|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
1.75e-113 |
|
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: 336.95 E-value: 1.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNtqslrdyclhnshrrdlnnnnrthtalmeefakliqtmwtsssseavspsefktqiqrya 310
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 311 prfvgyNQQDAQEFLRFLLDGLHnevnrvtvrprgntedfdhlpdeekgkkmwskyleredSKIVDLFVGQLKSSLTCSE 390
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 391 CGYCSTVFDPFWDLSLPIAKKG--YGEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKRF 468
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSGSgdAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 469 SEARIRTSKLSTFVNFPMKDLDLREFASDRS--SSAVYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVTPMSA 546
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSftGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 528501548 547 SQVRSSDAYVLFYE 560
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
230-559 |
5.18e-110 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 330.94 E-value: 5.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 230 VGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNRTHtALMEEFAKLIQTMWTSSSSEAVSPSEFKTQIQRY 309
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI-NLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 310 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTvrprgntedfdhlpdeekgkkmwskyLEREDSKIVDLFVGQLKSSLTCS 389
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNH--------------------------STENESLITDLFRGQLKSRLKCL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 390 ECGYCSTVFDPFWDLSLPIAKKGY--GEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKR 467
Cdd:pfam00443 134 SCGEVSETFEPFSDLSLPIPGDSAelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 468 FSEARIRTSKLSTFVNFPMkDLDLREFAS-----DRSSSAVYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVT 542
Cdd:pfam00443 214 FSYNRSTWEKLNTEVEFPL-ELDLSRYLAeelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVT 292
|
330
....*....|....*...
gi 528501548 543 PMSAS-QVRSSDAYVLFY 559
Cdd:pfam00443 293 EVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-559 |
6.17e-76 |
|
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: 242.95 E-value: 6.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNRTHTALMEEFAKliQTMWTSSSSEAVSPseFKTQIQRYA 310
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSAPRI--FSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 311 PRFVGYNQQDAQEFLRFLLDGLHnevnRVTVRPRGNTEDFDHLpdeekgkkmwskylEREDSKIVDLFVGQLKSSLTCSE 390
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS--------------SQETTLVQQIFGGYLRSQVKCLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 391 CGYCSTVFDPFWDLSLPIAKKGygevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKRFSE 470
Cdd:cd02661 141 CKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 471 arIRTSKLSTFVNFPMKdLDLREFASDRS-SSAVYNLYAVSNHSGTTM-GGHYTAYCCNPeNGEWYTYNDSRVTPMSASQ 548
Cdd:cd02661 217 --FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIET 292
|
330
....*....|.
gi 528501548 549 VRSSDAYVLFY 559
Cdd:cd02661 293 VLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
231-560 |
1.36e-75 |
|
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: 240.08 E-value: 1.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNtqslrdyclhnshrrdlnnnnrthtalmeefakliqtmwtsssseavspsefktqiqrya 310
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 311 prfvgyNQQDAQEFLRFLLDGLHNEVNRVTVRprgntedfdhlpdeekgkkmwSKYLEREDSKIVDLFVGQLKSSLTCSE 390
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 391 CGYCSTVFDPFWDLSLPIAKKGYGEVSLMDCMRLFTKEDVLDGDEKPTCYRCKaRRRCTKKFTVQKFPKILVLHLKRFS- 469
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 470 EARIRTSKLSTFVNFPMKDLDLREFASDRS------SSAVYNLYAVSNHSGTTM-GGHYTAYCCNPENGEWYTYNDSRVT 542
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLELDLSPYLSEGEKdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVT 232
|
330 340
....*....|....*....|...
gi 528501548 543 PMSASQV-----RSSDAYVLFYE 560
Cdd:cd02257 233 EVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-559 |
8.38e-64 |
|
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: 211.85 E-value: 8.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDlNNNNRTHTALMEEFAKLIQTMWTSSSSEAVSPSEFKTQIQRYA 310
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCT-CLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 311 PRFVGYNQQDAQEFLRFLLDGLHNevnrvtvrprgntedfdhlpDEEKGKKMWSKylEREDSKIVD-LFVGQLKSSLTCS 389
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHT--------------------HYGGDKNEAND--ESHCNCIIHqTFSGSLQSSVTCQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 390 ECGYCSTVFDPFWDLSLPI-----------AKKGYGEVSLMDCMRLFTKEDVLdGDEKPTCYRCKARRRCTKKFTVQKFP 458
Cdd:cd02660 139 RCGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 459 KILVLHLKRFS-EARIRTSKLSTFVNFPMkDLDLREFASDRS----------SSAVYNLYAVSNHSGTTMGGHYTAYCCN 527
Cdd:cd02660 218 PVLCFQLKRFEhSLNKTSRKIDTYVQFPL-ELNMTPYTSSSIgdtqdsnsldPDYTYDLFAVVVHKGTLDTGHYTAYCRQ 296
|
330 340 350
....*....|....*....|....*....|..
gi 528501548 528 pENGEWYTYNDSRVTPMSASQVRSSDAYVLFY 559
Cdd:cd02660 297 -GDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
1.60e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 204.16 E-value: 1.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSLRDycLHNSHRRDLnnnnrthtalmeeFAkliqtmwtsssseavspsefktQIQRYA 310
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE--LLSETPKEL-------------FS----------------------QVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 311 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtvrprgntedfdhlpdeekgkkmwskyleredskivdlFVGQLKSSLTCSE 390
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 391 CGYCSTVFDPFWDLSLPIAKKGYGEVSLMDCMRLFTKEDVLDGDEKptcYRCKARRRCTKKFTVQKFPKILVLHLKRFS- 469
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 470 EARIRTSKLSTFVNFPmKDLDLREF------ASDRSSSAVYNLYAVSNHSGTTMGGHYTAY------------------- 524
Cdd:cd02667 163 PRSANLRKVSRHVSFP-EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYvkvrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 528501548 525 --CCNPENGEWYTYNDSRVTPMSASQVRSSDAYVLFYE 560
Cdd:cd02667 242 adEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-561 |
4.43e-50 |
|
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: 175.52 E-value: 4.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 228 GLVGLRNLGNTCFMNSILQCLSNTQSLRDYCLH-NSHRRDLNNNNRThTALMEEFAKLiQTMwtsssseavsPSEFKTQI 306
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSiPPTEDDDDNKSVP-LALQRLFLFL-QLS----------ESPVKTTE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 307 QRYAPRFVG------YNQQDAQEFLRFLLDGLhnevnrvtvrprgntedfdhlpdEEKgkkmwSKYLEREDSkIVDLFVG 380
Cdd:cd02659 69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKL-----------------------EEK-----LKGTGQEGL-IKNLFGG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 381 QLKSSLTCSECGYCSTVFDPFWDLSLPIakKGYGevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKI 460
Cdd:cd02659 120 KLVNYIICKECPHESEREEYFLDLQVAV--KGKK--NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 461 LVLHLKRF-----SEARIrtsKLSTFVNFPMKdLDLREF------------ASDRSSSAVYNLYAVSNHSGTTMGGHYTA 523
Cdd:cd02659 196 LTLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYtekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYS 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 524 YCCNPENGEWYTYNDSRVTPMSASQV----------------------RSSDAYVLFYER 561
Cdd:cd02659 272 YIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYER 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
228-561 |
7.19e-48 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 178.54 E-value: 7.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 228 GLVGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNR--THTALMEEFAKLIQTMWTSSSSEAVSPSeFKTQ 305
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPlgMHGSVASAYADLIKQLYDGNLHAFTPSG-FKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 306 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTVRP---RGNTEDFDHLPDEEKGKKMWSKYLEREDSKIVDLFVGQL 382
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytsKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 383 KSSLTCSECGYCSTVFDPFWDLSLPIAKKGY----------------------GEVSLMDCMRLFTKEDVLDGDEKPTC- 439
Cdd:COG5560 423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtivvfpesgrrqplkieldASSTIRGLKKLVDAEYGKLGCFEIKVm 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 440 --YRCKARRRCTKKFTV--QKFPK---------------ILVLHL--------------------------------KRF 468
Cdd:COG5560 503 ciYYGGNYNMLEPADKVllQDIPQtdfvylyetndngieVPVVHLriekgykskrlfgdpflqlnvlikasiydklvKEF 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 469 SEARIRTSK------LSTF----------------------------------VNFPMK--------------------- 487
Cdd:COG5560 583 EELLVLVEMkktdvdLVSEqvrllreesspsswlkleteidtkreeqveeegqMNFNDAvvisceweekrylslfsydpl 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 488 --------------------------DLDLRE--------------------------------FASDRSSS-------- 501
Cdd:COG5560 663 wtireigaaertitlqdclnefskpeQLGLSDswycpgckefrqaskqmelwrlpmiliihlkrFSSVRSFRdkiddlve 742
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501548 502 -------------------AVYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVTPMSASQVRSSDAYVLFYER 561
Cdd:COG5560 743 ypiddldlsgveymvddprLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
7.61e-39 |
|
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: 144.87 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSLRDYCL------HNSHRRDLNNNNRTHTALMEEFAKLIQTMWTSSSSEAVSPSEFKt 304
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnsteDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 305 qiqryAPRFVGYNQQDAQEFLRFLLDGLHNEVnrvtvrprgntedfdhlpdeekgkkmwSKYLEREDSKIV-DLFVGQLK 383
Cdd:cd02668 80 -----ALGLDTGQQQDAQEFSKLFLSLLEAKL---------------------------SKSKNPDLKNIVqDLFRGEYS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 384 SSLTCSECGYCSTVFDPFWDLSLPIAkkgyGEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVL 463
Cdd:cd02668 128 YVTQCSKCGRESSLPSKFYELELQLK----GHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 464 HLKRFSEARIRTS--KLSTFVNFPmKDLDLREFASDRS-SSAVYNLYAVSNHSGT-TMGGHYTAYCCNPENGEWYTYNDS 539
Cdd:cd02668 204 QLLRFVFDRKTGAkkKLNASISFP-EILDMGEYLAESDeGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDE 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 528501548 540 RVTPM------------SASQVR---------SSDAYVLFYE 560
Cdd:cd02668 283 DVEEMpgkplklgnsedPAKPRKseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
1.60e-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: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNT---QSLRD--YCLHNSHRRdlnnnnrthtalmeefAKLIQTmwtsssseavspSEFKTQ 305
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEnllTCLKDlfESISEQKKR----------------TGVISP------------KKFITR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 306 IQRYAPRFVGYNQQDAQEFLRFLLdglhNEVnrvtvrprgnTEDFDHLPDEEKGKKMWSKYLEREDSK--IVDLFVGQLK 383
Cdd:cd02663 53 LKRENELFDNYMHQDAHEFLNFLL----NEI----------AEILDAERKAEKANRKLNNNNNAEPQPtwVHEIFQGILT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 384 SSLTCSECGYCSTVFDPFWDLSLPIAKkgygEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVL 463
Cdd:cd02663 119 NETRCLTCETVSSRDETFLDLSIDVEQ----NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILAL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 464 HLKRF--SEARIRTSKLSTFVNFPmkdLDLREF-ASDRSSSA--VYNLYAVSNHSGTT-MGGHYTAYCcnPENGEWYTYN 537
Cdd:cd02663 195 HLKRFkyDEQLNRYIKLFYRVVFP---LELRLFnTTDDAENPdrLYELVAVVVHIGGGpNHGHYVSIV--KSHGGWLLFD 269
|
330 340 350
....*....|....*....|....*....|.
gi 528501548 538 DSRVTPMSASQVR--------SSDAYVLFYE 560
Cdd:cd02663 270 DETVEKIDENAVEeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
1.67e-34 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 133.00 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTqslRDYCLH--NSHRRDLNNNNRTHTALMEEFAKLiqtMWTSSSSEAVSPSEFKtqiQR 308
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMA---KDFRRQvlSLNLPRLGDSQSVMKKLQLLQAHL---MHTQRRAEAPPDYFLE---AS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 309 YAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVtvrprgntedfdhlpdeekgkkmwskyleredskivdlFVGQLKSSLTC 388
Cdd:cd02664 72 RPPWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRC 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 389 SECGYCSTVFD--PFWDLSLPiakkgygevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLK 466
Cdd:cd02664 114 LNCNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 467 RFS---EARIRTsKLSTFVNFPmKDLDLREFASDRSSS--------------------AVYNLYAVSNHSGTTM-GGHYT 522
Cdd:cd02664 185 RFSydqKTHVRE-KIMDNVSIN-EVLSLPVRVESKSSEsplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSeSGHYF 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501548 523 AYC--------------------CNPENGEWYTYNDSRVTPMSASQV-------RSSDAYVLFYE 560
Cdd:cd02664 263 TYArdqtdadstgqecpepkdaeENDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
218-559 |
2.95e-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: 121.15 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 218 RESLNSksaqgLVGLRNLGNTCFMNSILQCL-------SNTQSLRDYCLHNSHRR---DLNNNNRTHTALMEEFAKLIQT 287
Cdd:cd02671 18 RENLLP-----FVGLNNLGNTCYLNSVLQVLyfcpgfkHGLKHLVSLISSVEQLQssfLLNPEKYNDELANQAPRRLLNA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 288 mwtsssseavspsefktqIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtvrprgntedfdhlpdeekgkkmwskyl 367
Cdd:cd02671 93 ------------------LREVNPMYEGYLQHDAQEVLQCILGNIQELVEK----------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 368 eredskivdLFVGQLKSSLTCSECGYCSTVFDPFWDLSLPIAKKGYGEV---------------SLMDCMRLFTKEDVLD 432
Cdd:cd02671 126 ---------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFASVERIV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 433 GDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKRFSEARIRT------SKLSTFVNFPMKdLDLREFaSDRSSSAVYNL 506
Cdd:cd02671 197 GEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEW-STKPKNDVYRL 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528501548 507 YAVSNHSGTTMG-GHYTAYCCnpengeWYTYNDSRVTPM---------SASQVRSSDAYVLFY 559
Cdd:cd02671 275 FAVVMHSGATISsGHYTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
231-561 |
9.81e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 115.67 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLS-NTQSLRDYCLHNSHR-RDLNN--NNRTHTALMEEFAKLIQTMWTSSSseavspsefktqi 306
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElKVLKNviRKPEPDLNQEEALKLFTALWSSKE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 307 QRYAPRFVGYNQQDAQEFLRFLLDGLHNevnrvtvrPRGNT-EDFDHLPDEEKGKkmwskyleredskivdlfvgqlkss 385
Cdd:COG5533 68 HKVGWIPPMGSQEDAHELLGKLLDELKL--------DLVNSfTIRIFKTTKDKKK------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 386 ltcsecgycsTVFDPFWDL--SLPIAKKGYGEVSLMDCMRLFtKEDVLDG--------DEKptcyrcKARRRCTKKFTVQ 455
Cdd:COG5533 115 ----------TSTGDWFDIiiELPDQTWVNNLKTLQEFIDNM-EELVDDEtgvkakenEEL------EVQAKQEYEVSFV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 456 KFPKILVLHLKRF----SEARIRTS---KLSTFVNFPMKDLDLREFasdrsssaVYNLYAVSNHSGTTMGGHYTAYCcnP 528
Cdd:COG5533 178 KLPKILTIQLKRFanlgGNQKIDTEvdeKFELPVKHDQILNIVKET--------YYDLVGFVLHQGSLEGGHYIAYV--K 247
|
330 340 350
....*....|....*....|....*....|....*.
gi 528501548 529 ENGEWYTYNDSRVTPMS---ASQVRSSDAYVLFYER 561
Cdd:COG5533 248 KGGKWEKANDSDVTPVSeeeAINEKAKNAYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
3.32e-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: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSLRDYclhnshrrdLNNNNrthtalmeefakliqtmwtsssseavspsefktqiqrya 310
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 311 prfvgyNQQDAQEFLRFLLDGLHNEVnrvtvrprgntedfdhlpdeekgkkmwskyleredskiVDLFVGQLKSSLTCSE 390
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------------------------------------KFPFDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 391 CGYCSTV-FDPFWDLSLPI-AKKGYGEVSLMDCMRLFTKEDVLDGdekPTCYRCKArrrctkkfTVQKFPKILVLHLKRF 468
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 469 S-EARIRTSKLSTFVNFPmkdldlrEFASDRSssavYNLYAVSNHSGTTMGGHYTAYCCNPEN----------------- 530
Cdd:cd02662 138 VfDGRGTSTKNSCKVSFP-------ERLPKVL----YRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 528501548 531 ---GEWYTYNDSRVTPMSASQVR-SSDAYVLFYE 560
Cdd:cd02662 207 stsHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
8.47e-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: 113.57 E-value: 8.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSL-RDYCLHNSHRrdLNNNNRTHTALMEEFAKLIQTMWTSSSSEAVSPSE-------- 301
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKF--PSDVVDPANDLNCQLIKLADGLLSGRYSKPASLKSendpyqvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 302 -----FKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtvrprgntedfdhlpdeekgkkmwskyleREDSKIVD 376
Cdd:cd02658 79 ikpsmFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK------------------------------NLGLNPND 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 377 LFVGQLKSSLTCSECGYCSTVFDPFWDLSLPI----------AKKGYGEVSLMDCMRLFTKEDVLDGdekpTCYRCKARR 446
Cdd:cd02658 129 LFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIED----FCSTCKEKT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 447 RCTKKFTVQKFPKILVLHLKRFS-EARIRTSKLSTFVNFPmkdldlrefasDRSSSAVYNLYAVSNHSGT-TMGGHYTAY 524
Cdd:cd02658 205 TATKTTGFKTFPDYLVINMKRFQlLENWVPKKLDVPIDVP-----------EELGPGKYELIAFISHKGTsVHSGHYVAH 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528501548 525 CCNPENGE--WYTYNDSRVtpmsasqVRSSD-------AYVLFYE 560
Cdd:cd02658 274 IKKEIDGEgkWVLFNDEKV-------VASQDppemkklGYIYFYQ 311
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
222-549 |
2.70e-27 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 117.28 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 222 NSKSAQGLVGLRNLGNTCFMNSILQCLSNTQSLRD--YCLHNSHRRdlnNNNRTHTALMEEFAKLiQTMwtsssSEAVSP 299
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR---GRDSVALALQRLFYNL-QTG-----EEPVDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 300 SEFKTQIQRYAprFVGYNQQDAQEFLRFLLDGLHNEVNRVTVrprgntedfdhlpdeekgkkmwskylereDSKIVDLFV 379
Cdd:COG5077 257 TELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKSMRGTVV-----------------------------ENALNGIFV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 380 GQLKSSLTCSECGYCSTVFDPFWDLSLPIakKGYGevSLMDCMRLFTKEDVLDGDekpTCYRCKAR--RRCTKKFTVQKF 457
Cdd:COG5077 306 GKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 458 PKILVLHLKRFSEARIRTS--KLSTFVNFPMkDLDLREFAS---DRS--SSAVYNLYAVSNHSGTTMGGHYTAYCCNPEN 530
Cdd:COG5077 379 PPVLHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFLDrdaDKSenSDAVYVLYGVLVHSGDLHEGHYYALLKPEKD 457
|
330
....*....|....*....
gi 528501548 531 GEWYTYNDSRVTPMSASQV 549
Cdd:COG5077 458 GRWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
231-560 |
5.13e-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 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: 111.27 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 231 GLRNLGNTCFMNSILQCLSNTQSLRDYCL-HNSHRRDLNNNNRTHTAlmeEFAKLIQTMwtSSSSEAVSPSEFKTQIQRY 309
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnYNPARRGANQSSDNLTN---ALRDLFDTM--DKKQEPVPPIEFLQLLRMA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 310 APRFV------GYNQQDAQEFLRFLLDGLHNEVnrvtvrprgntedfdhlpdeekgkkmwsKYLEREDSKIVDLFVGQLK 383
Cdd:cd02657 76 FPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGIELE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 384 SSLTCSECGYCSTV-FDPFWDLSLPIAKKgygevslMDCMRLFTK-EDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKIL 461
Cdd:cd02657 128 TKMKCTESPDEEEVsTESEYKLQCHISIT-------TEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 462 VLHLKRFS--EARIRTSKLSTFVNFPMkDLDLREFAsdrSSSAVYNLYAVSNHSGTTM-GGHYTAYCCNPENGEWYTYND 538
Cdd:cd02657 201 TVQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDD 276
|
330 340
....*....|....*....|....*....
gi 528501548 539 SRVTPMSASQVRSSD-------AYVLFYE 560
Cdd:cd02657 277 DKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-560 |
1.42e-25 |
|
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: 109.72 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 228 GLVGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNShrrDLNNNNRTHTALMEEFAKLIQTMWTSSSseavspseFKTQIQ 307
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE---NYENIKDRKSELVKRLSELIRKIWNPRN--------FKGHVS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 308 RY----------APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTVRPRGNtedfdhLPDEEKGK-KMWSKYLEREDSKivd 376
Cdd:cd02669 187 PHellqavskvsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSI------IHDCFQGKvQIETQKIKPHAEE--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 377 lfVGQLKSSLTCSECGycSTVFDPFWDLSL-----PIAKKGYGEVSLmdcmRLFTKEDVLDGDEKPTCYRCKARRrctKK 451
Cdd:cd02669 258 --EGSKDKFFKDSRVK--KTSVSPFLLLTLdlpppPLFKDGNEENII----PQVPLKQLLKKYDGKTETELKDSL---KR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 452 FTVQKFPKILVLHLKRFSEARIRTSKLSTFVNFPMKDLDLREF----ASDRSSSAVYNLYAVSNHSGTTMG-GHYTAYCC 526
Cdd:cd02669 327 YLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYvhfdKPSLNLSTKYNLVANIVHEGTPQEdGTWRVQLR 406
|
330 340 350
....*....|....*....|....*....|....
gi 528501548 527 NPENGEWYTYNDSRVTPMSASQVRSSDAYVLFYE 560
Cdd:cd02669 407 HKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
230-549 |
9.49e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 69.44 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 230 VGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNRTHTALM---EEFAKLIQTMWTSSSSEAVSPSEFKTQI 306
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRIggrEVSRSELQRSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 307 QRYA-PR----FVGYNQQDAQEFLRFLLDGLhnevnRVTVRPRGNTedfDHLPDEEKGKKmwskylerEDSKIVDLFVGQ 381
Cdd:cd02666 82 TRSVtPSkelaYLALRQQDVTECIDNVLFQL-----EVALEPISNA---FAGPDTEDDKE--------QSDLIKRLFSGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 382 LKSSLT-CSECGYCSTVFDPFWDLSLPI--AKKGY------GEVSLMDCMRLFTKEDVLDgdekptcyRCKARRRCTKKF 452
Cdd:cd02666 146 TKQQLVpESMGNQPSVRTKTERFLSLLVdvGKKGReivvllEPKDLYDALDRYFDYDSLT--------KLPQRSQVQAQL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 453 TVQKFPKIL------VLHLKRFSEARIRTSKLSTFVNFPMKDLDLREFASDRSS------SAVYNLYAVSNHSGTTMGGH 520
Cdd:cd02666 218 AQPLQRELIsmdryeLPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKqfddlkSYGYRLHAVFIHRGEASSGH 297
|
330 340
....*....|....*....|....*....
gi 528501548 521 YTAYCCNPENGEWYTYNDSRVTPMSASQV 549
Cdd:cd02666 298 YWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
318-559 |
2.95e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 60.65 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 318 QQDAQEFLRFLLDGLHNEVNRVtvrprgntedfdhLPDEEKGKKMWSKYLEREDSKIVDLFVGQLKSSLTCSECGycstv 397
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAA-------------AEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 398 fdpfwdlSLPIAKKGYGevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKkftvqkFPKILVLHLKRFSEARIRTSK 477
Cdd:cd02665 84 -------QYPLQVNGYG--NLHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 478 LSTFVNFPMkdlDLREFAsdrsssavYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVTPMSASQV-------- 549
Cdd:cd02665 149 IHDKLEFPQ---IIQQVP--------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfggg 217
|
250
....*....|
gi 528501548 550 RSSDAYVLFY 559
Cdd:cd02665 218 RNPSAYCLMY 227
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
232-560 |
4.61e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 57.15 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 232 LRNLGNTCFMNSILQCLSNTqslrdyclhNSHRRDLNNNNrthtalmeefakliqtmwtsssseavspsefktqiqryap 311
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSI---------GKINTEFDNDD---------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 312 rfvgynQQDAQEFLRFLLDGLHN--EVNRVTVRPRGNTedfdhlpdeekgkkmwSKYLEREDSkivdlFVGQLKSSLTCS 389
Cdd:cd02673 33 ------QQDAHEFLLTLLEAIDDimQVNRTNVPPSNIE----------------IKRLNPLEA-----FKYTIESSYVCI 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 390 ECGYCSTVFDPFWDLSLPIAKKGYGEVSLMDCMRLFTKEDvldgdEKpTCYRCKARRRCTKKfTVQKFPKILVLHLKRFS 469
Cdd:cd02673 86 GCSFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EK-DCSSCKCESAISSE-RIMTFPECLSINLKRYK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 470 EaRIRTSKlstfvnFPMKD-LDLREFASDRSSsavYNLYAVSNHSG-TTMGGHYTAYCCNPENG-EWYTYNDSRVTPMSA 546
Cdd:cd02673 159 L-RIATSD------YLKKNeEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSK 228
|
330
....*....|....*..
gi 528501548 547 SQVR---SSDAYVLFYE 560
Cdd:cd02673 229 NDVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
431-560 |
1.90e-04 |
|
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: 43.27 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501548 431 LDGDEKPTCYRCKARRRCTKKFTVQKFPKI----LVLHLKRFSEAR-------IRTSKLSTFVNFPMKDLDLREFASDRS 499
Cdd:cd02672 129 LEKVTKAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQE 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528501548 500 SSAVYNLYA-VSNHSGTTMGGHYTA----YCCNPENGEWYTYNDSRVTPMsasqvrSSDAYVLFYE 560
Cdd:cd02672 209 SIYKYELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPV------SELAYILLYQ 268
|
|
| |
