|
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: 545.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFcrpfrenvlaykaqqkkkENLLTCLADLFHSIATQKKKVGVIPPKKFISRLRKENDLFDN 115
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFDN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 116 YMQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENskpeltWVHEIFQGTLTNETRCLNCETVSSKDEDF 195
Cdd:cd02663 63 YMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT------WVHEIFQGILTNETRCLTCETVSSRDETF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 196 LDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVV 275
Cdd:cd02663 137 LDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 276 FPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVEKIDAQAIEEFYGltsdISKNSE 355
Cdd:cd02663 217 FPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEFFG----DSPNQA 292
|
....*...
gi 1018740110 356 SGYILFYQ 363
Cdd:cd02663 293 TAYVLFYQ 300
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
35-362 |
8.83e-91 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 274.70 E-value: 8.83e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 35 FGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKE-----NLLTCLADLFHSIaTQKKKVGVIPPKKFISRLRKE 109
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRynkdiNLLCALRDLFKAL-QKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 110 NDLFDNYMQQDAHEFLNYLLNTiadiLQEEKKQEkqngklkngnmnepaeNSKPELTWVHEIFQGTLTNETRCLNCETVS 189
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDG----LHEDLNGN----------------HSTENESLITDLFRGQLKSRLKCLSCGEVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 190 SKDEDFLDLSVDVEQNTSITH------CLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQ 263
Cdd:pfam00443 140 ETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY--N 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 264 LHRYTKLSYRVVFPLELRLFNTSSDAVNLD----RMYDLVAVVVHCGSgPNRGHYITIVKS--HGFWLLFDDDIVEKIDA 337
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTEVDE 296
|
330 340
....*....|....*....|....*
gi 1018740110 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 |
4.00e-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: 4.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFcrpfrenvlaykaqqkkkenlltcladlfhsiatqkkkvgvippkkfisrlrkendlfdn 115
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 116 yMQQDAHEFLNYLLNTIADILQEEKKQEkqngklkngnmnepaENSKPELTWVHEIFQGTLTNETRCLNC--ETVSSKDE 193
Cdd:cd02257 21 -EQQDAHEFLLFLLDKLHEELKKSSKRT---------------SDSSSLKSLIHDLFGGKLESTIVCLECghESVSTEPE 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 194 DFLDLSVDVEQ--NTSITHCLRDFSNTETLCSEQKYYCEtCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLhRYTKLS 271
Cdd:cd02257 85 LFLSLPLPVKGlpQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDG-TKEKLN 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 272 YRVVFPLELRLFN------TSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK--SHGFWLLFDDDIVEKIDAQAIEEF 343
Cdd:cd02257 163 TKVSFPLELDLSPylsegeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdpSDGKWYKFNDDKVTEVSEEEVLEF 242
|
330 340
....*....|....*....|
gi 1018740110 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 |
3.80e-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: 212.50 E-value: 3.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 34 YFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN--LLTCLADLFHSIATQKKKVGVippKKFISRLRKEND 111
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNksVPLALQRLFLFLQLSESPVKT---TELTDKTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 112 LFDN-YMQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaenskpeltwvheIFQGTLTNETRCLNCETVSS 190
Cdd:cd02659 79 DSLNtFEQHDVQEFFRVLF----DKLEEKLKGTGQEGLIKN-------------------LFGGKLVNYIICKECPHESE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 191 KDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKY-MEQLHRYtK 269
Cdd:cd02659 136 REEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdFETMMRI-K 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 270 LSYRVVFPLEL-----------RLFNTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKS--HGFWLLFDDDIVEKID 336
Cdd:cd02659 215 INDRFEFPLELdmepytekglaKKEGDSEKKDSESYIYELHGVLVHSGDAHG-GHYYSYIKDrdDGKWYKFNDDVVTPFD 293
|
330 340 350
....*....|....*....|....*....|....*..
gi 1018740110 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 |
9.13e-62 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 200.19 E-value: 9.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENLLTCLADLFHSIATQKKKVG-VIPPKKFISRLRKENDLFD 114
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGpGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 115 NYMQQDAHEFLNYLLNTiadilqeekkqeKQNGKLKNGNMNEPAENSKPELTWVHEIFQGTLTNETRCLNCETVSSKDED 194
Cdd:cd02661 83 IGRQEDAHEFLRYLLDA------------MQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 195 FLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeqlHRYTKLSYRV 274
Cdd:cd02661 151 FLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 275 VFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK-SHGFWLLFDDDIVEKIDAQAIEefygltsdiskn 353
Cdd:cd02661 227 SFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKsSNGKWYNMDDSKVSPVSIETVL------------ 294
|
....*....
gi 1018740110 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 |
4.60e-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: 4.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQAL----YFCRPFRENVLAYKAQQKKKENLLTC-LADLFHSIATQKKKVGVIPPKKFISRLRKEN 110
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpLLRNYFLSDRHSCTCLSCSPNSCLSCaMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 111 DLfDNYMQQDAHEFLNYLLNTIAdilQEEKKQEKQNGKLKNGNmnepaenskpelTWVHEIFQGTLTNETRCLNCETVSS 190
Cdd:cd02660 82 NL-AGYSQQDAHEFFQFLLDQLH---THYGGDKNEANDESHCN------------CIIHQTFSGSLQSSVTCQRCGGVST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 191 KDEDFLDLSVDVEQNT---------------SITHCLRDFSNTETLCSEQkYYCETCCSKQEAQKRMRVKKLPMILALHL 255
Cdd:cd02660 146 TVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 256 KRFKYmEQLHRYTKLSYRVVFPLELRL--FNTSSDAVNLDR-------MYDLVAVVVHCGSgPNRGHYITIVKSH-GFWL 325
Cdd:cd02660 225 KRFEH-SLNKTSRKIDTYVQFPLELNMtpYTSSSIGDTQDSnsldpdyTYDLFAVVVHKGT-LDTGHYTAYCRQGdGQWF 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 1018740110 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 |
5.70e-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: 5.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKkkENLLTCLADLFHSIAT------------QKKKVGVIPPKKFI 103
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTED--AELKNMPPDKPHEPQTiidqlqlifaqlQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 104 SRLRkendlFDNYMQQDAHEFLNYLLNTIADILQEEKkqekqNGKLKNgnmnepaenskpeltWVHEIFQGTLTNETRCL 183
Cdd:cd02668 79 KALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSK-----NPDLKN---------------IVQDLFRGEYSYVTQCS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 184 NCETVSSKDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQ 263
Cdd:cd02668 134 KCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 264 LHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK--SHGFWLLFDDDIVEKIDAQAIE 341
Cdd:cd02668 214 TGAKKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdeQTGEWYKFNDEDVEEMPGKPLK 293
|
330 340 350
....*....|....*....|....*....|
gi 1018740110 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 |
2.89e-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: 165.84 E-value: 2.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENL-LTCLA--DLFHSIATQKkkvgviPPKKFISRLRKENDL 112
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLqSSFLLnpEKYNDELANQ------APRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 113 FDNYMQQDAHEFLNYLLNTIADIlqeekkqekqngklkngnmnepaenskpeltwVHEIFQGTLTNETRCLNCETVSSKD 192
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQEL--------------------------------VEKDFQGQLVLRTRCLECETFTERR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 193 EDFLDLSVDVE-------------------QNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILAL 253
Cdd:cd02671 148 EDFQDISVPVQeselskseesseispdpktEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 254 HLKRFKYMEQLHRY----TKLSYRVVFPLELRLFNTSSDAVNldRMYDLVAVVVHCGSGPNRGHYITIVKshgfWLLFDD 329
Cdd:cd02671 228 HLKCFAANGSEFDCygglSKVNTPLLTPLKLSLEEWSTKPKN--DVYRLFAVVMHSGATISSGHYTAYVR----WLLFDD 301
|
330 340 350
....*....|....*....|....*....|...
gi 1018740110 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 |
1.51e-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: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN-LLTCLADLFHSIATQKKKVGViPPKKFISRLRKENdlFD 114
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQsVMKKLQLLQAHLMHTQRRAEA-PPDYFLEASRPPW--FT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 115 NYMQQDAHEFLNYLLntiaDILQeekkqekqngklkngnmnepaenskpelTWVHEIFQGTLTNETRCLNCETVSSKDED 194
Cdd:cd02664 78 PGSQQDCSEYLRYLL----DRLH----------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTER 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 195 FLDLSVDVeqnTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRV 274
Cdd:cd02664 126 FRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 275 VFPLELRL-----FNTSSDAVNLDRM--------------YDLVAVVVHCGSGPNRGHYITIVKS--------------- 320
Cdd:cd02664 203 SINEVLSLpvrveSKSSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepk 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1018740110 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 |
3.40e-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: 3.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQalyfcrpfrenvlaykaqqkkkenlltCLADlfhsiatqkkkvgvippkkfisrlrkendlfdn 115
Cdd:cd02674 1 GLRNLGNTCYMNSILQ---------------------------CLSA--------------------------------- 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 116 yMQQDAHEFLNYLLNTIADILQEekkqekqngklkngnmnepaenskpeltwvheIFQGTLTNETRCLNCETVSSKDEDF 195
Cdd:cd02674 21 -DQQDAQEFLLFLLDGLHSIIVD--------------------------------LFQGQLKSRLTCLTCGKTSTTFEPF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 196 LDLSVDVEQNT------SITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQlhRYTK 269
Cdd:cd02674 68 TYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG--STRK 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 270 LSYRVVFPLE---LRLFNTSSDAVNLDRmYDLVAVVVHCGSGpNRGHYITIVKSHGF--WLLFDDDIVEKIDaqaieefy 344
Cdd:cd02674 146 LTTPVTFPLNdldLTPYVDTRSFTGPFK-YDLYAVVNHYGSL-NGGHYTAYCKNNETndWYKFDDSRVTKVS-------- 215
|
330
....*....|....*....
gi 1018740110 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 |
3.44e-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: 148.30 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCrPFRENVLaykaqqkkKENlltcladlfhsiatqkkkvgvipPKKFISRLRKENDLFDN 115
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQT-PALRELL--------SET-----------------------PKELFSQVCRKAPQFKG 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 116 YMQQDAHEFLNYLLNTIadilqeekkqekqngklkngnmnepaenskpeLTWVHEIFQGTLTNETRCLNCETVSSKDEDF 195
Cdd:cd02667 49 YQQQDSHELLRYLLDGL--------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPF 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 196 LDLS----VDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCskqEAQKRMRVKKLPMILALHLKRFKyMEQLHRYTKLS 271
Cdd:cd02667 97 LDLSlprsDEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ-QPRSANLRKVS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 272 YRVVFP--LELRLFNTSSDAVNLDR---MYDLVAVVVHCGSgPNRGHYITIVKSHGFWLLFDDDIVEKIDAQAIEE---- 342
Cdd:cd02667 173 RHVSFPeiLDLAPFCDPKCNSSEDKssvLYRLYGVVEHSGT-MRSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPgsgq 251
|
330 340
....*....|....*....|....*...
gi 1018740110 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 |
2.40e-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: 130.91 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKE----NLLTCLADLFHSIatqKKKVGVIPPKKFISRLRK--- 108
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANqssdNLTNALRDLFDTM---DKKQEPVPPIEFLQLLRMafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 109 ---ENDLFDNYMQQDAHEFLNYLLNTIADILqeekkqekqngklkngnmnePAENSKPEltWVHEIFQGTLTNETRCL-- 183
Cdd:cd02657 78 qfaEKQNQGGYAQQDAEECWSQLLSVLSQKL--------------------PGAGSKGS--FIDQLFGIELETKMKCTes 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 184 -NCETVSSKDEDFLDLSVDVEQNTS-----ITHCLR--DFSNTETLCSEQKYycetccskqeaQKRMRVKKLPMILALHL 255
Cdd:cd02657 136 pDEEEVSTESEYKLQCHISITTEVNylqdgLKKGLEeeIEKHSPTLGRDAIY-----------TKTSRISRLPKYLTVQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 256 KRFKYMEQLHRYTKLSYRVVFPLELRLFntssDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKS--HGFWLLFDDDIVE 333
Cdd:cd02657 205 VRFFWKRDIQKKAKILRKVKFPFELDLY----ELCTPSGYYELVAVITHQGRSADSGHYVAWVRRknDGKWIKFDDDKVS 280
|
330 340
....*....|....*....|....*....
gi 1018740110 334 KIDAQAIEEFYGltsdiSKNSESGYILFY 362
Cdd:cd02657 281 EVTEEDILKLSG-----GGDWHIAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
34-345 |
1.62e-30 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 123.06 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 34 YFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKK-KENLLTCLADLFHSIATQKKKVGVippkkfiSRLRKEN-- 110
Cdd:COG5077 193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRgRDSVALALQRLFYNLQTGEEPVDT-------TELTRSFgw 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 111 DLFDNYMQQDAHEFLNYLLntiaDILQEEKKQEKQNGKLKNgnmnepaenskpeltwvheIFQGTLTNETRCLNCETVSS 190
Cdd:COG5077 266 DSDDSFMQHDIQEFNRVLQ----DNLEKSMRGTVVENALNG-------------------IFVGKMKSYIKCVNVNYESA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 191 KDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETcCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKL 270
Cdd:COG5077 323 RVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 271 SYRVVFPLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNrGHYITIVKSH--GFWLLFDDDIV-EKIDAQAIEEF 343
Cdd:COG5077 402 NDRYEFPLEIDLLpfldRDADKSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFDDTRVtRATEKEVLEEN 480
|
..
gi 1018740110 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 |
2.42e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 117.81 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKK-----KENLLTCLADLFHSIATQKKKVGV------------IP 98
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpANDLNCQLIKLADGLLSGRYSKPAslksendpyqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 99 PKKFISRLRKENDLFDNYMQQDAHEFLNYLLntiaDILQEEKKQekqngklkngnmnepaeNSKPELTwvhEIFQGTLTN 178
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLI----DKLDRESFK-----------------NLGLNPN---DLFKFMIED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 179 ETRCLNCETVSSKDEDFLDLSVDVE--------------QNTSITHCLRDFSNTETLcseqKYYCETCCSKQEAQKRMRV 244
Cdd:cd02658 137 RLECLSCKKVKYTSELSEILSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 245 KKLPMILALHLKRFKYMEQlHRYTKLSYRVVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGPNRGHYITIVK----S 320
Cdd:cd02658 213 KTFPDYLVINMKRFQLLEN-WVPKKLDVPIDVPEELGPGK-----------YELIAFISHKGTSVHSGHYVAHIKkeidG 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1018740110 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 |
4.78e-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: 101.67 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFREnvlaykaqqkkkenlltcladlfhsiatqkkkvgvippkkFISRLRKendlfdn 115
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIE----------------------------------------YLEEFLE------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 116 ymQQDAHEFLNYLLNTIADILqeekkqekqngklkngnmnepaenSKPeltwvheiFQGTLTNETRCLNCETVSSKDED- 194
Cdd:cd02662 34 --QQDAHELFQVLLETLEQLL------------------------KFP--------FDGLLASRIVCLQCGESSKVRYEs 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 195 FLDLSVDVEQNTSIT-----HCLRDFSNTETLcseQKYYCETCcskQEAqkrmrVKKLPMILALHLKRFKYMEQLHrYTK 269
Cdd:cd02662 80 FTMLSLPVPNQSSGSgttleHCLDDFLSTEII---DDYKCDRC---QTV-----IVRLPQILCIHLSRSVFDGRGT-STK 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 270 LSYRVVFPLELRlfntssdavnlDRMYDLVAVVVHCGSgPNRGHYITIVKSHGFWLLFDDDIV---EKIDAQAIEEFYgL 346
Cdd:cd02662 148 NSCKVSFPERLP-----------KVLYRLRAVVVHYGS-HSSGHYVCYRRKPLFSKDKEPGSFvrmREGPSSTSHPWW-R 214
|
330 340
....*....|....*....|....*.
gi 1018740110 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 1018740110 37 LVNFGNTCYCNSVLQALyfcrpfrenvlaykaqqkkkenlltcladlfhsiatqkkkvgvippkkfiSRLRKENDLFDNY 116
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL--------------------------------------------------SSIGKINTEFDND 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 117 MQQDAHEFLNYLLNTIADILQEEKKQEKQNGklKNGNMNEPAenskpeltwvhEIFQGTLTNETRCLNC---ETVSSKDE 193
Cdd:cd02673 32 DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSN--IEIKRLNPL-----------EAFKYTIESSYVCIGCsfeENVSDVGN 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 194 dflDLSVDVEQNTSITHCLRDFSNTETLCSEQKyyCETcCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYR 273
Cdd:cd02673 99 ---FLDVSMIDNKLDIDELLISNFKTWSPIEKD--CSS-CKCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 274 VVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGPNRGHYITIVKS---HGFWLLFDDDIVEKIDaqaieefyglTSDI 350
Cdd:cd02673 173 IMKKYCGTDAK-----------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEIRPVS----------KNDV 231
|
330
....*....|...
gi 1018740110 351 SKN-SESGYILFY 362
Cdd:cd02673 232 STNaRSSGYLIFY 244
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
36-329 |
1.68e-21 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 93.49 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENLLTC-LADLFHSIATQKKK----------VGVIPPKKFIS 104
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCeLGFLFDMLEKAKGKncqasnflraLSSIPEASALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 105 RL--RKENDLFDNY--MQQDaheFLNYLLNTIAdilQEEKKQEKqngklkngnmnepaeNSKPELTWVHEIFQGTLTNET 180
Cdd:pfam13423 82 LLdeDRETNSAISLssLIQS---FNRFLLDQLS---SEENSTPP---------------NPSPAESPLEQLFGIDAETTI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 181 RCLNCETVSSKDEDF--LDLSV--------DVEQNTSITHCLRDFSNTETLcseQKYYCETCCSKQEAQKRMRVKKLPMI 250
Cdd:pfam13423 141 RCSNCGHESVRESSThvLDLIYprkpssnnKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 251 LALHLKRFkymEQLHRYTKLSYRVvFPLELRLF-NTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVK---------S 320
Cdd:pfam13423 218 LSLNAALT---NEEWRQLWKTPGW-LPPEIGLTlSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledpT 293
|
....*....
gi 1018740110 321 HGFWLLFDD 329
Cdd:pfam13423 294 ESQWYLFND 302
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
207-365 |
1.95e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.11 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 207 SIT--HCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYmeQLHRYTKLSYRVVFPLELRLFN 284
Cdd:COG5560 674 TITlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSS--VRSFRDKIDDLVEYPIDDLDLS 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 285 TSSDAVNLDRM-YDLVAVVVHCGsGPNRGHYITIVK--SHGFWLLFDDDIVEKIDAQaieefygltsDISKnsESGYILF 361
Cdd:COG5560 752 GVEYMVDDPRLiYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRITEVDPE----------DSVT--SSAYVLF 818
|
....
gi 1018740110 362 YQSR 365
Cdd:COG5560 819 YRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
36-362 |
3.85e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.09 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPfrenvlaykAQQKKKENLLTCLADLfhsiatQKKKVGVIPPKKFISRLR-------- 107
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLP---------KLDELLDDLSKELKVL------KNVIRKPEPDLNQEEALKlftalwss 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 108 ---KENDLFDNYMQQDAHEFLNYLL--------NTIADILQEEKKQEKQNGKlknGNMNEpAENSKPELTWVHEifQGTL 176
Cdd:COG5533 66 kehKVGWIPPMGSQEDAHELLGKLLdelkldlvNSFTIRIFKTTKDKKKTST---GDWFD-IIIELPDQTWVNN--LKTL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 177 TNetrCLNCETVSSKDEDFLDLSVDVEQNTSIthclrdfsntetlcsEQKYYcetccskqeaqkrMRVKKLPMILALHLK 256
Cdd:COG5533 140 QE---FIDNMEELVDDETGVKAKENEELEVQA---------------KQEYE-------------VSFVKLPKILTIQLK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 257 RFKYmeqLHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSgPNRGHYITIVKSHGFWLLFDDDIVEKI- 335
Cdd:COG5533 189 RFAN---LGGNQKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQGS-LEGGHYIAYVKKGGKWEKANDSDVTPVs 264
|
330 340
....*....|....*....|....*..
gi 1018740110 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 |
1.50e-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: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 34 YFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN---LLTCLADLFHSIATQKKKVGVIPPKKF---ISRLR 107
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRkseLVKRLSELIRKIWNPRNFKGHVSPHELlqaVSKVS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 108 KENdlFDNYMQQDAHEFLNYLLNTIadilqeekkqEKQNGKLKNGNMNEpaenskpeltwVHEIFQGTLTNETRCLNCET 187
Cdd:cd02669 199 KKK--FSITEQSDPVEFLSWLLNTL----------HKDLGGSKKPNSSI-----------IHDCFQGKVQIETQKIKPHA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 188 VS-SKDEDFLDLSVDVEQNTSITHCLR---------DFSNTETLCSE-------QKYYCETCCSKQEAQKRMRVKKLPMI 250
Cdd:cd02669 256 EEeGSKDKFFKDSRVKKTSVSPFLLLTldlpppplfKDGNEENIIPQvplkqllKKYDGKTETELKDSLKRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 251 LALHLKRF-KYMEQLHRYTKLsyrVVFPLELRLF----NTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIV--KSHGF 323
Cdd:cd02669 336 LIFHIKRFsKNNFFKEKNPTI---VNFPIKNLDLsdyvHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrhKSTNK 412
|
330
....*....|....*..
gi 1018740110 324 WLLFDDDIVEKIDAQAI 340
Cdd:cd02669 413 WFEIQDLNVKEVLPQLI 429
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
36-200 |
2.87e-14 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 74.15 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKEN--------LLTCLADLFHSIATQkkKVGVIPPKKFISRLR 107
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEnplgmhgsVASAYADLIKQLYDG--NLHAFTPSGFKKTIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 108 KENDLFDNYMQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENSKPELTWVH---------EIFQGTLTN 178
Cdd:COG5560 345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWEHlkrndsiitDLFQGMYKS 424
|
170 180
....*....|....*....|..
gi 1018740110 179 ETRCLNCETVSSKDEDFLDLSV 200
Cdd:COG5560 425 TLTCPGCGSVSITFDPFMDLTL 446
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
34-363 |
1.06e-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: 52.51 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 34 YFGLVNFGNTCYCNSVLQALYFCRPFReNVLAYKAQQKKKEN-LLTCLADLFhsiATQKKKvgvippkkfisrlrkendl 112
Cdd:cd02672 15 YAGLENHITNSYCNSLLQLLYFIPPFR-NFTAIILVACPKEScLLCELGYLF---STLIQN------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 113 fdnymqqdaheFLNYLLNTIadilqeekkQEKQNGKLKNGNMNEPAENSKPELTwVHEIFQGTLTNetrcLNCETVsskd 192
Cdd:cd02672 72 -----------FTRFLLETI---------SQDQLGTPFSCGTSRNSVSLLYTLS-LPLGSTKTSKE----STFLQL---- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 193 edfLDLSVDVEQNTsithclrdfsntetlcseqKYYCETCCSKQEAQKRMRVKKLPMI----LALHLKRFKYME-----Q 263
Cdd:cd02672 123 ---LKRSLDLEKVT-------------------KAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 264 LHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIV------KSHGFWLLFDDDIVEKIDa 337
Cdd:cd02672 181 LPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVikvneeSTHGRWYLFNDFLVTPVS- 259
|
330 340
....*....|....*....|....*.
gi 1018740110 338 qaieefygltsdisknsESGYILFYQ 363
Cdd:cd02672 260 -----------------ELAYILLYQ 268
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
118-362 |
1.81e-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: 51.40 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 118 QQDAHEFLNYLLNTIADILQEEKkqekqngklkngNMNEPAENSKPELTwvhEIFQGTLTNE-----TRCLNCETvsskd 192
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAA------------EAISPGEKSKNPMV---QLFYGTFLTEgvlegKPFCNCET----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 193 edFLDLSVDVEQNTSITHCLRDFS---NTETLCSEQkyycetccSKQEAQKRMrVKKLPMILALHLKRFKYMEQlhRYTK 269
Cdd:cd02665 82 --FGQYPLQVNGYGNLHECLEAAMfegEVELLPSDH--------SVKSGQERW-FTELPPVLTFELSRFEFNQG--RPEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 270 LSYRVVFPLELRLFNtssdavnldrmYDLVAVVVHCGSGpNRGHYITIV--KSHGFWLLFDDDIVEKIDAQAIE-EFYGL 346
Cdd:cd02665 149 IHDKLEFPQIIQQVP-----------YELHAVLVHEGQA-NAGHYWAYIykQSRQEWEKYNDISVTESSWEEVErDSFGG 216
|
250
....*....|....*.
gi 1018740110 347 TSDIsknseSGYILFY 362
Cdd:cd02665 217 GRNP-----SAYCLMY 227
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-343 |
3.86e-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: 51.34 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 36 GLVNFGNTCYCNSVLQALYFCRPFRENVLAYkaQQKKKENLLTCLADlfHSIATQKK-KVGVIPPKKFISRLRKendLFd 114
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNF--DESKAELASDYPTE--RRIGGREVsRSELQRSNQFVYELRS---LF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 115 NYM--------------------QQDAHEFL---------------NYLLNTIADILQEEKKQEKQ--NGKLKNgNMNEP 157
Cdd:cd02666 75 NDLihsntrsvtpskelaylalrQQDVTECIdnvlfqlevalepisNAFAGPDTEDDKEQSDLIKRlfSGKTKQ-QLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 158 AENSKPELTWVHEIFQGTLTN--ETRCLNCETVSSKD-EDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYcetcCS 234
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLVDvgKKGREIVVLLEPKDlYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELIS----MD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 235 KQEAQKrmrVKKLPMILALHLKRFKYMEQLHRYTKLSyrvvfplELRLFNTSSDAVNLDRMYDLVAVVVHCGSGpNRGHY 314
Cdd:cd02666 230 RYELPS---SIDDIDELIREAIQSESSLVRQAQNELA-------ELKHEIEKQFDDLKSYGYRLHAVFIHRGEA-SSGHY 298
|
330 340 350
....*....|....*....|....*....|.
gi 1018740110 315 ITIVKSH--GFWLLFDDDIVEKIDAQAIEEF 343
Cdd:cd02666 299 WVYIKDFeeNVWRKYNDETVTVVPASEVFLF 329
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-363 |
2.92e-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: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018740110 245 KKLPMILALHLKRFKYMEQLHRytKLSYRVVFPLELRL----------------------FNTSSDAVNLDRMYDLVAVV 302
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQ--KMFKKILIPDEIDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAV 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1018740110 303 VHCGSGPNRGHYITIVKS-------------HGFWLLFDDDIVEKidaqaiEEFYGLTSDISKNSESGYILFYQ 363
Cdd:cd02670 174 CHRGTSLETGHYVAFVRYgsysltetdneayNAQWVFFDDMADRD------GVSNGFNIPAARLLEDPYMLFYQ 241
|
|
| |
