|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
7.13e-114 |
|
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: 331.56 E-value: 7.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNtqslrdyclhnshrrdlnnnnrthtalmeefakliqtmwtsssseavspsefktqiqrya 141
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 142 prfvgyNQQDAQEFLRFLLDGLHnevnrvtvrprgntedfdhlpdeekgkkmwskyleredSKIVDLFVGQLKSSLTCSE 221
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 222 CGYCSTVFDPFWDLSLPIAKKG--YGEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKRF 299
Cdd:cd02674 57 CGKTSTTFEPFTYLSLPIPSGSgdAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 300 SEARIRTSKLSTFVNFPMKDLDLREFASDRS--SSAVYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVTPMSA 377
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSftGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330
....*....|....
gi 2511096478 378 SQVRSSDAYVLFYE 391
Cdd:cd02674 217 SSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
61-390 |
1.80e-110 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 326.32 E-value: 1.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 61 VGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNRTHtALMEEFAKLIQTMWTSSSSEAVSPSEFKTQIQRY 140
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI-NLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 141 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTvrprgntedfdhlpdeekgkkmwskyLEREDSKIVDLFVGQLKSSLTCS 220
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNH--------------------------STENESLITDLFRGQLKSRLKCL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 221 ECGYCSTVFDPFWDLSLPIAKKGY--GEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKR 298
Cdd:pfam00443 134 SCGEVSETFEPFSDLSLPIPGDSAelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 299 FSEARIRTSKLSTFVNFPMkDLDLREFAS-----DRSSSAVYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVT 373
Cdd:pfam00443 214 FSYNRSTWEKLNTEVEFPL-ELDLSRYLAeelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVT 292
|
330
....*....|....*...
gi 2511096478 374 PMSAS-QVRSSDAYVLFY 390
Cdd:pfam00443 293 EVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-390 |
5.12e-77 |
|
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: 240.26 E-value: 5.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNRTHTALMEEFAKliQTMWTSSSSEAVSPseFKTQIQRYA 141
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSAPRI--FSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 142 PRFVGYNQQDAQEFLRFLLDGLHnevnRVTVRPRGNTEDFDHLpdeekgkkmwskylEREDSKIVDLFVGQLKSSLTCSE 221
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS--------------SQETTLVQQIFGGYLRSQVKCLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 222 CGYCSTVFDPFWDLSLPIAKKGygevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLKRFSE 301
Cdd:cd02661 141 CKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 302 arIRTSKLSTFVNFPMKdLDLREFASDRS-SSAVYNLYAVSNHSGTTM-GGHYTAYCCNPeNGEWYTYNDSRVTPMSASQ 379
Cdd:cd02661 217 --FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIET 292
|
330
....*....|.
gi 2511096478 380 VRSSDAYVLFY 390
Cdd:cd02661 293 VLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
62-391 |
1.05e-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: 235.46 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNtqslrdyclhnshrrdlnnnnrthtalmeefakliqtmwtsssseavspsefktqiqrya 141
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 142 prfvgyNQQDAQEFLRFLLDGLHNEVNRVTVRprgntedfdhlpdeekgkkmwSKYLEREDSKIVDLFVGQLKSSLTCSE 221
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 222 CGYCSTVFDPFWDLSLPIAKKGYGEVSLMDCMRLFTKEDVLDGDEKPTCYRCKaRRRCTKKFTVQKFPKILVLHLKRFS- 300
Cdd:cd02257 74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSf 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 301 EARIRTSKLSTFVNFPMKDLDLREFASDRS------SSAVYNLYAVSNHSGTTM-GGHYTAYCCNPENGEWYTYNDSRVT 373
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLELDLSPYLSEGEKdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVT 232
|
330 340
....*....|....*....|...
gi 2511096478 374 PMSASQV-----RSSDAYVLFYE 391
Cdd:cd02257 233 EVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-390 |
1.56e-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: 209.15 E-value: 1.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDlNNNNRTHTALMEEFAKLIQTMWTSSSSEAVSPSEFKTQIQRYA 141
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCT-CLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 142 PRFVGYNQQDAQEFLRFLLDGLHNevnrvtvrprgntedfdhlpDEEKGKKMWSKylEREDSKIVD-LFVGQLKSSLTCS 220
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHT--------------------HYGGDKNEAND--ESHCNCIIHqTFSGSLQSSVTCQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 221 ECGYCSTVFDPFWDLSLPI-----------AKKGYGEVSLMDCMRLFTKEDVLdGDEKPTCYRCKARRRCTKKFTVQKFP 289
Cdd:cd02660 139 RCGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 290 KILVLHLKRFS-EARIRTSKLSTFVNFPMkDLDLREFASDRS----------SSAVYNLYAVSNHSGTTMGGHYTAYCCN 358
Cdd:cd02660 218 PVLCFQLKRFEhSLNKTSRKIDTYVQFPL-ELNMTPYTSSSIgdtqdsnsldPDYTYDLFAVVVHKGTLDTGHYTAYCRQ 296
|
330 340 350
....*....|....*....|....*....|..
gi 2511096478 359 pENGEWYTYNDSRVTPMSASQVRSSDAYVLFY 390
Cdd:cd02660 297 -GDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
3.46e-63 |
|
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: 3.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSLRDycLHNSHRRDLnnnnrthtalmeeFAkliqtmwtsssseavspsefktQIQRYA 141
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE--LLSETPKEL-------------FS----------------------QVCRKA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 142 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtvrprgntedfdhlpdeekgkkmwskyleredskivdlFVGQLKSSLTCSE 221
Cdd:cd02667 44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 222 CGYCSTVFDPFWDLSLPIAKKGYGEVSLMDCMRLFTKEDVLDGDEKptcYRCKARRRCTKKFTVQKFPKILVLHLKRFS- 300
Cdd:cd02667 86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 301 EARIRTSKLSTFVNFPmKDLDLREF------ASDRSSSAVYNLYAVSNHSGTTMGGHYTAY------------------- 355
Cdd:cd02667 163 PRSANLRKVSRHVSFP-EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYvkvrppqqrlsdltkskpa 241
|
330 340 350
....*....|....*....|....*....|....*...
gi 2511096478 356 --CCNPENGEWYTYNDSRVTPMSASQVRSSDAYVLFYE 391
Cdd:cd02667 242 adEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-392 |
8.31e-51 |
|
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: 173.60 E-value: 8.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 59 GLVGLRNLGNTCFMNSILQCLSNTQSLRDYCLH-NSHRRDLNNNNRThTALMEEFAKLiQTMwtsssseavsPSEFKTQI 137
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSiPPTEDDDDNKSVP-LALQRLFLFL-QLS----------ESPVKTTE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 138 QRYAPRFVG------YNQQDAQEFLRFLLDGLhnevnrvtvrprgntedfdhlpdEEKgkkmwSKYLEREDSkIVDLFVG 211
Cdd:cd02659 69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKL-----------------------EEK-----LKGTGQEGL-IKNLFGG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 212 QLKSSLTCSECGYCSTVFDPFWDLSLPIakKGYGevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKI 291
Cdd:cd02659 120 KLVNYIICKECPHESEREEYFLDLQVAV--KGKK--NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 292 LVLHLKRF-----SEARIrtsKLSTFVNFPMKdLDLREF------------ASDRSSSAVYNLYAVSNHSGTTMGGHYTA 354
Cdd:cd02659 196 LTLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYtekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYS 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 355 YCCNPENGEWYTYNDSRVTPMSASQV----------------------RSSDAYVLFYER 392
Cdd:cd02659 272 YIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYER 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
59-392 |
2.41e-49 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 178.15 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 59 GLVGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNR--THTALMEEFAKLIQTMWTSSSSEAVSPSeFKTQ 136
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPlgMHGSVASAYADLIKQLYDGNLHAFTPSG-FKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 137 IQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTVRP---RGNTEDFDHLPDEEKGKKMWSKYLEREDSKIVDLFVGQL 213
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytsKPDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 214 KSSLTCSECGYCSTVFDPFWDLSLPIAKKGY----------------------GEVSLMDCMRLFTKEDVLDGDEKPTC- 270
Cdd:COG5560 423 KSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtivvfpesgrrqplkieldASSTIRGLKKLVDAEYGKLGCFEIKVm 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 271 --YRCKARRRCTKKFTV--QKFPK---------------ILVLHL--------------------------------KRF 299
Cdd:COG5560 503 ciYYGGNYNMLEPADKVllQDIPQtdfvylyetndngieVPVVHLriekgykskrlfgdpflqlnvlikasiydklvKEF 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 300 SEARIRTSK------LSTF----------------------------------VNFPMK--------------------- 318
Cdd:COG5560 583 EELLVLVEMkktdvdLVSEqvrllreesspsswlkleteidtkreeqveeegqMNFNDAvvisceweekrylslfsydpl 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 319 --------------------------DLDLRE--------------------------------FASDRSSS-------- 332
Cdd:COG5560 663 wtireigaaertitlqdclnefskpeQLGLSDswycpgckefrqaskqmelwrlpmiliihlkrFSSVRSFRdkiddlve 742
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2511096478 333 -------------------AVYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVTPMSASQVRSSDAYVLFYER 392
Cdd:COG5560 743 ypiddldlsgveymvddprLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
7.48e-40 |
|
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: 144.49 E-value: 7.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSLRDYCL------HNSHRRDLNNNNRTHTALMEEFAKLIQTMWTSSSSEAVSPSEFKt 135
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnsteDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 136 qiqryAPRFVGYNQQDAQEFLRFLLDGLHNEVnrvtvrprgntedfdhlpdeekgkkmwSKYLEREDSKIV-DLFVGQLK 214
Cdd:cd02668 80 -----ALGLDTGQQQDAQEFSKLFLSLLEAKL---------------------------SKSKNPDLKNIVqDLFRGEYS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 215 SSLTCSECGYCSTVFDPFWDLSLPIAkkgyGEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVL 294
Cdd:cd02668 128 YVTQCSKCGRESSLPSKFYELELQLK----GHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 295 HLKRFSEARIRTS--KLSTFVNFPmKDLDLREFASDRS-SSAVYNLYAVSNHSGT-TMGGHYTAYCCNPENGEWYTYNDS 370
Cdd:cd02668 204 QLLRFVFDRKTGAkkKLNASISFP-EILDMGEYLAESDeGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDE 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2511096478 371 RVTPM------------SASQVR---------SSDAYVLFYE 391
Cdd:cd02668 283 DVEEMpgkplklgnsedPAKPRKseikkgthsSRTAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
1.46e-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: 137.44 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNT---QSLRD--YCLHNSHRRdlnnnnrthtalmeefAKLIQTmwtsssseavspSEFKTQ 136
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEnllTCLKDlfESISEQKKR----------------TGVISP------------KKFITR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 137 IQRYAPRFVGYNQQDAQEFLRFLLdglhNEVNRVTVRPRGNTEdfdhlpdeEKGKKMWSKYLEREDSKIVDLFVGQLKSS 216
Cdd:cd02663 53 LKRENELFDNYMHQDAHEFLNFLL----NEIAEILDAERKAEK--------ANRKLNNNNNAEPQPTWVHEIFQGILTNE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 217 LTCSECGYCSTVFDPFWDLSLPIAKkgygEVSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHL 296
Cdd:cd02663 121 TRCLTCETVSSRDETFLDLSIDVEQ----NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 297 KRF--SEARIRTSKLSTFVNFPmkdLDLREF-ASDRSSSA--VYNLYAVSNHSGTT-MGGHYTAYCcnPENGEWYTYNDS 370
Cdd:cd02663 197 KRFkyDEQLNRYIKLFYRVVFP---LELRLFnTTDDAENPdrLYELVAVVVHIGGGpNHGHYVSIV--KSHGGWLLFDDE 271
|
330 340
....*....|....*....|....*....
gi 2511096478 371 RVTPMSASQVR--------SSDAYVLFYE 391
Cdd:cd02663 272 TVEKIDENAVEeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
2.76e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 132.23 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTqslRDYCLH--NSHRRDLNNNNRTHTALMEEFAKLiqtMWTSSSSEAVSPSEFKtqiQR 139
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMA---KDFRRQvlSLNLPRLGDSQSVMKKLQLLQAHL---MHTQRRAEAPPDYFLE---AS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 140 YAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVtvrprgntedfdhlpdeekgkkmwskyleredskivdlFVGQLKSSLTC 219
Cdd:cd02664 72 RPPWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRC 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 220 SECGYCSTVFD--PFWDLSLPiakkgygevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKILVLHLK 297
Cdd:cd02664 114 LNCNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 298 RFS---EARIRTsKLSTFVNFPmKDLDLREFASDRSSS--------------------AVYNLYAVSNHSGTTM-GGHYT 353
Cdd:cd02664 185 RFSydqKTHVRE-KIMDNVSIN-EVLSLPVRVESKSSEsplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSeSGHYF 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2511096478 354 AYC--------------------CNPENGEWYTYNDSRVTPMSASQV-------RSSDAYVLFYE 391
Cdd:cd02664 263 TYArdqtdadstgqecpepkdaeENDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
60-390 |
1.42e-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: 119.61 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 60 LVGLRNLGNTCFMNSILQCL-------SNTQSLRDYCLHNSHRR---DLNNNNRTHTALMEEFAKLIQTmwtsssseavs 129
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLyfcpgfkHGLKHLVSLISSVEQLQssfLLNPEKYNDELANQAPRRLLNA----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 130 psefktqIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtvrprgntedfdhlpdeekgkkmwskyleredskivdLF 209
Cdd:cd02671 93 -------LREVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------------------DF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 210 VGQLKSSLTCSECGYCSTVFDPFWDLSLPIAKKGYGEV---------------SLMDCMRLFTKEDVLDGDEKPTCYRCK 274
Cdd:cd02671 128 QGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCH 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 275 ARRRCTKKFTVQKFPKILVLHLKRFSEARIRT------SKLSTFVNFPMKdLDLREFaSDRSSSAVYNLYAVSNHSGTTM 348
Cdd:cd02671 208 HYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEW-STKPKNDVYRLFAVVMHSGATI 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2511096478 349 G-GHYTAYCCnpengeWYTYNDSRVTPM---------SASQVRSSDAYVLFY 390
Cdd:cd02671 286 SsGHYTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
62-392 |
1.57e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 115.67 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLS-NTQSLRDYCLHNSHR-RDLNN--NNRTHTALMEEFAKLIQTMWTSSSseavspsefktqi 137
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElKVLKNviRKPEPDLNQEEALKLFTALWSSKE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 138 QRYAPRFVGYNQQDAQEFLRFLLDGLHNevnrvtvrPRGNT-EDFDHLPDEEKGKkmwskyleredskivdlfvgqlkss 216
Cdd:COG5533 68 HKVGWIPPMGSQEDAHELLGKLLDELKL--------DLVNSfTIRIFKTTKDKKK------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 217 ltcsecgycsTVFDPFWDL--SLPIAKKGYGEVSLMDCMRLFtKEDVLDG--------DEKptcyrcKARRRCTKKFTVQ 286
Cdd:COG5533 115 ----------TSTGDWFDIiiELPDQTWVNNLKTLQEFIDNM-EELVDDEtgvkakenEEL------EVQAKQEYEVSFV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 287 KFPKILVLHLKRF----SEARIRTS---KLSTFVNFPMKDLDLREFasdrsssaVYNLYAVSNHSGTTMGGHYTAYCcnP 359
Cdd:COG5533 178 KLPKILTIQLKRFanlgGNQKIDTEvdeKFELPVKHDQILNIVKET--------YYDLVGFVLHQGSLEGGHYIAYV--K 247
|
330 340 350
....*....|....*....|....*....|....*.
gi 2511096478 360 ENGEWYTYNDSRVTPMS---ASQVRSSDAYVLFYER 392
Cdd:COG5533 248 KGGKWEKANDSDVTPVSeeeAINEKAKNAYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
7.19e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 112.46 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSLRDYclhnshrrdLNNNNrthtalmeefakliqtmwtsssseavspsefktqiqrya 141
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY---------LEEFL--------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 142 prfvgyNQQDAQEFLRFLLDGLHNEVnrvtvrprgntedfdhlpdeekgkkmwskyleredskiVDLFVGQLKSSLTCSE 221
Cdd:cd02662 33 ------EQQDAHELFQVLLETLEQLL--------------------------------------KFPFDGLLASRIVCLQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 222 CGYCSTV-FDPFWDLSLPI-AKKGYGEVSLMDCMRLFTKEDVLDGdekPTCYRCKArrrctkkfTVQKFPKILVLHLKRF 299
Cdd:cd02662 69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRS 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 300 S-EARIRTSKLSTFVNFPmkdldlrEFASDRSssavYNLYAVSNHSGTTMGGHYTAYCCNPEN----------------- 361
Cdd:cd02662 138 VfDGRGTSTKNSCKVSFP-------ERLPKVL----YRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|....
gi 2511096478 362 ---GEWYTYNDSRVTPMSASQVR-SSDAYVLFYE 391
Cdd:cd02662 207 stsHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
53-380 |
4.06e-28 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 116.89 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 53 NSKSAQGLVGLRNLGNTCFMNSILQCLSNTQSLRD--YCLHNSHRRdlnNNNRTHTALMEEFAKLiQTMwtsssSEAVSP 130
Cdd:COG5077 186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR---GRDSVALALQRLFYNL-QTG-----EEPVDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 131 SEFKTQIQRYAprFVGYNQQDAQEFLRFLLDGLHNEVNRVTVrprgntedfdhlpdeekgkkmwskylereDSKIVDLFV 210
Cdd:COG5077 257 TELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKSMRGTVV-----------------------------ENALNGIFV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 211 GQLKSSLTCSECGYCSTVFDPFWDLSLPIakKGYGevSLMDCMRLFTKEDVLDGDekpTCYRCKAR--RRCTKKFTVQKF 288
Cdd:COG5077 306 GKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 289 PKILVLHLKRFSEARIRTS--KLSTFVNFPMkDLDLREFAS---DRS--SSAVYNLYAVSNHSGTTMGGHYTAYCCNPEN 361
Cdd:COG5077 379 PPVLHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFLDrdaDKSenSDAVYVLYGVLVHSGDLHEGHYYALLKPEKD 457
|
330
....*....|....*....
gi 2511096478 362 GEWYTYNDSRVTPMSASQV 380
Cdd:COG5077 458 GRWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
5.91e-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: 112.03 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSL-RDYCLHNSHRrdLNNNNRTHTALMEEFAKLIQTMWTSSSSEAVSPSE-------- 132
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKF--PSDVVDPANDLNCQLIKLADGLLSGRYSKPASLKSendpyqvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 133 -----FKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtvrprgntedfdhlpdeekgkkmwskyleREDSKIVD 207
Cdd:cd02658 79 ikpsmFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK------------------------------NLGLNPND 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 208 LFVGQLKSSLTCSECGYCSTVFDPFWDLSLPI----------AKKGYGEVSLMDCMRLFTKEDVLDGdekpTCYRCKARR 277
Cdd:cd02658 129 LFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIED----FCSTCKEKT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 278 RCTKKFTVQKFPKILVLHLKRFS-EARIRTSKLSTFVNFPmkdldlrefasDRSSSAVYNLYAVSNHSGT-TMGGHYTAY 355
Cdd:cd02658 205 TATKTTGFKTFPDYLVINMKRFQlLENWVPKKLDVPIDVP-----------EELGPGKYELIAFISHKGTsVHSGHYVAH 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2511096478 356 CCNPENGE--WYTYNDSRVtpmsasqVRSSD-------AYVLFYE 391
Cdd:cd02658 274 IKKEIDGEgkWVLFNDEKV-------VASQDppemkklGYIYFYQ 311
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
62-391 |
1.04e-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: 110.88 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 62 GLRNLGNTCFMNSILQCLSNTQSLRDYCL-HNSHRRDLNNNNRTHTAlmeEFAKLIQTMwtSSSSEAVSPSEFKTQIQRY 140
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnYNPARRGANQSSDNLTN---ALRDLFDTM--DKKQEPVPPIEFLQLLRMA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 141 APRFV------GYNQQDAQEFLRFLLDGLHNEVnrvtvrprgntedfdhlpdeekgkkmwsKYLEREDSKIVDLFVGQLK 214
Cdd:cd02657 76 FPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL----------------------------PGAGSKGSFIDQLFGIELE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 215 SSLTCSECGYCSTV-FDPFWDLSLPIAKKgygevslMDCMRLFTK-EDVLDGDEKPTCYRCKARRRCTKKFTVQKFPKIL 292
Cdd:cd02657 128 TKMKCTESPDEEEVsTESEYKLQCHISIT-------TEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 293 VLHLKRFS--EARIRTSKLSTFVNFPMkDLDLREFAsdrSSSAVYNLYAVSNHSGTTM-GGHYTAYCCNPENGEWYTYND 369
Cdd:cd02657 201 TVQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDD 276
|
330 340
....*....|....*....|....*....
gi 2511096478 370 SRVTPMSASQVRSSD-------AYVLFYE 391
Cdd:cd02657 277 DKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
59-391 |
9.11e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 107.79 E-value: 9.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 59 GLVGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNShrrDLNNNNRTHTALMEEFAKLIQTMWTSSSseavspseFKTQIQ 138
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE---NYENIKDRKSELVKRLSELIRKIWNPRN--------FKGHVS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 139 RY----------APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTVRPRGNtedfdhLPDEEKGK-KMWSKYLEREDSKivd 207
Cdd:cd02669 187 PHellqavskvsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSI------IHDCFQGKvQIETQKIKPHAEE--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 208 lfVGQLKSSLTCSECGycSTVFDPFWDLSL-----PIAKKGYGEVSLmdcmRLFTKEDVLDGDEKPTCYRCKARRrctKK 282
Cdd:cd02669 258 --EGSKDKFFKDSRVK--KTSVSPFLLLTLdlpppPLFKDGNEENII----PQVPLKQLLKKYDGKTETELKDSL---KR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 283 FTVQKFPKILVLHLKRFSEARIRTSKLSTFVNFPMKDLDLREF----ASDRSSSAVYNLYAVSNHSGTTMG-GHYTAYCC 357
Cdd:cd02669 327 YLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYvhfdKPSLNLSTKYNLVANIVHEGTPQEdGTWRVQLR 406
|
330 340 350
....*....|....*....|....*....|....
gi 2511096478 358 NPENGEWYTYNDSRVTPMSASQVRSSDAYVLFYE 391
Cdd:cd02669 407 HKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
61-380 |
2.35e-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: 70.60 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 61 VGLRNLGNTCFMNSILQCLSNTQSLRDYCLHNSHRRDLNNNNRTHTALM---EEFAKLIQTMWTSSSSEAVSPSEFKTQI 137
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRIggrEVSRSELQRSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 138 QRYA-PR----FVGYNQQDAQEFLRFLLDGLhnevnRVTVRPRGNTedfDHLPDEEKGKKmwskylerEDSKIVDLFVGQ 212
Cdd:cd02666 82 TRSVtPSkelaYLALRQQDVTECIDNVLFQL-----EVALEPISNA---FAGPDTEDDKE--------QSDLIKRLFSGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 213 LKSSLT-CSECGYCSTVFDPFWDLSLPI--AKKGY------GEVSLMDCMRLFTKEDVLDgdekptcyRCKARRRCTKKF 283
Cdd:cd02666 146 TKQQLVpESMGNQPSVRTKTERFLSLLVdvGKKGReivvllEPKDLYDALDRYFDYDSLT--------KLPQRSQVQAQL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 284 TVQKFPKIL------VLHLKRFSEARIRTSKLSTFVNFPMKDLDLREFASDRSS------SAVYNLYAVSNHSGTTMGGH 351
Cdd:cd02666 218 AQPLQRELIsmdryeLPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKqfddlkSYGYRLHAVFIHRGEASSGH 297
|
330 340
....*....|....*....|....*....
gi 2511096478 352 YTAYCCNPENGEWYTYNDSRVTPMSASQV 380
Cdd:cd02666 298 YWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
149-390 |
2.99e-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: 59.88 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 149 QQDAQEFLRFLLDGLHNEVNRVtvrprgntedfdhLPDEEKGKKMWSKYLEREDSKIVDLFVGQLKSSLTCSECGycstv 228
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAA-------------AEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 229 fdpfwdlSLPIAKKGYGevSLMDCMRLFTKEDVLDGDEKPTCYRCKARRRCTKkftvqkFPKILVLHLKRFSEARIRTSK 308
Cdd:cd02665 84 -------QYPLQVNGYG--NLHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 309 LSTFVNFPMkdlDLREFAsdrsssavYNLYAVSNHSGTTMGGHYTAYCCNPENGEWYTYNDSRVTPMSASQV-------- 380
Cdd:cd02665 149 IHDKLEFPQ---IIQQVP--------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfggg 217
|
250
....*....|
gi 2511096478 381 RSSDAYVLFY 390
Cdd:cd02665 218 RNPSAYCLMY 227
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
63-391 |
5.81e-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: 56.38 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 63 LRNLGNTCFMNSILQCLSNTqslrdyclhNSHRRDLNNNNrthtalmeefakliqtmwtsssseavspsefktqiqryap 142
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSI---------GKINTEFDNDD---------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 143 rfvgynQQDAQEFLRFLLDGLHN--EVNRVTVRPRGNTedfdhlpdeekgkkmwSKYLEREDSkivdlFVGQLKSSLTCS 220
Cdd:cd02673 33 ------QQDAHEFLLTLLEAIDDimQVNRTNVPPSNIE----------------IKRLNPLEA-----FKYTIESSYVCI 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 221 ECGYCSTVFDPFWDLSLPIAKKGYGEVSLMDCMRLFTKEDvldgdEKpTCYRCKARRRCTKKfTVQKFPKILVLHLKRFS 300
Cdd:cd02673 86 GCSFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EK-DCSSCKCESAISSE-RIMTFPECLSINLKRYK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 301 EaRIRTSKlstfvnFPMKD-LDLREFASDRSSsavYNLYAVSNHSG-TTMGGHYTAYCCNPENG-EWYTYNDSRVTPMSA 377
Cdd:cd02673 159 L-RIATSD------YLKKNeEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSK 228
|
330
....*....|....*..
gi 2511096478 378 SQVR---SSDAYVLFYE 391
Cdd:cd02673 229 NDVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
262-391 |
2.71e-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: 42.50 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511096478 262 LDGDEKPTCYRCKARRRCTKKFTVQKFPKI----LVLHLKRFSEAR-------IRTSKLSTFVNFPMKDLDLREFASDRS 330
Cdd:cd02672 129 LEKVTKAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQE 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2511096478 331 SSAVYNLYA-VSNHSGTTMGGHYTA----YCCNPENGEWYTYNDSRVTPMsasqvrSSDAYVLFYE 391
Cdd:cd02672 209 SIYKYELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPV------SELAYILLYQ 268
|
|
| |
