 |
4.11e-47 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 177.77 E-value: 4.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 279 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTS--SAHTALMEEFAKLIQTIWTSSpNDVVSPSEFKTQ 356
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplGMHGSVASAYADLIKQLYDGN-LHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 357 IQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRVAARPKASPETL---DHLPDEEKGRQMWRKYLEREDSRIGDLFVGQL 433
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLspgDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
|
170 180
....*....|....*....|....*.
gi 114052502 434 KSSLTCTDCGYCSTVFDPFWDLSLPI 459
Cdd:COG5560 423 KSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-615 |
3.55e-45 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 163.58 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 279 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLiQTiwtsSPNDVVSPSEFKTQiq 358
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLALQRLFLFL-QL----SESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 359 ryapRFMG------YNQQDAQEFLRFLLDGLhnevnrvaarpkaspetldhlpdEEKgrqMwrKYLEREDSrIGDLFVGQ 432
Cdd:cd02659 74 ----RSFGwdslntFEQHDVQEFFRVLFDKL-----------------------EEK---L--KGTGQEGL-IKNLFGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 433 LKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYpeVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKIL 512
Cdd:cd02659 121 LVNYIICKECPHESEREEYFLDLQVAV--KGK--KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 513 VLHLKRF-----SESRIrtsKLTTFVNFPLRdLDLREFASENTNH------------AVYNLYAVSNHSGTTMGGHYTAY 575
Cdd:cd02659 197 TLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYTEKGLAKkegdsekkdsesYIYELHGVLVHSGDAHGGHYYSY 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114052502 576 CRSPVTGEWHTFNDSSVTPMSSSQV----------------------RTSDAYLLFYELASP 615
Cdd:cd02659 273 IKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
1.14e-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: 141.68 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELrdYCLqrlymRDLGHTSSAHTALMeefakliqtiwtsspnDVVSPSEFKTQIQRYA 361
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLL--TCL-----KDLFESISEQKKRT----------------GVISPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 PRFMGYNQQDAQEFLRFLLdglhNEVNR-VAARPKASPETLDHLPDEEKGRQ-MWrkyleredsrIGDLFVGQLKSSLTC 439
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLL----NEIAEiLDAERKAEKANRKLNNNNNAEPQpTW----------VHEIFQGILTNETRC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 440 TDCGYCSTVFDPFWDLSLPIakrgYPEVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRF 519
Cdd:cd02663 124 LTCETVSSRDETFLDLSIDV----EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 520 --SESRIRTSKLTTFVNFPlrdLDLREFASENTNHAV---YNLYAVSNHSGTT-MGGHYTAYCRSpvTGEWHTFNDSSVT 593
Cdd:cd02663 200 kyDEQLNRYIKLFYRVVFP---LELRLFNTTDDAENPdrlYELVAVVVHIGGGpNHGHYVSIVKS--HGGWLLFDDETVE 274
|
330 340
....*....|....*....|....*.
gi 114052502 594 PMSSSQV-------RTSD-AYLLFYE 611
Cdd:cd02663 275 KIDENAVeeffgdsPNQAtAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
8.81e-36 |
|
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: 137.17 E-value: 8.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLIQ-----TIWTSSPNDVVSPSEFKTq 356
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQlqlifAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 357 iqryAPRFMGYNQQDAQEFLRFLLDGLHNevnrvaarpkaspeTLDHLPDEeKGRQMwrkyleredsrIGDLFVGQLKSS 436
Cdd:cd02668 80 ----ALGLDTGQQQDAQEFSKLFLSLLEA--------------KLSKSKNP-DLKNI-----------VQDLFRGEYSYV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 437 LTCTDCGYCSTVFDPFWDLSLPIAKrgypEVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHL 516
Cdd:cd02668 130 TQCSKCGRESSLPSKFYELELQLKG----HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 517 KRFSESRIRTS--KLTTFVNFPLrDLDLREF-ASENTNHAVYNLYAVSNHSGT-TMGGHYTAYCRSPVTGEWHTFNDSSV 592
Cdd:cd02668 206 LRFVFDRKTGAkkKLNASISFPE-ILDMGEYlAESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 114052502 593 TPMSSSQVR---------------------TSDAYLLFYE 611
Cdd:cd02668 285 EEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
8.51e-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: 130.91 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELRDYCLQrlYMRDLGHTSSAHTALMEEFAKLIQTIWTSSpnDVVSPSEFKTQIQRYA 361
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN--YNPARRGANQSSDNLTNALRDLFDTMDKKQ--EPVPPIEFLQLLRMAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 PRFM------GYNQQDAQEFLRFLLDGLHNEVnrvaarpkaspetldhlpdeekgrqmwrKYLEREDSRIGDLFVGQLKS 435
Cdd:cd02657 77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGIELET 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 436 SLTCTDCGYCSTV-FDPFWDLSLPIAkrgypevTLMDCMRLFTK-EDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILV 513
Cdd:cd02657 129 KMKCTESPDEEEVsTESEYKLQCHIS-------ITTEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 514 LHLKRFS--ESRIRTSKLTTFVNFPLrDLDLREFAsenTNHAVYNLYAVSNHSGTTM-GGHYTAYCRSPVTGEWHTFNDS 590
Cdd:cd02657 202 VQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDD 277
|
330 340
....*....|....*....|....*...
gi 114052502 591 SVTPMSSSQVRTSD-------AYLLFYE 611
Cdd:cd02657 278 KVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
280-610 |
1.63e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 119.61 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 280 LAGLRNLGNTCFMNSILQCLSntrelrdYC------LQRLYmrDLGHTSSAHTALMEEFAKLIQTIWTSSPndvvsPSEF 353
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLY-------FCpgfkhgLKHLV--SLISSVEQLQSSFLLNPEKYNDELANQA-----PRRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 354 KTQIQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRvaarpkaspetldhlpdeekgrqmwrkyleredsrigdLFVGQL 433
Cdd:cd02671 90 LNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------------------DFQGQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 434 KSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEV---------------TLMDCMRLFTKEDILDGDEKPTCCRCRARKR 498
Cdd:cd02671 132 VLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 499 CIKKFSVQRFPKILVLHLKRFSESRIRT------SKLTTFVNFPLrDLDLREFASENTNHaVYNLYAVSNHSGTTMG-GH 571
Cdd:cd02671 212 AERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL-KLSLEEWSTKPKND-VYRLFAVVMHSGATISsGH 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 114052502 572 YTAYCRspvtgeWHTFNDSSVTPM---------SSSQVRTSDAYLLFY 610
Cdd:cd02671 290 YTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-611 |
5.97e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 120.12 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 270 DTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLqrLYMRDLGHTSSAhTALMEEFAKLIQTIWtsSPND--- 346
Cdd:cd02669 109 DLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--LYENYENIKDRK-SELVKRLSELIRKIW--NPRNfkg 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 347 VVSPSEFKTQIQRYAPRFMGYNQQ-DAQEFLRFLLDGLHNEVNRVAARP----------KASPETLDHLPDEEKGRQmwr 415
Cdd:cd02669 184 HVSPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSKKPNssiihdcfqgKVQIETQKIKPHAEEEGS--- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 416 KYLEREDSRigdlfvgQLKSSLTctdcgycstvfdPFWDLSL-----PIAKRGY-----PEVTLmdcmrlftkEDILDGD 485
Cdd:cd02669 261 KDKFFKDSR-------VKKTSVS------------PFLLLTLdlpppPLFKDGNeeniiPQVPL---------KQLLKKY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 486 EKPTccrCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTN----HAVYNLYAVS 561
Cdd:cd02669 313 DGKT---ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPslnlSTKYNLVANI 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 114052502 562 NHSGTTMG-GHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 611
Cdd:cd02669 390 VHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
282-611 |
2.42e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 114.90 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLS-NTRELRDYCLQRLY-MRDL--GHTSSAHTALMEEFAKLIQTIWTSspndvvspsefktQI 357
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKeLKVLknVIRKPEPDLNQEEALKLFTALWSS-------------KE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 358 QRYAPRFMGYNQQDAQEFLRFLLDGLHNevnrvaarPKASPETLD-HLPDEEKGRqmwrkyleredSRIGDLFvgqlksS 436
Cdd:COG5533 68 HKVGWIPPMGSQEDAHELLGKLLDELKL--------DLVNSFTIRiFKTTKDKKK-----------TSTGDWF------D 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 437 LTctdcgycstvfdpfwdLSLPIAKRGYPEVTLMDCmrlFTKEDILDGDEKPTCCRCRARKRCIKK----FSVQRFPKIL 512
Cdd:COG5533 123 II----------------IELPDQTWVNNLKTLQEF---IDNMEELVDDETGVKAKENEELEVQAKqeyeVSFVKLPKIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 513 VLHLKRFSESrIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRspVTGEWHTFNDSSV 592
Cdd:COG5533 184 TIQLKRFANL-GGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDV 260
|
330 340
....*....|....*....|..
gi 114052502 593 TPMSSSQVRTSD---AYLLFYE 611
Cdd:COG5533 261 TPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
4.26e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 112.84 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYmrdlghtssahtalmeefakliqtiwtsspndvvspsefktqiqrya 361
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-LEEFL----------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 362 prfmgyNQQDAQEFLRFLLDGLHNEVnrvaarpkASPetldhlpdeekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 441
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------KFP------------------------------FDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 442 CGYCSTV-FDPFWDLSLPI-AKRGYPEVTLMDCMRLFTKEDILDGdekptccrcraRKRCIKKFSVQRFPKILVLHLKRF 519
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD-----------YKCDRCQTVIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 520 SESRIRTS-KLTTFVNFPLRdldlrefasenTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPV------------------ 580
Cdd:cd02662 138 VFDGRGTStKNSCKVSFPER-----------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLfskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 114052502 581 --TGEWHTFNDSSVTPMSSSQVR-TSDAYLLFYE 611
Cdd:cd02662 207 stSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
1.82e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 112.80 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELrdyclQRLYMRDLGHTSSA----HTALMEEFAKLIQTIWT---SSPNDVVS----- 349
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSF-----QWRYDDLENKFPSDvvdpANDLNCQLIKLADGLLSgrySKPASLKSendpy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 350 -----PSEFKTQIQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRvaarpkaspetldhlpdeekgrqmwrkyleREDSR 424
Cdd:cd02658 76 qvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK------------------------------NLGLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 425 IGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPI----------AKRGYPEVTLMDCMRLFTKEDILDGDEKPTCCRCR 494
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 495 ArkrcIKKFSVQRFPKILVLHLKRFsesrirtsklTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT-TMGGHYT 573
Cdd:cd02658 206 A----TKTTGFKTFPDYLVINMKRF----------QLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTsVHSGHYV 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 114052502 574 AYCRSPVTGE--WHTFNDSSVTPMSSSQVRTSDAYLLFYE 611
Cdd:cd02658 272 AHIKKEIDGEgkWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
282-611 |
8.54e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 111.43 E-value: 8.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 282 GLRNLGNTCFMNSILQCLSNTRELRdYCLQRLYMRDLGHTSSAHTALMEEFAKLIQT--IWTSSPNDVVSPSefktqiqr 359
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFR-RQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTqrRAEAPPDYFLEAS-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 360 YAPRFMGYNQQDAQEFLRFLLDGLHNEVNRVaarpkaspetldhlpdeekgrqmwrkyleredsrigdlFVGQLKSSLTC 439
Cdd:cd02664 72 RPPWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRC 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 440 TDCGYCSTVFD--PFWDLSLPiakrgypevTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLK 517
Cdd:cd02664 114 LNCNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 518 RFS---ESRIRTsKLTTFVNFPL-------------------RDLDLREFASENTNHAVYNLYAVSNHSGTTM-GGHYTA 574
Cdd:cd02664 185 RFSydqKTHVRE-KIMDNVSINEvlslpvrveskssesplekKEEESGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYFT 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114052502 575 YCRSPVTGE--------------------WHTFNDSSVTPMSSSQV-------RTSDAYLLFYE 611
Cdd:cd02664 264 YARDQTDADstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
273-600 |
1.27e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 112.66 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 273 NSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHtALMEEFAKLiQTIwtsspNDVVSPSE 352
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVAL-ALQRLFYNL-QTG-----EEPVDTTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 353 F-KTQIQRYAPRFMgynQQDAQEFLRFLLDGLHNEvnrvaarpkaspetldhlpdeekgrqmwRKYLEREDSrIGDLFVG 431
Cdd:COG5077 259 LtRSFGWDSDDSFM---QHDIQEFNRVLQDNLEKS----------------------------MRGTVVENA-LNGIFVG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 432 QLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYPevTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCiKKFSVQRFPKI 511
Cdd:COG5077 307 KMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGDNRYNAEKHGLQDAK-KGVIFESLPPV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 512 LVLHLKRFSESRIRTS--KLTTFVNFPLrDLDLREF------ASENTNHaVYNLYAVSNHSGTTMGGHYTAYCRSPVTGE 583
Cdd:COG5077 382 LHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFldrdadKSENSDA-VYVLYGVLVHSGDLHEGHYYALLKPEKDGR 459
|
330
....*....|....*..
gi 114052502 584 WHTFNDSSVTPMSSSQV 600
Cdd:COG5077 460 WYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
283-611 |
4.76e-13 |
|
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: 69.09 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 283 LRNLGNTCFMNSILQCLSNTRELRdyclqrlymrdlghtssahtalmEEFAkliqtiwtsspNDvvspsefktqiqryap 362
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKIN-----------------------TEFD-----------ND---------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 363 rfmgyNQQDAQEFLRFLLDGLHNEVNRVAARPKASPETLDHLPDEEKgrqmwrkyleredsrigdlFVGQLKSSLTCTDC 442
Cdd:cd02673 32 -----DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEA-------------------FKYTIESSYVCIGC 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 443 GYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDildgdEKPTCCRCRARKRCIKKFSvqRFPKILVLHLKRFsES 522
Cdd:cd02673 88 SFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EKDCSSCKCESAISSERIM--TFPECLSINLKRY-KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 523 RIRTSKLttfvnfpLRD--LDLREFASEntnHAVYNLYAVSNHSG-TTMGGHYTAYCRSPVTG-EWHTFNDSSVTPMSSS 598
Cdd:cd02673 160 RIATSDY-------LKKneEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
|
330
....*....|....*.
gi 114052502 599 QVR---TSDAYLLFYE 611
Cdd:cd02673 230 DVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-610 |
9.85e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 63.66 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 281 AGLRNLGNTCFMNSILQCLSNTRELRDYCL---------------------QRLYMRDLGHTSSAHTALMEEFAKLIqti 339
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLnfdeskaelasdypterriggREVSRSELQRSNQFVYELRSLFNDLI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 340 wtSSPNDVVSPSefktqiQRYAprFMGYNQQDAQEFLRFLLDGLhnevnRVAARPkasPETLDHLPDEEKGrqmwrkyLE 419
Cdd:cd02666 79 --HSNTRSVTPS------KELA--YLALRQQDVTECIDNVLFQL-----EVALEP---ISNAFAGPDTEDD-------KE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 420 REDsRIGDLFVGQLKSSLTCTDCGYCSTVFDP---FWDLSLPIAKRGYPEVT------LMDCM-RLFTKEDILDGDEKPT 489
Cdd:cd02666 134 QSD-LIKRLFSGKTKQQLVPESMGNQPSVRTKterFLSLLVDVGKKGREIVVllepkdLYDALdRYFDYDSLTKLPQRSQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 490 CCRCRARKRCIKKFSVQRF-PKILVLHLKRFSESRIRT-SKLTTFVNFPLRDLD-LREFASENTNHAVYNLYAVSNHSGT 566
Cdd:cd02666 213 VQAQLAQPLQRELISMDRYeLPSSIDDIDELIREAIQSeSSLVRQAQNELAELKhEIEKQFDDLKSYGYRLHAVFIHRGE 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 114052502 567 TMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQV----RTSDA--YLLFY 610
Cdd:cd02666 293 ASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftLGNTAtpYFLVY 342
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
281-592 |
4.43e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 58.05 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 281 AGLRNLGNTCFMNSILQCLSNTRELR-------------DYCL--QRLY---M---------------RDLGHTSSAHT- 326
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCLlcELGFlfdMlekakgkncqasnflRALSSIPEASAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 327 ALMEEFAkliqtiwtsSPNDVVSPSefkTQIQRyaprfmgynqqdaqeFLRFLLDGLHNEVNRVAARPKASPETLDhlpd 406
Cdd:pfam13423 81 GLLDEDR---------ETNSAISLS---SLIQS---------------FNRFLLDQLSSEENSTPPNPSPAESPLE---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 407 eekgrqmwrkyleredsrigDLFVGQLKSSLTCTDCGYCST------VFDpfwdLSLPIAK----RGYPEVTLMDCMRLF 476
Cdd:pfam13423 130 --------------------QLFGIDAETTIRCSNCGHESVressthVLD----LIYPRKPssnnKKPPNQTFSSILKSS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 477 TKEDILdgdEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFvnFPLR-DLDLREFASENTNHAVY 555
Cdd:pfam13423 186 LERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEiGLTLSDDLQGDNEIVKY 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 114052502 556 NLYA-VSNHSGTTMGGHYTAYCR-------SPVTGEWHTFNDSSV 592
Cdd:pfam13423 261 ELRGvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
369-610 |
2.41e-08 |
|
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: 54.87 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 369 QQDAQEFLRFLLDGLHNEVNRVAARPKASPETLDHLPDEEKGRQMWRKYLERedsrigdlfvgqlKSSLTCTDCGycstv 448
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG-------------KPFCNCETFG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 449 fdpfwdlSLPIAKRGYPEvtLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKkfsvqrFPKILVLHLKRFSESRIRTSK 528
Cdd:cd02665 84 -------QYPLQVNGYGN--LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 529 LTTFVNFPlrdldlREFASENtnhavYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQV-------- 600
Cdd:cd02665 149 IHDKLEFP------QIIQQVP-----YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfggg 217
|
250
....*....|
gi 114052502 601 RTSDAYLLFY 610
Cdd:cd02665 218 RNPSAYCLMY 227
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
502-611 |
3.46e-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: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052502 502 KFSVQRFPKI----LVLHLKRFSESR-------IRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYA-VSNHSGTTMG 569
Cdd:cd02672 149 TTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGyVCEINDSSRG 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 114052502 570 GHYTA----YCRSPVTGEWHTFNDSSVTPMSssqvrtSDAYLLFYE 611
Cdd:cd02672 229 QHNVVfvikVNEESTHGRWYLFNDFLVTPVS------ELAYILLYQ 268
|
|
| |
