|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-363 |
0e+00 |
|
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: 545.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFcrpfrenvlaykaqqkkkENLLTCLADLFHSIATQKKKVGVIPPKKFISRLRKENDLFDN 115
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFDN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 116 YMQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENnkpeltWVHEIFQGTLTNETRCLNCETVSSKDEDF 195
Cdd:cd02663 63 YMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT------WVHEIFQGILTNETRCLTCETVSSRDETF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 196 LDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVV 275
Cdd:cd02663 137 LDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 276 FPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVEKIDAQAIEEFYGltsdISKNSE 355
Cdd:cd02663 217 FPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEFFG----DSPNQA 292
|
....*...
gi 29243896 356 SGYILFYQ 363
Cdd:cd02663 293 TAYVLFYQ 300
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
35-362 |
1.95e-90 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 273.93 E-value: 1.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 35 FGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKE-----NLLTCLADLFHSIaTQKKKVGVIPPKKFISRLRKE 109
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRynkdiNLLCALRDLFKAL-QKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 110 NDLFDNYMQQDAHEFLNYLLNTiadiLQEEKKQEkqngklkngnmnepaeNNKPELTWVHEIFQGTLTNETRCLNCETVS 189
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDG----LHEDLNGN----------------HSTENESLITDLFRGQLKSRLKCLSCGEVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 190 SKDEDFLDLSVDVEQNTSITH------CLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQ 263
Cdd:pfam00443 140 ETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--N 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 264 LHRYTKLSYRVVFPLELRLFNTSSDAVNLD----RMYDLVAVVVHCGSgPNRGHYITIVKS--HGFWLLFDDDIVEKIDA 337
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTEVDE 296
|
330 340
....*....|....*....|....*
gi 29243896 338 QAIEEfygltsdisknSESGYILFY 362
Cdd:pfam00443 297 ETAVL-----------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
36-363 |
3.79e-71 |
|
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: 222.74 E-value: 3.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFcrpfrenvlaykaqqkkkenlltcladlfhsiatqkkkvgvippkkfisrlrkendlfdn 115
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 116 yMQQDAHEFLNYLLNTIADILQEEKKQEkqngklkngnmnepaENNKPELTWVHEIFQGTLTNETRCLNC--ETVSSKDE 193
Cdd:cd02257 21 -EQQDAHEFLLFLLDKLHEELKKSSKRT---------------SDSSSLKSLIHDLFGGKLESTIVCLECghESVSTEPE 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 194 DFLDLSVDVEQ--NTSITHCLRDFSNTETLCSEQKYYCEtCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLhRYTKLS 271
Cdd:cd02257 85 LFLSLPLPVKGlpQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDG-TKEKLN 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 272 YRVVFPLELRLFN------TSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK--SHGFWLLFDDDIVEKIDAQAIEEF 343
Cdd:cd02257 163 TKVSFPLELDLSPylsegeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdpSDGKWYKFNDDKVTEVSEEEVLEF 242
|
330 340
....*....|....*....|
gi 29243896 344 YGLTSdisknseSGYILFYQ 363
Cdd:cd02257 243 GSLSS-------SAYILFYE 255
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
34-363 |
4.46e-66 |
|
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: 212.12 E-value: 4.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 34 YFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN--LLTCLADLFHSIATQKKKVGVippKKFISRLRKEND 111
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNksVPLALQRLFLFLQLSESPVKT---TELTDKTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 112 LFDN-YMQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSS 190
Cdd:cd02659 79 DSLNtFEQHDVQEFFRVLF----DKLEEKLKGTGQEGLIKN-------------------LFGGKLVNYIICKECPHESE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 191 KDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKY-MEQLHRYtK 269
Cdd:cd02659 136 REEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdFETMMRI-K 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 270 LSYRVVFPLEL-----------RLFNTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKS--HGFWLLFDDDIVEKID 336
Cdd:cd02659 215 INDRFEFPLELdmepytekglaKKEGDSEKKDSESYIYELHGVLVHSGDAHG-GHYYSYIKDrdDGKWYKFNDDVVTPFD 293
|
330 340 350
....*....|....*....|....*....|....*..
gi 29243896 337 -AQAIEEFYG---------LTSDISKNSESGYILFYQ 363
Cdd:cd02659 294 pNDAEEECFGgeetqktydSGPRAFKRTTNAYMLFYE 330
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-362 |
5.08e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 198.27 E-value: 5.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENLLTCLADLFHSIATQKKKVG-VIPPKKFISRLRKENDLFD 114
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGpGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 115 NYMQQDAHEFLNYLLNTiadilqeekkqeKQNGKLKNGNMNEPAENNKPELTWVHEIFQGTLTNETRCLNCETVSSKDED 194
Cdd:cd02661 83 IGRQEDAHEFLRYLLDA------------MQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 195 FLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeqlHRYTKLSYRV 274
Cdd:cd02661 151 FLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 275 VFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK-SHGFWLLFDDDIVEKIDAQAIEefygltsdiskn 353
Cdd:cd02661 227 SFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKsSNGKWYNMDDSKVSPVSIETVL------------ 294
|
....*....
gi 29243896 354 SESGYILFY 362
Cdd:cd02661 295 SQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-362 |
4.36e-49 |
|
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: 167.93 E-value: 4.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQAL----YFCRPFRENVLAYKAQQKKKENLLTC-LADLFHSIATQKKKVGVIPPKKFISRLRKEN 110
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpLLRNYFLSDRHSCTCLSCSPNSCLSCaMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 111 DLfDNYMQQDAHEFLNYLLNTIAdilQEEKKQEKQNGKLKNGNmnepaennkpelTWVHEIFQGTLTNETRCLNCETVSS 190
Cdd:cd02660 82 NL-AGYSQQDAHEFFQFLLDQLH---THYGGDKNEANDESHCN------------CIIHQTFSGSLQSSVTCQRCGGVST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 191 KDEDFLDLSVDVEQNT---------------SITHCLRDFSNTETLCSEQkYYCETCCSKQEAQKRMRVKKLPMILALHL 255
Cdd:cd02660 146 TVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 256 KRFKYmEQLHRYTKLSYRVVFPLELRL--FNTSSDAVNLDR-------MYDLVAVVVHCGSgPNRGHYITIVKSH-GFWL 325
Cdd:cd02660 225 KRFEH-SLNKTSRKIDTYVQFPLELNMtpYTSSSIGDTQDSnsldpdyTYDLFAVVVHKGT-LDTGHYTAYCRQGdGQWF 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 29243896 326 LFDDDIVEKIDaqaIEEFYGltsdisknsESGYILFY 362
Cdd:cd02660 303 KFDDAMITRVS---EEEVLK---------SQAYLLFY 327
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-362 |
5.94e-49 |
|
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: 167.60 E-value: 5.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKkkENLLTCLADLFHSIAT------------QKKKVGVIPPKKFI 103
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTED--AELKNMPPDKPHEPQTiidqlqlifaqlQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 104 SRLRkendlFDNYMQQDAHEFLNYLLNTIADILQEEKkqekqNGKLKNgnmnepaennkpeltWVHEIFQGTLTNETRCL 183
Cdd:cd02668 79 KALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSK-----NPDLKN---------------IVQDLFRGEYSYVTQCS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 184 NCETVSSKDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQ 263
Cdd:cd02668 134 KCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 264 LHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK--SHGFWLLFDDDIVEKIDAQAIE 341
Cdd:cd02668 214 TGAKKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdeQTGEWYKFNDEDVEEMPGKPLK 293
|
330 340 350
....*....|....*....|....*....|
gi 29243896 342 E------FYGLTSDISKNSES---GYILFY 362
Cdd:cd02668 294 LgnsedpAKPRKSEIKKGTHSsrtAYMLVY 323
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-362 |
2.68e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 166.22 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENL-LTCLA--DLFHSIATQKkkvgviPPKKFISRLRKENDL 112
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLqSSFLLnpEKYNDELANQ------APRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 113 FDNYMQQDAHEFLNYLLNTIADIlqeekkqekqngklkngnmnepaennkpeltwVHEIFQGTLTNETRCLNCETVSSKD 192
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQEL--------------------------------VEKDFQGQLVLRTRCLECETFTERR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 193 EDFLDLSVDVE-------------------QNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILAL 253
Cdd:cd02671 148 EDFQDISVPVQeselskseesseispdpktEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 254 HLKRFKYMEQLHRY----TKLSYRVVFPLELRLFNTSSDAVNldRMYDLVAVVVHCGSGPNRGHYITIVKshgfWLLFDD 329
Cdd:cd02671 228 HLKCFAANGSEFDCygglSKVNTPLLTPLKLSLEEWSTKPKN--DVYRLFAVVMHSGATISSGHYTAYVR----WLLFDD 301
|
330 340 350
....*....|....*....|....*....|...
gi 29243896 330 DiveKIDAQAIEEFYGLTSDISKNSESGYILFY 362
Cdd:cd02671 302 S---EVKVTEEKDFLEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-363 |
1.36e-45 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 158.81 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN-LLTCLADLFHSIATQKKKVGViPPKKFISRLRKENdlFD 114
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQsVMKKLQLLQAHLMHTQRRAEA-PPDYFLEASRPPW--FT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 115 NYMQQDAHEFLNYLLntiaDILQeekkqekqngklkngnmnepaennkpelTWVHEIFQGTLTNETRCLNCETVSSKDED 194
Cdd:cd02664 78 PGSQQDCSEYLRYLL----DRLH----------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTER 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 195 FLDLSVDVeqnTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRV 274
Cdd:cd02664 126 FRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 275 VFPLELRL-----FNTSSDAVNLDRM--------------YDLVAVVVHCGSGPNRGHYITIVKS--------------- 320
Cdd:cd02664 203 SINEVLSLpvrveSKSSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepk 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 29243896 321 -------HGFWLLFDDDIVEKIDAQAIEEFYGLTSdisknSESGYILFYQ 363
Cdd:cd02664 283 daeendeSKNWYLFNDSRVTFSSFESVQNVTSRFP-----KDTPYILFYE 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-363 |
3.47e-45 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 154.75 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQalyfcrpfrenvlaykaqqkkkenlltCLADlfhsiatqkkkvgvippkkfisrlrkendlfdn 115
Cdd:cd02674 1 GLRNLGNTCYMNSILQ---------------------------CLSA--------------------------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 116 yMQQDAHEFLNYLLNTIADILQEekkqekqngklkngnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSSKDEDF 195
Cdd:cd02674 21 -DQQDAQEFLLFLLDGLHSIIVD--------------------------------LFQGQLKSRLTCLTCGKTSTTFEPF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 196 LDLSVDVEQNT------SITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQlhRYTK 269
Cdd:cd02674 68 TYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG--STRK 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 270 LSYRVVFPLE---LRLFNTSSDAVNLDRmYDLVAVVVHCGSGpNRGHYITIVKSHGF--WLLFDDDIVEKIDaqaieefy 344
Cdd:cd02674 146 LTTPVTFPLNdldLTPYVDTRSFTGPFK-YDLYAVVNHYGSL-NGGHYTAYCKNNETndWYKFDDSRVTKVS-------- 215
|
330
....*....|....*....
gi 29243896 345 gltsDISKNSESGYILFYQ 363
Cdd:cd02674 216 ----ESSVVSSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-363 |
3.16e-42 |
|
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: 148.69 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCrPFRENVLaykaqqkkKENlltcladlfhsiatqkkkvgvipPKKFISRLRKENDLFDN 115
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQT-PALRELL--------SET-----------------------PKELFSQVCRKAPQFKG 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 116 YMQQDAHEFLNYLLNTIadilqeekkqekqngklkngnmnepaennkpeLTWVHEIFQGTLTNETRCLNCETVSSKDEDF 195
Cdd:cd02667 49 YQQQDSHELLRYLLDGL--------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPF 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 196 LDLS----VDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCskqEAQKRMRVKKLPMILALHLKRFKyMEQLHRYTKLS 271
Cdd:cd02667 97 LDLSlprsDEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ-QPRSANLRKVS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 272 YRVVFP--LELRLFNTSSDAVNLDR---MYDLVAVVVHCGSgPNRGHYITIVKSHGFWLLFDDDIVEKIDAQAIEE---- 342
Cdd:cd02667 173 RHVSFPeiLDLAPFCDPKCNSSEDKssvLYRLYGVVEHSGT-MRSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPgsgq 251
|
330 340
....*....|....*....|....*...
gi 29243896 343 -FYGLTSDISKNSES------GYILFYQ 363
Cdd:cd02667 252 wYYISDSDVREVSLEevlkseAYLLFYE 279
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-362 |
2.23e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 131.30 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKE----NLLTCLADLFHSIatqKKKVGVIPPKKFISRLRK--- 108
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANqssdNLTNALRDLFDTM---DKKQEPVPPIEFLQLLRMafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 109 ---ENDLFDNYMQQDAHEFLNYLLNTIADILqeekkqekqngklkngnmnepaENNKPELTWVHEIFQGTLTNETRCL-- 183
Cdd:cd02657 78 qfaEKQNQGGYAQQDAEECWSQLLSVLSQKL----------------------PGAGSKGSFIDQLFGIELETKMKCTes 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 184 -NCETVSSKDEDFLDLSVDVEQNTS-----ITHCLR--DFSNTETLCSEQKYycetccskqeaQKRMRVKKLPMILALHL 255
Cdd:cd02657 136 pDEEEVSTESEYKLQCHISITTEVNylqdgLKKGLEeeIEKHSPTLGRDAIY-----------TKTSRISRLPKYLTVQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 256 KRFKYMEQLHRYTKLSYRVVFPLELRLFntssDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKS--HGFWLLFDDDIVE 333
Cdd:cd02657 205 VRFFWKRDIQKKAKILRKVKFPFELDLY----ELCTPSGYYELVAVITHQGRSADSGHYVAWVRRknDGKWIKFDDDKVS 280
|
330 340
....*....|....*....|....*....
gi 29243896 334 KIDAQAIEEFYGltsdiSKNSESGYILFY 362
Cdd:cd02657 281 EVTEEDILKLSG-----GGDWHIAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
34-345 |
1.66e-30 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 123.06 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 34 YFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKK-KENLLTCLADLFHSIATQKKKVGVippkkfiSRLRKEN-- 110
Cdd:COG5077 193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRgRDSVALALQRLFYNLQTGEEPVDT-------TELTRSFgw 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 111 DLFDNYMQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaennkpeltwvheIFQGTLTNETRCLNCETVSS 190
Cdd:COG5077 266 DSDDSFMQHDIQEFNRVLQ----DNLEKSMRGTVVENALNG-------------------IFVGKMKSYIKCVNVNYESA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 191 KDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETcCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKL 270
Cdd:COG5077 323 RVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 271 SYRVVFPLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKSH--GFWLLFDDDIV-EKIDAQAIEEF 343
Cdd:COG5077 402 NDRYEFPLEIDLLpfldRDADKSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFDDTRVtRATEKEVLEEN 480
|
..
gi 29243896 344 YG 345
Cdd:COG5077 481 FG 482
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-363 |
3.79e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 117.42 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKK-----KENLLTCLADLFHSIATQKKKVGV------------IP 98
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpANDLNCQLIKLADGLLSGRYSKPAslksendpyqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 99 PKKFISRLRKENDLFDNYMQQDAHEFLNYLLNTIAdilQEEKKQEKQNgklkngnmnepaennkpeltwVHEIFQGTLTN 178
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD---RESFKNLGLN---------------------PNDLFKFMIED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 179 ETRCLNCETVSSKDEDFLDLSVDVE--------------QNTSITHCLRDFSNTETLcseqKYYCETCCSKQEAQKRMRV 244
Cdd:cd02658 137 RLECLSCKKVKYTSELSEILSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 245 KKLPMILALHLKRFKYMEQlHRYTKLSYRVVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGPNRGHYITIVK----S 320
Cdd:cd02658 213 KTFPDYLVINMKRFQLLEN-WVPKKLDVPIDVPEELGPGK-----------YELIAFISHKGTSVHSGHYVAHIKkeidG 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 29243896 321 HGFWLLFDDdivEKIdaqaieefyGLTSDISKNSESGYILFYQ 363
Cdd:cd02658 281 EGKWVLFND---EKV---------VASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-363 |
5.74e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 101.29 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFREnvlaykaqqkkkenlltcladlfhsiatqkkkvgvippkkFISRLRKendlfdn 115
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIE----------------------------------------YLEEFLE------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 116 ymQQDAHEFLNYLLNTIADILQEekkqekqngklkngnmnepaennkPeltwvheiFQGTLTNETRCLNCETVSSKDED- 194
Cdd:cd02662 34 --QQDAHELFQVLLETLEQLLKF------------------------P--------FDGLLASRIVCLQCGESSKVRYEs 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 195 FLDLSVDVEQNTSIT-----HCLRDFSNTETLcseQKYYCETCcskQEAqkrmrVKKLPMILALHLKRFKYMEQLHrYTK 269
Cdd:cd02662 80 FTMLSLPVPNQSSGSgttleHCLDDFLSTEII---DDYKCDRC---QTV-----IVRLPQILCIHLSRSVFDGRGT-STK 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 270 LSYRVVFPLELRlfntssdavnlDRMYDLVAVVVHCGSgPNRGHYITIVKSHGFWLLFDDDIV---EKIDAQAIEEFYgL 346
Cdd:cd02662 148 NSCKVSFPERLP-----------KVLYRLRAVVVHYGS-HSSGHYVCYRRKPLFSKDKEPGSFvrmREGPSSTSHPWW-R 214
|
330 340
....*....|....*....|....*.
gi 29243896 347 TSD--ISKNSES-------GYILFYQ 363
Cdd:cd02662 215 ISDttVKEVSESevleqksAYMLFYE 240
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
37-362 |
1.06e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 95.29 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 37 LVNFGNTCYCNSVLQALyfcrpfrenvlaykaqqkkkenlltcladlfhsiatqkkkvgvippkkfiSRLRKENDLFDNY 116
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL--------------------------------------------------SSIGKINTEFDND 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 117 MQQDAHEFLNYLLNTIADILQEEKKQEKQNGklKNGNMNEPAennkpeltwvhEIFQGTLTNETRCLNC---ETVSSKDE 193
Cdd:cd02673 32 DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSN--IEIKRLNPL-----------EAFKYTIESSYVCIGCsfeENVSDVGN 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 194 dflDLSVDVEQNTSITHCLRDFSNTETLCSEQKyyCETcCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYR 273
Cdd:cd02673 99 ---FLDVSMIDNKLDIDELLISNFKTWSPIEKD--CSS-CKCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 274 VVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGPNRGHYITIVKS---HGFWLLFDDDIVEKIDaqaieefyglTSDI 350
Cdd:cd02673 173 IMKKYCGTDAK-----------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEIRPVS----------KNDV 231
|
330
....*....|...
gi 29243896 351 SKN-SESGYILFY 362
Cdd:cd02673 232 STNaRSSGYLIFY 244
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
36-329 |
1.82e-21 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 93.10 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENLLTC-LADLFHSIATQKKK----------VGVIPPKKFIS 104
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCeLGFLFDMLEKAKGKncqasnflraLSSIPEASALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 105 RL--RKENDLFDNY--MQQDaheFLNYLLNTIAdilQEEKKQEKqngklkngnmnepaeNNKPELTWVHEIFQGTLTNET 180
Cdd:pfam13423 82 LLdeDRETNSAISLssLIQS---FNRFLLDQLS---SEENSTPP---------------NPSPAESPLEQLFGIDAETTI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 181 RCLNCETVSSKDEDF--LDLSV--------DVEQNTSITHCLRDFSNTETLcseQKYYCETCCSKQEAQKRMRVKKLPMI 250
Cdd:pfam13423 141 RCSNCGHESVRESSThvLDLIYprkpssnnKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 251 LALHLKRFkymEQLHRYTKLSYRVvFPLELRLF-NTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK---------S 320
Cdd:pfam13423 218 LSLNAALT---NEEWRQLWKTPGW-LPPEIGLTlSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledpT 293
|
....*....
gi 29243896 321 HGFWLLFDD 329
Cdd:pfam13423 294 ESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
207-365 |
1.90e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.11 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 207 SIT--HCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQLHRYTKLSYRVVFPLELRLFN 284
Cdd:COG5560 674 TITlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSS--VRSFRDKIDDLVEYPIDDLDLS 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 285 TSSDAVNLDRM-YDLVAVVVHCGsGPNRGHYITIVK--SHGFWLLFDDDIVEKIDAQaieefygltsDISKnsESGYILF 361
Cdd:COG5560 752 GVEYMVDDPRLiYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRITEVDPE----------DSVT--SSAYVLF 818
|
....
gi 29243896 362 YQSR 365
Cdd:COG5560 819 YRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
36-362 |
2.15e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 87.16 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPfrenvlaykAQQKKKENLLTCLADLfhsiatQKKKVGVIPPKKFISRLR-------- 107
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLP---------KLDELLDDLSKELKVL------KNVIRKPEPDLNQEEALKlftalwss 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 108 ---KENDLFDNYMQQDAHEFLNYLL--------NTIADILQEEKKQEKQNGKlknGNMNEpAENNKPELTWVHEifQGTL 176
Cdd:COG5533 66 kehKVGWIPPMGSQEDAHELLGKLLdelkldlvNSFTIRIFKTTKDKKKTST---GDWFD-IIIELPDQTWVNN--LKTL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 177 TNetrCLNCETVSSKDEDFLDLSVDVEQNTSIthclrdfsntetlcsEQKYYcetccskqeaqkrMRVKKLPMILALHLK 256
Cdd:COG5533 140 QE---FIDNMEELVDDETGVKAKENEELEVQA---------------KQEYE-------------VSFVKLPKILTIQLK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 257 RFKYmeqLHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSgPNRGHYITIVKSHGFWLLFDDDIVEKI- 335
Cdd:COG5533 189 RFAN---LGGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGS-LEGGHYIAYVKKGGKWEKANDSDVTPVs 264
|
330 340
....*....|....*....|....*..
gi 29243896 336 DAQAIEEfygltsdiskNSESGYILFY 362
Cdd:COG5533 265 EEEAINE----------KAKNAYLYFY 281
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
34-340 |
1.61e-17 |
|
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: 83.52 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 34 YFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN---LLTCLADLFHSIATQKKKVGVIPPKKF---ISRLR 107
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRkseLVKRLSELIRKIWNPRNFKGHVSPHELlqaVSKVS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 108 KENdlFDNYMQQDAHEFLNYLLNTIadilqeekkqEKQNGKLKNGNMNEpaennkpeltwVHEIFQGTLTNETRCLNCET 187
Cdd:cd02669 199 KKK--FSITEQSDPVEFLSWLLNTL----------HKDLGGSKKPNSSI-----------IHDCFQGKVQIETQKIKPHA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 188 VS-SKDEDFLDLSVDVEQNTSITHCLR---------DFSNTETLCSE-------QKYYCETCCSKQEAQKRMRVKKLPMI 250
Cdd:cd02669 256 EEeGSKDKFFKDSRVKKTSVSPFLLLTldlpppplfKDGNEENIIPQvplkqllKKYDGKTETELKDSLKRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 251 LALHLKRF-KYMEQLHRYTKLsyrVVFPLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIV--KSHGF 323
Cdd:cd02669 336 LIFHIKRFsKNNFFKEKNPTI---VNFPIKNLDLsdyvHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrhKSTNK 412
|
330
....*....|....*..
gi 29243896 324 WLLFDDDIVEKIDAQAI 340
Cdd:cd02669 413 WFEIQDLNVKEVLPQLI 429
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
36-200 |
3.44e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 73.76 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN--------LLTCLADLFHSIATQkkKVGVIPPKKFISRLR 107
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEnplgmhgsVASAYADLIKQLYDG--NLHAFTPSGFKKTIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 108 KENDLFDNYMQQDAHEFLNYLLNTIADILQEEKKQEkQNGKLKNGNMNEPAENNKPELTW----------VHEIFQGTLT 177
Cdd:COG5560 345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKP-YTSKPDLSPGDDVVVKKKAKECWwehlkrndsiITDLFQGMYK 423
|
170 180
....*....|....*....|...
gi 29243896 178 NETRCLNCETVSSKDEDFLDLSV 200
Cdd:COG5560 424 STLTCPGCGSVSITFDPFMDLTL 446
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-343 |
1.09e-07 |
|
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: 52.88 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYkaQQKKKENLLTCLADlfHSIATQKK-KVGVIPPKKFISRLRKendLFd 114
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNF--DESKAELASDYPTE--RRIGGREVsRSELQRSNQFVYELRS---LF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 115 NYM--------------------QQDAHEFL---------------NYLLNTIADILQEEKKQEKQ--NGKLKNgNMNEP 157
Cdd:cd02666 75 NDLihsntrsvtpskelaylalrQQDVTECIdnvlfqlevalepisNAFAGPDTEDDKEQSDLIKRlfSGKTKQ-QLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 158 AENNKPELTWVHEIFQGTLTN--ETRCLNCETVSSKD-EDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYcetcCS 234
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLVDvgKKGREIVVLLEPKDlYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELIS----MD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 235 KQEAQKrmrVKKLPMILALHLKRFKYMEQLHRYTKLSyrvvfplELRLFNTSSDAVNLDRMYDLVAVVVHCGSGpNRGHY 314
Cdd:cd02666 230 RYELPS---SIDDIDELIREAIQSESSLVRQAQNELA-------ELKHEIEKQFDDLKSYGYRLHAVFIHRGEA-SSGHY 298
|
330 340 350
....*....|....*....|....*....|.
gi 29243896 315 ITIVKSH--GFWLLFDDDIVEKIDAQAIEEF 343
Cdd:cd02666 299 WVYIKDFeeNVWRKYNDETVTVVPASEVFLF 329
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-362 |
1.15e-07 |
|
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: 52.18 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 118 QQDAHEFLNYLLNTIADILQEEkkqekqngklkngnMNEPAENNKPELTWVhEIFQGTLTNE-----TRCLNCETvsskd 192
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAA--------------AEAISPGEKSKNPMV-QLFYGTFLTEgvlegKPFCNCET----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 193 edFLDLSVDVEQNTSITHCLRDFS---NTETLCSEQkyycetccSKQEAQKRMrVKKLPMILALHLKRFKYMEQlhRYTK 269
Cdd:cd02665 82 --FGQYPLQVNGYGNLHECLEAAMfegEVELLPSDH--------SVKSGQERW-FTELPPVLTFELSRFEFNQG--RPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 270 LSYRVVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGpNRGHYITIV--KSHGFWLLFDDDIVEKIDAQAIE-EFYGL 346
Cdd:cd02665 149 IHDKLEFPQIIQQVP-----------YELHAVLVHEGQA-NAGHYWAYIykQSRQEWEKYNDISVTESSWEEVErDSFGG 216
|
250
....*....|....*.
gi 29243896 347 TSDIsknseSGYILFY 362
Cdd:cd02665 217 GRNP-----SAYCLMY 227
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
34-363 |
2.66e-07 |
|
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: 51.36 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 34 YFGLVNFGNTCYCNSVLQALYFCRPFReNVLAYKAQQKKKEN-LLTCLADLFhsiATQKKKvgvippkkfisrlrkendl 112
Cdd:cd02672 15 YAGLENHITNSYCNSLLQLLYFIPPFR-NFTAIILVACPKEScLLCELGYLF---STLIQN------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 113 fdnymqqdaheFLNYLLNTIADILQEEKKQEKQNGKLKNgnmnepaENNKPELtwvHEIFQGTLTNetrcLNCETVsskd 192
Cdd:cd02672 72 -----------FTRFLLETISQDQLGTPFSCGTSRNSVS-------LLYTLSL---PLGSTKTSKE----STFLQL---- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 193 edfLDLSVDVEQNTsithclrdfsntetlcseqKYYCETCCSKQEAQKRMRVKKLPMI----LALHLKRFKYME-----Q 263
Cdd:cd02672 123 ---LKRSLDLEKVT-------------------KAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 264 LHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIV------KSHGFWLLFDDDIVEKIDa 337
Cdd:cd02672 181 LPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVikvneeSTHGRWYLFNDFLVTPVS- 259
|
330 340
....*....|....*....|....*.
gi 29243896 338 qaieefygltsdisknsESGYILFYQ 363
Cdd:cd02672 260 -----------------ELAYILLYQ 268
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-363 |
2.84e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 41.74 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243896 245 KKLPMILALHLKRFKYMEQLHRytKLSYRVVFPLELRL----------------------FNTSSDAVNLDRMYDLVAVV 302
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAV 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29243896 303 VHCGSGPNRGHYITIVKS-------------HGFWLLFDDDIVEKidaqaiEEFYGLTSDISKNSESGYILFYQ 363
Cdd:cd02670 174 CHRGTSLETGHYVAFVRYgsysltetdneayNAQWVFFDDMADRD------GVSNGFNIPAARLLEDPYMLFYQ 241
|
|
| |
