|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
71-413 |
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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 519.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 71 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRH--RCEMQSPSSCLVCEMSSLFQEF-YSGHRSPHIPYKLLHLVWTHA 147
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 148 RHLAGYEQQDAHEFLIAALDVLHRHCKGDDNgkKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 227
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN--EANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 228 GSSTPFWPLspgsegnvvnGESHVSGTTTLTDCLRRFTRPEHLGSSAkIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 307
Cdd:cd02660 159 NKSTPSWAL----------GESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 308 EHSA-KLRRKITTYVSFPLELDMTPFMASSKesrmngQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQW 386
Cdd:cd02660 228 EHSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQW 301
|
330 340
....*....|....*....|....*..
gi 530410180 387 FKCDDAIITKASIKDVLDSEGYLLFYH 413
Cdd:cd02660 302 FKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
71-412 |
6.76e-88 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 269.31 E-value: 6.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 71 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCE--MQSPSSCLVCEMSSLFQEFYSGHRSPHI-PYKLLHLVWTHA 147
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEdsRYNKDINLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 148 RHLAGYEQQDAHEFLIAALDVLHRhckgddnGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 227
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE-------DLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 228 GSSTPfwplspgsegnvvngeshvSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 307
Cdd:pfam00443 154 GDSAE-------------------LKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 308 EHSAKLRRKITTYVSFPLELDMTPFMASSKESrmngqyqqptdSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKD-QW 386
Cdd:pfam00443 215 SYNRSTWEKLNTEVEFPLELDLSRYLAEELKP-----------KTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRW 283
|
330 340
....*....|....*....|....*..
gi 530410180 387 FKCDDAIITKAS-IKDVLDSEGYLLFY 412
Cdd:pfam00443 284 YKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
71-412 |
3.88e-77 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 241.41 E-value: 3.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 71 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHL 150
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 151 AGYEQQDAHEFLIAALDVLHRHC-KGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGS 229
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAClDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 230 STpfwplspgsegnvvngeshvsgtttLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFeh 309
Cdd:cd02661 162 DS-------------------------LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 310 SAKLRRKITTYVSFPLELDMTPFMASSKESrmngqyqqPTdslnndnKYSLFAVVNHQGT-LESGHYTSFIRQHKDQWFK 388
Cdd:cd02661 215 SNFRGGKINKQISFPETLDLSPYMSQPNDG--------PL-------KYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYN 279
|
330 340
....*....|....*....|....
gi 530410180 389 CDDAIITKASIKDVLDSEGYLLFY 412
Cdd:cd02661 280 MDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
72-412 |
4.55e-72 |
|
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: 226.98 E-value: 4.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 151
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 152 gyEQQDAHEFLIAALDVLHRHCKGddNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 231
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 232 PfwplspgsegnvvngeshvsgTTTLTDCLRRFTRPEHLGSSAKIKCSgCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 311
Cdd:cd02257 97 P---------------------QVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 312 KLRR-KITTYVSFPLELDMTPFMASSKEsrmngqyqqPTDSLNNDNKYSLFAVVNHQGTL-ESGHYTSFIRQH-KDQWFK 388
Cdd:cd02257 155 DGTKeKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYK 225
|
330 340
....*....|....*....|....*....
gi 530410180 389 CDDAIITKASIKDVLD-----SEGYLLFY 412
Cdd:cd02257 226 FNDDKVTEVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
2.55e-70 |
|
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: 221.39 E-value: 2.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 151
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 152 gyEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 231
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 232 PFWPLspgsegnvvngeshvsgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 311
Cdd:cd02674 80 DAPKV-------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 312 KLRRKITTYVSFPLE-LDMTPFMASSkesrmngqyqqptdSLNNDNKYSLFAVVNHQGTLESGHYTSFIR-QHKDQWFKC 389
Cdd:cd02674 141 GSTRKLTTPVTFPLNdLDLTPYVDTR--------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKnNETNDWYKF 206
|
330 340
....*....|....*....|...
gi 530410180 390 DDAIITKASIKDVLDSEGYLLFY 412
Cdd:cd02674 207 DDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
4.75e-55 |
|
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: 183.74 E-value: 4.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRhrcemqspssclvcemSSLFQEFysghRSPHIPYKllhlvwtharhla 151
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP----------------KELFSQV----CRKAPQFK------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 152 GYEQQDAHEFLIAALDVLhrhckgddngkkannpnhcNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISldLPGSST 231
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLS--LPRSDE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 232 PFWPlspgsegnvvngeshvsgtTTLTDCLRRFTRPEHLGSSAKIKCSGChsyQESTKQLTMKKLPIVACFHLKRFEHSA 311
Cdd:cd02667 107 IKSE-------------------CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 312 KLR-RKITTYVSFPLELDMTPFMASSKESrmngqyqqptDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQH-------- 382
Cdd:cd02667 165 SANlRKVSRHVSFPEILDLAPFCDPKCNS----------SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsd 234
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530410180 383 --------------KDQWFKCDDAIITKASIKDVLDSEGYLLFY 412
Cdd:cd02667 235 ltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
69-405 |
2.21e-50 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 173.21 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 69 GLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRcEMQSPSSCLVCEMSSLFQEFYSGHrSPHIPYKLLHLV----W 144
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLSE-SPVKTTELTDKTrsfgW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 145 THarhLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISL 224
Cdd:cd02659 79 DS---LNTFEQHDVQEFFRVLFDKL------EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 225 DlpgsstpfwplspgsegnvvngeshVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHL 304
Cdd:cd02659 146 A-------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 305 KRFEHS--AKLRRKITTYVSFPLELDMTPFMASSkesrMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQ- 381
Cdd:cd02659 201 KRFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDr 276
|
330 340
....*....|....*....|....
gi 530410180 382 HKDQWFKCDDAIITKASIKDVLDS 405
Cdd:cd02659 277 DDGKWYKFNDDVVTPFDPNDAEEE 300
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
1.53e-39 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 143.60 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPL---LRDFFlsdrhrcEMQSPSSCLVCEMSslfqefysghrsphiPYKLLHLVWTHAR 148
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLltcLKDLF-------ESISEQKKRTGVIS---------------PKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 149 HLAGYEQQDAHEFL-------IAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWD 221
Cdd:cd02663 59 LFDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 222 ISLDLPGSstpfwplspgsegnvvngeshvsgtTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVAC 301
Cdd:cd02663 139 LSIDVEQN-------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 302 FHLKRFEHSAKLRR--KITTYVSFPLELdmTPFMASSkesrmngqyqqptDSLNNDNKYSLFAVVNHQG-TLESGHYTSF 378
Cdd:cd02663 194 LHLKRFKYDEQLNRyiKLFYRVVFPLEL--RLFNTTD-------------DAENPDRLYELVAVVVHIGgGPNHGHYVSI 258
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530410180 379 IRqHKDQWFKCDDAIITKASIKDVLD--------SEGYLLFY 412
Cdd:cd02663 259 VK-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
58-412 |
1.37e-37 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 145.03 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 58 KRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPS-----SCLVCEMSSLFQEFYSGHRS 132
Cdd:COG5560 253 DDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplgmhGSVASAYADLIKQLYDGNLH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 133 PHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHR--------------HCKGDDNGKKANNPNHC-------NC- 190
Cdd:COG5560 333 AFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKECwwehlkrNDs 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 191 IIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDIS--------------------------LDLPGSST------------- 231
Cdd:COG5560 413 IITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTlplpvsmvwkhtivvfpesgrrqplkIELDASSTirglkklvdaeyg 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 232 ---------------------------------------------------------------------PFWPLSPGSEG 242
Cdd:COG5560 493 klgcfeikvmciyyggnynmlepadkvllqdipqtdfvylyetndngievpvvhlriekgykskrlfgdPFLQLNVLIKA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 243 NVVNG-------------------------------ESHVSG-------------------------------------- 253
Cdd:COG5560 573 SIYDKlvkefeellvlvemkktdvdlvseqvrllreESSPSSwlkleteidtkreeqveeegqmnfndavvisceweekr 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 254 ---------------------TTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAK 312
Cdd:COG5560 653 ylslfsydplwtireigaaerTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 313 LRRKITTYVSFPL-ELDMTPFMASSKESRMNgqyqqptdslnndnkYSLFAVVNHQGTLESGHYTSFIRQHKDQ-WFKCD 390
Cdd:COG5560 733 FRDKIDDLVEYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFD 797
|
570 580
....*....|....*....|..
gi 530410180 391 DAIITKASIKDVLDSEGYLLFY 412
Cdd:COG5560 798 DSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-400 |
8.59e-32 |
|
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: 123.30 E-value: 8.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPLLRDFFL---SDRHRCEMQSPSSC------LVCEMSSLFQEFYSGHRSPHIPYKLLHl 142
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnSTEDAELKNMPPDKphepqtIIDQLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 143 vwthARHLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNHCNcIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDI 222
Cdd:cd02668 80 ----ALGLDTGQQQDAQEFSKLFLSLL------EAKLSKSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 223 SLDLpgsstpfwplspgsegnvvngeshvSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACF 302
Cdd:cd02668 149 ELQL-------------------------KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 303 HLKRFEHSAKL--RRKITTYVSFPLELDMTPFMASSKEsrmngqyqqptdslnNDNKYSLFAVVNHQGT-LESGHYTSFI 379
Cdd:cd02668 204 QLLRFVFDRKTgaKKKLNASISFPEILDMGEYLAESDE---------------GSYVYELSGVLIHQGVsAYSGHYIAHI 268
|
330 340
....*....|....*....|..
gi 530410180 380 R-QHKDQWFKCDDAIITKASIK 400
Cdd:cd02668 269 KdEQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
1.46e-29 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 117.30 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPllrDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSpHIPYKLLHLVWTHARHLA 151
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELAN-QAPRRLLNALREVNPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 152 GYEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 231
Cdd:cd02671 102 GYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 232 PfwplspGSEGNVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 311
Cdd:cd02671 163 S------KSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 312 KLR------RKITTYVSFPLELDMtpFMASSKESRmngqyqqptdslnndNKYSLFAVVNHQG-TLESGHYTSFIRqhkd 384
Cdd:cd02671 237 SEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR---- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 530410180 385 qWFKCDDAIITKASIKDVLD---------SEGYLLFY 412
Cdd:cd02671 296 -WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
5.70e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 109.72 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHR--CEMQSPSSCLVCEMSSLFQEFYSG-------HRSPHIPYKlLHL 142
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpSDVVDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQ-VGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 143 VWTHARHLAGY--------EQQDAHEFLIAALDVLHRHCKgddnGKKANNPNhcnciidQIFTGGLQSDVTCQVCHGVST 214
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESF----KNLGLNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 215 TIDPFWDISLDLPGSstpfwPLSPGSEGNVVNGEshvsgtTTLTDCLRRFTRPEHLgssaKIKCSGCHSYQESTKQLTMK 294
Cdd:cd02658 149 TSELSEILSLPVPKD-----EATEKEEGELVYEP------VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 295 KLPIVACFHLKRFEHSA-KLRRKITTYVSFPLELDmtpfmasskesrmngqyqqptdslnnDNKYSLFAVVNHQGT-LES 372
Cdd:cd02658 214 TFPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG--------------------------PGKYELIAFISHKGTsVHS 267
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530410180 373 GHYTSFIRQ---HKDQWFKCDDAIITKASIKDVLDSEGYLLFY 412
Cdd:cd02658 268 GHYVAHIKKeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
69-404 |
1.70e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 112.27 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 69 GLRGLINLGNTCFMNCIVQALTHTPLLRdfflSDRHRCEMQSPSSCLVCEMSsLFQEFYSGHRSPHiPYKLLHLV----W 144
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFR----KDVYGIPTDHPRGRDSVALA-LQRLFYNLQTGEE-PVDTTELTrsfgW 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 145 THARHlagYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNpnhcnciidqIFTGGLQSDVTCQVCHGVSTTIDPFWDISL 224
Cdd:COG5077 266 DSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENALNG----------IFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 225 DLPGSSTpfwplspgsegnvvngeshvsgtttLTDCLRRFTRPEHLGSSAKIKCSGcHSYQESTKQLTMKKLPIVACFHL 304
Cdd:COG5077 333 NVKGMKN-------------------------LQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 305 KRFEHSAK--LRRKITTYVSFPLELDMTPFMasSKESRmngqyqqptDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQH 382
Cdd:COG5077 387 KRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDAD---------KSENSDAVYVLYGVLVHSGDLHEGHYYALLKPE 455
|
330 340
....*....|....*....|...
gi 530410180 383 KD-QWFKCDDAIITKASIKDVLD 404
Cdd:COG5077 456 KDgRWYKFDDTRVTRATEKEVLE 478
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-412 |
1.83e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 110.49 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 46 TKRELELLKHNPKRRKITSNCT--IGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLS---DRHRCEMQSPsscLVCEMS 120
Cdd:cd02669 93 TKEQISDLDRDPKLSRDLDGKPylPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKDRKSE---LVKRLS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 121 SLFQEFYS-----GHRSPHipyKLLHLV--WTHARHLAGyEQQDAHEFLIAALDVLHRhckgDDNGKKANNPNhcncIID 193
Cdd:cd02669 170 ELIRKIWNprnfkGHVSPH---ELLQAVskVSKKKFSIT-EQSDPVEFLSWLLNTLHK----DLGGSKKPNSS----IIH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 194 QIFTGGLQ--------------SDVTCQVCHGVSTTID-PFWDISLDLPgsstPFWPLSPGSEGNVVngeSHVsgttTLT 258
Cdd:cd02669 238 DCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVsPFLLLTLDLP----PPPLFKDGNEENII---PQV----PLK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 259 DCLRRFTrpehlGSSakikcsgCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLE-LDMTPFMAssk 337
Cdd:cd02669 307 QLLKKYD-----GKT-------ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDYVH--- 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530410180 338 esrmngqyqQPTDSLNNDNKYSLFAVVNHQGT-LESGHYTSFIRQHK-DQWFKCDDAIITKASIKDVLDSEGYLLFY 412
Cdd:cd02669 372 ---------FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKStNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
3.43e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 105.53 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALthtpllrdfflsdrhrcemqspSSClvcemsslfqefysghrsphiPYKLLHLVWTharhla 151
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL----------------------ASL---------------------PSLIEYLEEF------ 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 152 gYEQQDAHEFLIAALDVLHRHCKgddngkkanNPnhcnciidqiFTGGLQSDVTCQVCHGVST-TIDPFWDISLDLPgss 230
Cdd:cd02662 32 -LEQQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 231 tpfwplspgsegnvvngESHVSGTTTLTDCLRRFTRPEHLGSsakIKCSGChsyqestkQLTMKKLPIVACFHLKRFEHS 310
Cdd:cd02662 89 -----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 311 AK-LRRKITTYVSFPLELdmtpfmasskesrmngqyqqptdslnNDNKYSLFAVVNHQGTLESGHYTSFIRQH------- 382
Cdd:cd02662 141 GRgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdke 194
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530410180 383 --------------KDQWFKCDDAIITKASIKDVL-DSEGYLLFY 412
Cdd:cd02662 195 pgsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
72-414 |
3.76e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.81 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALT-HTPLLRDffLSDRHRCEMQSpssclvcemsslFQEFYSGHRSP---HIPYKLLHLVWTHA 147
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDE--LLDDLSKELKV------------LKNVIRKPEPDlnqEEALKLFTALWSSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 148 RHLAG-----YEQQDAHEFLIAALDVLhrhckgddngkkaNNPNHcNCIIDQIF-TGGlqsdvtcqvcHGVSTTIDPFWD 221
Cdd:COG5533 67 EHKVGwippmGSQEDAHELLGKLLDEL-------------KLDLV-NSFTIRIFkTTK----------DKKKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 222 ISLDLPGsstpfwplspgsegnvvngESHVSGTTTLTDCLRRFtrpEHLGSSAK-IKCS---GCHSYQESTKQLTMKKLP 297
Cdd:COG5533 123 IIIELPD-------------------QTWVNNLKTLQEFIDNM---EELVDDETgVKAKeneELEVQAKQEYEVSFVKLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 298 IVACFHLKRFEHSAKlRRKITTYVSFPLELDMTPfmasskesrmngqyqQPTDSLNNDNKYSLFAVVNHQGTLESGHYTS 377
Cdd:COG5533 181 KILTIQLKRFANLGG-NQKIDTEVDEKFELPVKH---------------DQILNIVKETYYDLVGFVLHQGSLEGGHYIA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530410180 378 FIRQhKDQWFKCDDAIITKASIKDVLDS---EGYLLFYHK 414
Cdd:COG5533 245 YVKK-GGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
6.09e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 107.19 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGhRSPHIPYKLLHLVWThARHLA 151
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQR-RAEAPPDYFLEASRP-PWFTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 152 GYeQQDAHEFLIAALDVLHrhckgddngkkannpnhcnCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPgsst 231
Cdd:cd02664 79 GS-QQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 232 pfwplspgsegnvvngeshvsgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 311
Cdd:cd02664 135 ------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 312 K--LRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQP--TDSLNNDNK--YSLFAVVNHQGT-LESGHYTSFIR---- 380
Cdd:cd02664 191 KthVREKIMDNVSINEVLSLPVRVESKSSESPLEKKEEEsgDDGELVTRQvhYRLYAVVVHSGYsSESGHYFTYARdqtd 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530410180 381 -----------------QHKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 412
Cdd:cd02664 271 adstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
4.17e-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 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: 104.34 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPLLRD---FFLSDRhRCEMQSPSScLVCEMSSLFQEFySGHRSPHIPYKLLHLVWTHAR 148
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPAR-RGANQSSDN-LTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 149 HLA------GYEQQDAHEFLIAALDVLHRHCKGDDNGKKAnnpnhcnciIDQIFTGGLQSDVTCQvchgvsttidpfwDI 222
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCT-------------ES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 223 SLDLPGSSTPFWPLSpgsegnvvngeSHVSGTT---TLTDCLRrftrpEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIV 299
Cdd:cd02657 136 PDEEEVSTESEYKLQ-----------CHISITTevnYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 300 ACFHLKRF--EHSAKLRRKITTYVSFPLELDMTPFMASSkesrmngqyqqptdslnndNKYSLFAVVNHQG-TLESGHYT 376
Cdd:cd02657 200 LTVQFVRFfwKRDIQKKAKILRKVKFPFELDLYELCTPS-------------------GYYELVAVITHQGrSADSGHYV 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530410180 377 SFIRQ-HKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 412
Cdd:cd02657 261 AWVRRkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
72-391 |
5.44e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 75.00 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQALTHTPLLRDFFLSdrHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHAR--- 148
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 149 -HLAGYEQQDAHEFLIAAL-DVLHR---HCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDIS 223
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 224 LDLPGSSTPfwplspgsegnvvngESHVSGTTTLTDCLRRFTRPEhlgSSAKIKCSGCHSYQESTKQLTMKKLPIVACFH 303
Cdd:pfam13423 160 LIYPRKPSS---------------NNKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 304 LKRfeHSAKLRRKITTYVSFPLELDMTPFMASSKEsrmngqyqqptdslNNDNKYSLFAVVNH-QGTLESGHYTSFIR-- 380
Cdd:pfam13423 222 AAL--TNEEWRQLWKTPGWLPPEIGLTLSDDLQGD--------------NEIVKYELRGVVVHiGDSGTSGHLVSFVKva 285
|
330
....*....|....*..
gi 530410180 381 ------QHKDQWFKCDD 391
Cdd:pfam13423 286 dseledPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
72-412 |
1.95e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 72 GLINLGNTCFMNCIVQAL-THTPLlRDFFLS-DRHRCEMQSP-------------------SSCLVCEMSSLFQEF-YSG 129
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKPL-RDLVLNfDESKAELASDypterriggrevsrselqrSNQFVYELRSLFNDLiHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 130 HRSPHiPYKLLHLvwtharhlAGYEQQDAHEFLIAALDVLHRHCKGDDN---GKKANNPNHCNCIIDQIFTGGL-QSDVT 205
Cdd:cd02666 82 TRSVT-PSKELAY--------LALRQQDVTECIDNVLFQLEVALEPISNafaGPDTEDDKEQSDLIKRLFSGKTkQQLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 206 CQVCHGVSTTIDPFWDISLdlpgsstpfwPLSPGSEGNVVNGESHvsgTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQ 285
Cdd:cd02666 153 ESMGNQPSVRTKTERFLSL----------LVDVGKKGREIVVLLE---PKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 286 -ESTKQLTMKK--LPIVAcfhlkrfEHSAKLRRKITTYVSFPLEldmtpfMASSKESRMNGQYQQPTDSLNNdNKYSLFA 362
Cdd:cd02666 220 pLQRELISMDRyeLPSSI-------DDIDELIREAIQSESSLVR------QAQNELAELKHEIEKQFDDLKS-YGYRLHA 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 530410180 363 VVNHQGTLESGHYTSFIRQH-KDQWFKCDDAIIT-KASIKDVLDSEG-----YLLFY 412
Cdd:cd02666 286 VFIHRGEASSGHYWVYIKDFeENVWRKYNDETVTvVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
355-412 |
2.59e-08 |
|
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: 54.46 E-value: 2.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530410180 355 DNKYSLFAVVNHQG-TLESGHYTSFIRQ--HKDQWFKCDDAIITKASIKDVLD---SEGYLLFY 412
Cdd:cd02673 181 DAKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
294-412 |
1.96e-06 |
|
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: 48.68 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 294 KKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPT-------DSLNNDNKYSLFAVVNH 366
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVcyddkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530410180 367 QGT-LESGHYTSFIRQHKD------------QWFKCDD-----AIITKASIKDVLDSE-GYLLFY 412
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
251-412 |
1.37e-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: 46.01 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 251 VSGTTTLTDCLRRFT---RPEHLGSSAKIKCSGCHSYQEstkqltmkkLPIVACFHLKRFEHSAKLRRKITTYVSFPLEL 327
Cdd:cd02665 89 VNGYGNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQII 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410180 328 DMTPfmasskesrmngqyqqptdslnndnkYSLFAVVNHQGTLESGHYTSFI-RQHKDQWFKCDDAIITKASIKDVL-DS 405
Cdd:cd02665 160 QQVP--------------------------YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVErDS 213
|
170
....*....|....
gi 530410180 406 EG-------YLLFY 412
Cdd:cd02665 214 FGggrnpsaYCLMY 227
|
|
| |
