|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-342 |
1.06e-125 |
|
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: 390.08 E-value: 1.06e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 39 NLSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEElgsledkDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTIDLT 118
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTE-------DDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 119 DSFGWTNDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNVSGL 198
Cdd:cd02659 74 RSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 199 EDELCNmYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFCE 278
Cdd:cd02659 154 EESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310688895 279 QSE---------LDDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCQEeisDTNVNVKAPQSEEEAN 342
Cdd:cd02659 233 KGLakkegdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDD-GKWYKFN---DDVVTPFDPNDAEEEC 301
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
42-330 |
2.74e-56 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 198.05 E-value: 2.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSlgpeelGSLEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAA-STIDLTDS 120
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 121 FGWTNDE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNV 195
Cdd:pfam00443 76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 196 SGLEDELCNM-----YVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTscYTFPLR 270
Cdd:pfam00443 156 SAELKTASLQicflqFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTE--VEFPLE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 310688895 271 INLKPFC--EQSELDDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCqeeISDTNV 330
Cdd:pfam00443 234 LDLSRYLaeELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEN-NRWYK---FDDEKV 291
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
35-319 |
1.92e-52 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 201.25 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 35 REFTNLSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLgpeelgsleDKDKPDAKvRIIPLQLQRLFAQLLLLDqEAAST 114
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQTGE-EPVDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 115 IDLTDSFGWTNDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKN 194
Cdd:COG5077 257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 195 VSGLEDELCNmYVEEEIFDYDNLYHCGTCDrLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLK 274
Cdd:COG5077 337 MKNLQESFRR-YIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 310688895 275 PF----CEQSELDDmeYMYDLFSVIIHKGGCYGGHYHVYIK-DVDhlGNW 319
Cdd:COG5077 415 PFldrdADKSENSD--AVYVLYGVLVHSGDLHEGHYYALLKpEKD--GRW 460
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-324 |
1.58e-47 |
|
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: 172.99 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLG-PEELGSLEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTIDLTDS 120
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNsTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 121 FGWTNDEemrQHDVQELNRILFSALETSLVGTSGHDL---IHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNVSG 197
Cdd:cd02668 81 LGLDTGQ---QQDAQEFSKLFLSLLEAKLSKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 198 LEDELcNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFC 277
Cdd:cd02668 158 LEECI-DEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 310688895 278 EQSELDDmeYMYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW-QCQEE 324
Cdd:cd02668 237 AESDEGS--YVYELSGVLIHQGvSAYSGHYIAHIKD-EQTGEWyKFNDE 282
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
42-353 |
5.78e-47 |
|
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: 169.20 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHftpefrealfslgpeelgsledkdkpdakvriiplqlqrlfaqlllldqeaastidltdsf 121
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 122 gwtndeeMRQHDVQELNRILFSALETSLVG--------TSGHDLIHRLYHGTIVNQIVCKECK--NISERQEDFLDLTVA 191
Cdd:cd02257 20 -------SEQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGheSVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 192 VKNVSGLE-DELCNMYVEEEIFDYDNLYHCGtCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvKCERYKDTSCYTFPLR 270
Cdd:cd02257 93 VKGLPQVSlEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 271 INLKPFCE----QSELDDMEYMYDLFSVIIHKGG-CYGGHYHVYIKDVDHlGNWQCqeeISDTNVNvkaPQSEEEANDPL 345
Cdd:cd02257 171 LDLSPYLSegekDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSD-GKWYK---FNDDKVT---EVSEEEVLEFG 243
|
330
....*....|
gi 310688895 346 VVLKT--ILL 353
Cdd:cd02257 244 SLSSSayILF 253
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
41-321 |
1.92e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 140.10 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 41 SGIRNQGGTCYLSSLLQTLHFTPEFreALFSLGPEElgSLEDKDKPDAKVRIIPLQLQRLFaqlllldqEAASTIDLTDS 120
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPL--ANYLLSREH--SKDCCNEGFCMMCALEAHVERAL--------ASSGPGSAPRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 121 FG------WTNDEEMRQHDVQELNRILFSALETS----LVGTSGHD-------LIHRLYHGTIVNQIVCKECKNISERQE 183
Cdd:cd02661 70 FSsnlkqiSKHFRIGRQEDAHEFLRYLLDAMQKAcldrFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 184 DFLDLTVAVKNVSGLEDELcNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvkceRYKDTS 263
Cdd:cd02661 150 PFLDLSLDIKGADSLEDAL-EQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR----GGKINK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 310688895 264 CYTFPLRINLKPFCEQSEldDMEYMYDLFSVIIHKGG-CYGGHYHVYIKDVDhlGNWQC 321
Cdd:cd02661 225 QISFPETLDLSPYMSQPN--DGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSN--GKWYN 279
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-314 |
2.62e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 122.99 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLEdkdkpdakvrIIPLQLQRLFAQLLLLDQEAASTID--LTD 119
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ----------SVMKKLQLLQAHLMHTQRRAEAPPDyfLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 120 SF-GWTNDEemRQHDVQELNRILFSALetslvgtsgHDLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNVSgl 198
Cdd:cd02664 71 SRpPWFTPG--SQQDCSEYLRYLLDRL---------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQ-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 199 edELCNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvKCE-RYKDTSCYTFPLRINL---- 273
Cdd:cd02664 138 --DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ-KTHvREKIMDNVSINEVLSLpvrv 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 310688895 274 -------------KPFCEQSELDDMEYMYDLFSVIIHKG-GCYGGHYHVYIKDVD 314
Cdd:cd02664 215 eskssesplekkeEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQT 269
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-319 |
1.20e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 115.16 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSlgpeelgsleDKDKPDAKVR----IIPLQLQRLFAQLllldqeaaSTIDL 117
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS----------DRHSCTCLSCspnsCLSCAMDEIFQEF--------YYSGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 118 TDSFG--------WTNDEEM---RQHDVQELNRILFSALETSLVGTSGHD--------LIHRLYHGTIVNQIVCKECKNI 178
Cdd:cd02660 64 RSPYGpinllylsWKHSRNLagySQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcncIIHQTFSGSLQSSVTCQRCGGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 179 SERQEDFLDLTVAVKNVSG---------------LEDELCNMYVEEEIFDYDnlYHCGTCDRLVKAAKSAKLRKLPPFLT 243
Cdd:cd02660 144 STTVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKLGDFA--YKCSGCGSTQEATKQLSIKKLPPVLC 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 244 ISLLRFNFDFVKCERyKDTSCYTFPLRINLKPFCEQSELDDME-------YMYDLFSVIIHKGGCYGGHYHVYIKdvDHL 316
Cdd:cd02660 222 FQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdYTYDLFAVVVHKGTLDTGHYTAYCR--QGD 298
|
...
gi 310688895 317 GNW 319
Cdd:cd02660 299 GQW 301
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-312 |
1.35e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 110.94 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREaLFSLGPEELgsledkdkpdakvriiplqlqrlFAQLllldqeAASTIDLTDSf 121
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSETPKEL-----------------------FSQV------CRKAPQFKGY- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 122 gwtndeemRQHDVQELNRILFSALETslvgtsghdLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNVSGLEDE 201
Cdd:cd02667 50 --------QQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 202 L--C-NMYVEEEIFDYDNLYHCGTCDrlvKAAKSAKLRKLPPFLTISLLRF----NFDFVKCERYKDtscytFPLRINLK 274
Cdd:cd02667 113 IesClKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFqqprSANLRKVSRHVS-----FPEILDLA 184
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 310688895 275 PFCEQSEL---DDMEYMYDLFSVIIHKGGCYGGHYHVYIKD 312
Cdd:cd02667 185 PFCDPKCNsseDKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-306 |
1.73e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 111.25 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFtpefrEALFSLGPEELGSLEDKDKpdaKVRIIPLQLqrlFAQLLLLDQEAASTIDLTDS- 120
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLTCLKDLFESISEQKK---RTGVISPKK---FITRLKRENELFDNYMHQDAh 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 121 --FGW---TNDEEMRQHDVQELNRILFSALETSlvgTSGHDLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNV 195
Cdd:cd02663 70 efLNFllnEIAEILDAERKAEKANRKLNNNNNA---EPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 196 SGLEDELCNMYvEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDfVKCERYKDTScYTFPLRINLKP 275
Cdd:cd02663 147 TSITSCLRQFS-ATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD-EQLNRYIKLF-YRVVFPLELRL 223
|
250 260 270
....*....|....*....|....*....|..
gi 310688895 276 FCEQSELDDMEYMYDLFSVIIHKG-GCYGGHY 306
Cdd:cd02663 224 FNTTDDAENPDRLYELVAVVVHIGgGPNHGHY 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
130-312 |
1.49e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 106.60 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 130 RQHDVQELNRILFSALetslvgtsgHDLIHRLYHGTIVNQIVCKECKNISERQEDFLDLTVAVKNVSGLED----ELC-N 204
Cdd:cd02674 21 DQQDAQEFLLFLLDGL---------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPkvtlEDClR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 205 MYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvkCERYKDTSCYTFPLRI-NLKPFCEQSElD 283
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPLNDlDLTPYVDTRS-F 168
|
170 180
....*....|....*....|....*....
gi 310688895 284 DMEYMYDLFSVIIHKGGCYGGHYHVYIKD 312
Cdd:cd02674 169 TGPFKYDLYAVVNHYGSLNGGHYTAYCKN 197
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
31-311 |
7.09e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 98.43 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 31 PPAPREFTNL---SGIRNQGGTCYLSSLLQTLHFTPEFREA---LFSLGpeelGSLEdkdkpdaKVRIIPLQLQRLFAQL 104
Cdd:cd02671 12 ATSCEKRENLlpfVGLNNLGNTCYLNSVLQVLYFCPGFKHGlkhLVSLI----SSVE-------QLQSSFLLNPEKYNDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 105 LLldQEAASTI-----DLTDSFgwtndEEMRQHDVQE-LNRILFSAletslvgtsgHDLIHRLYHGTIVNQIVCKECKNI 178
Cdd:cd02671 81 LA--NQAPRRLlnalrEVNPMY-----EGYLQHDAQEvLQCILGNI----------QELVEKDFQGQLVLRTRCLECETF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 179 SERQEDFLDLTVAVknvsgLEDELCNMYVEEEIFDY-----------------------DNLYHCGTCDRLVKAAKSAKL 235
Cdd:cd02671 144 TERREDFQDISVPV-----QESELSKSEESSEISPDpktemktlkwaisqfasverivgEDKYFCENCHHYTEAERSLLF 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310688895 236 RKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFCEQSELDDMEYMYDLFSVIIHKGGCYG-GHYHVYIK 311
Cdd:cd02671 219 DKLPEVITIHLKCFAANGSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISsGHYTAYVR 295
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
42-343 |
2.50e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 86.78 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHF-TPEFREALFSLgPEELGSLED---KDKPDAKVRiiplQLQRLFAQLLLLDQEaastidl 117
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALyLPKLDELLDDL-SKELKVLKNvirKPEPDLNQE----EALKLFTALWSSKEH------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 118 tdSFGWTNDEEmRQHDVQELNRILFSALETSLVGT-----------SGHDLIHRLYHGTIVNQIvcKECKNISERQEDFL 186
Cdd:COG5533 69 --KVGWIPPMG-SQEDAHELLGKLLDELKLDLVNSftirifkttkdKKKTSTGDWFDIIIELPD--QTWVNNLKTLQEFI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 187 DltvavkNVSGLEDELCNmyVEEEIFDYDNLyhcgtcdrLVKAAKSAKLRKLPPFLTISLLRF--NFDFVKCERYKDTsc 264
Cdd:COG5533 144 D------NMEELVDDETG--VKAKENEELEV--------QAKQEYEVSFVKLPKILTIQLKRFanLGGNQKIDTEVDE-- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310688895 265 ytfPLRINLKPfcEQSELDDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlgnWqcqEEISDTNVNvkaPQSEEEAND 343
Cdd:COG5533 206 ---KFELPVKH--DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGK---W---EKANDSDVT---PVSEEEAIN 270
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-309 |
6.47e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 81.64 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALfslgpeelgsledkdkpdakvriiplqlqrlfaqlllldqeaastidltdsf 121
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------------------------------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 122 gwtnDEEMRQHDVQELNRILFSALETSLVGtsghdlihrLYHGTIVNQIVCKECKNISE-RQEDFLDLTVAV---KNVSG 197
Cdd:cd02662 29 ----EEFLEQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKvRYESFTMLSLPVpnqSSGSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 198 LEDELC-NMYVEEEIFDYDNLYHCgtcdrlvkaakSAKLRKLPPFLTISLLRFNFDfVKCERYKDTSCYTFPLRINlkpf 276
Cdd:cd02662 96 TTLEHClDDFLSTEIIDDYKCDRC-----------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP---- 159
|
250 260 270
....*....|....*....|....*....|...
gi 310688895 277 ceqselddmEYMYDLFSVIIHKGGCYGGHYHVY 309
Cdd:cd02662 160 ---------KVLYRLRAVVVHYGSHSSGHYVCY 183
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-319 |
4.46e-16 |
|
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: 80.45 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLEDKDKpdakvriIPLQLQRLFAQlllLD--QEAASTIDLTD 119
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDN-------LTNALRDLFDT---MDkkQEPVPPIEFLQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 120 SFG--------WTNDEEMRQHDVQELNRILFSALETSLVGTSGH-DLIHRLYHGTIVNQIVCKECKNISE---RQEDFLD 187
Cdd:cd02657 71 LLRmafpqfaeKQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKgSFIDQLFGIELETKMKCTESPDEEEvstESEYKLQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 188 LTVAVK-NVSGLEDELcNMYVEEEIfdydnLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFnfdFVKCE---RYKDTS 263
Cdd:cd02657 151 CHISITtEVNYLQDGL-KKGLEEEI-----EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRF---FWKRDiqkKAKILR 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 310688895 264 CYTFPLRINLKPFCEQSElddmeyMYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW 319
Cdd:cd02657 222 KVKFPFELDLYELCTPSG------YYELVAVITHQGrSADSGHYVAWVRR-KNDGKW 271
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-319 |
2.23e-14 |
|
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: 75.44 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLgpeELGSLEDKDKPD-------AKVR----------------------- 91
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL---ENKFPSDVVDPAndlncqlIKLAdgllsgryskpaslksendpyqv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 92 -IIPLQLQRLFAQllllDQEAASTidltdsfgwtndeeMRQHDVQELNRILFSALETSLVGTSGHDLIhRLYHGTIVNQI 170
Cdd:cd02658 78 gIKPSMFKALIGK----GHPEFST--------------MRQQDALEFLLHLIDKLDRESFKNLGLNPN-DLFKFMIEDRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 171 VCKECK--NISERQEDFLDLTV-AVKNVSGLEDEL---------C-NMYVEEEIFDYdnlyHCGTCDRLVKAAKSAKLRK 237
Cdd:cd02658 139 ECLSCKkvKYTSELSEILSLPVpKDEATEKEEGELvyepvpledClKAYFAPETIED----FCSTCKEKTTATKTTGFKT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 238 LPPFLTISLLRFnfDFVKCERYKDTSCYTF-PLRINLKPfceqselddmeymYDLFSVIIHKG-GCYGGHYHVYI-KDVD 314
Cdd:cd02658 215 FPDYLVINMKRF--QLLENWVPKKLDVPIDvPEELGPGK-------------YELIAFISHKGtSVHSGHYVAHIkKEID 279
|
....*
gi 310688895 315 HLGNW 319
Cdd:cd02658 280 GEGKW 284
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-339 |
3.06e-14 |
|
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: 75.61 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLEDKDK----PDAKVRIIPLQLQRLFAQ---LLLLDQEAAST 114
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTerriGGREVSRSELQRSNQFVYelrSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 115 IDLTDSFGWTNdEEMRQHDVQE-LNRILFSaLETSLVGTSGH-------------DLIHRLYHGTIVNQIV-CKECKNIS 179
Cdd:cd02666 83 RSVTPSKELAY-LALRQQDVTEcIDNVLFQ-LEVALEPISNAfagpdteddkeqsDLIKRLFSGKTKQQLVpESMGNQPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 180 ER--QEDFLDLTVAV---KNVSGLEDELCNMYveeEIFDYDNLYhcgtcDRLVKA-AKSAKLRKLPPFLTISLLRfnfdf 253
Cdd:cd02666 161 VRtkTERFLSLLVDVgkkGREIVVLLEPKDLY---DALDRYFDY-----DSLTKLpQRSQVQAQLAQPLQRELIS----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 254 vkCERY-------------------KDTSCYTFPLRINLKPFCEQSELDDM-EYMYDLFSVIIHKGGCYGGHYHVYIKdv 313
Cdd:cd02666 228 --MDRYelpssiddidelireaiqsESSLVRQAQNELAELKHEIEKQFDDLkSYGYRLHAVFIHRGEASSGHYWVYIK-- 303
|
330 340
....*....|....*....|....*..
gi 310688895 314 DHLGN-WQcqeEISDTNVNVKaPQSEE 339
Cdd:cd02666 304 DFEENvWR---KYNDETVTVV-PASEV 326
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
41-311 |
4.33e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 68.45 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 41 SGIRNQGGTCYLSSLLQTLHFTPEFRE-ALFSLGPE---------ELGSLEDkdkPDAKVRIIPLQ---LQRLFAQLlll 107
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATEclkehcllcELGFLFD---MLEKAKGKNCQasnFLRALSSI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 108 dqEAASTIDLTDSFGWTNDEEMRQHDVQELNRILFS-----ALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNISERQ 182
Cdd:pfam13423 75 --PEASALGLLDEDRETNSAISLSSLIQSFNRFLLDqlsseENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 183 EDF--LDLTVAVKNVSGLEDELCN---MYVEEEIF-DYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKC 256
Cdd:pfam13423 153 SSThvLDLIYPRKPSSNNKKPPNQtfsSILKSSLErETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 310688895 257 ERykdTSCYtFPLRINLKPFcEQSELDDMEYMYDLFSVIIH-KGGCYGGHYHVYIK 311
Cdd:pfam13423 233 WK---TPGW-LPPEIGLTLS-DDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVK 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
198-321 |
3.27e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.97 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 198 LEDELcNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDfvKCERYKDTSCYTFPL-RINLKPF 276
Cdd:COG5560 677 LQDCL-NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPIdDLDLSGV 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 310688895 277 ceQSELDDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQC 321
Cdd:COG5560 754 --EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFAN-NGWYL 795
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
131-331 |
1.88e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 47.55 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 131 QHDVQELNRILFSALE---------TSLVGTSGHDLIhRLYHGTIVNQIVCKECKniSERQEDFLDLTVAVKNVSGLEDE 201
Cdd:cd02665 22 QQDVSEFTHLLLDWLEdafqaaaeaISPGEKSKNPMV-QLFYGTFLTEGVLEGKP--FCNCETFGQYPLQVNGYGNLHEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310688895 202 LCNMYVEEEIfdyDNLyhcgTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTScyTFPLRINLKPfceqse 281
Cdd:cd02665 99 LEAAMFEGEV---ELL----PSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKL--EFPQIIQQVP------ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 310688895 282 lddmeymYDLFSVIIHKGGCYGGHYHVYIKDvDHLGNWQCQEEISDTNVN 331
Cdd:cd02665 164 -------YELHAVLVHEGQANAGHYWAYIYK-QSRQEWEKYNDISVTESS 205
|
|
| |
