|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-505 |
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 84569929 163 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRH--RCEMQSPSSCLVCEMSSLFQEF-YSGHRSPHIPYKLLHLVWTHA 239
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 240 RHLAGYEQQDAHEFLIAALDVLHRHCKGDDNgkKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 319
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN--EANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 320 GSSTPFWPLspgsegnvvnGESHVSGTTTLTDCLRRFTRPEHLGSSAkIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 399
Cdd:cd02660 159 NKSTPSWAL----------GESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 400 EHSA-KLRRKITTYVSFPLELDMTPFMASSKesrmngQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQW 478
Cdd:cd02660 228 EHSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQW 301
|
330 340
....*....|....*....|....*..
gi 84569929 479 FKCDDAIITKASIKDVLDSEGYLLFYH 505
Cdd:cd02660 302 FKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
163-504 |
3.30e-88 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 273.16 E-value: 3.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 163 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCE--MQSPSSCLVCEMSSLFQEFYSGHRSPHI-PYKLLHLVWTHA 239
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEdsRYNKDINLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 240 RHLAGYEQQDAHEFLIAALDVLHRhckgddnGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 319
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE-------DLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 320 GSSTPfwplspgsegnvvngeshvSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 399
Cdd:pfam00443 154 GDSAE-------------------LKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 400 EHSAKLRRKITTYVSFPLELDMTPFMASSKESRmngqyqqptdsLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKD-QW 478
Cdd:pfam00443 215 SYNRSTWEKLNTEVEFPLELDLSRYLAEELKPK-----------TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRW 283
|
330 340
....*....|....*....|....*..
gi 84569929 479 FKCDDAIITKAS-IKDVLDSEGYLLFY 504
Cdd:pfam00443 284 YKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-504 |
8.22e-76 |
|
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: 241.03 E-value: 8.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 163 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHL 242
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 243 AGYEQQDAHEFLIAALDVLHRHC-KGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGS 321
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAClDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 322 STpfwplspgsegnvvngeshvsgtttLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFeh 401
Cdd:cd02661 162 DS-------------------------LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 402 SAKLRRKITTYVSFPLELDMTPFMASSKESrmngqyqqPTdslnndnKYSLFAVVNHQGT-LESGHYTSFIRQHKDQWFK 480
Cdd:cd02661 215 SNFRGGKINKQISFPETLDLSPYMSQPNDG--------PL-------KYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYN 279
|
330 340
....*....|....*....|....
gi 84569929 481 CDDAIITKASIKDVLDSEGYLLFY 504
Cdd:cd02661 280 MDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
164-504 |
1.37e-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: 230.83 E-value: 1.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 243
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 244 gyEQQDAHEFLIAALDVLHRHCKGddNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 323
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 324 PfwplspgsegnvvngeshvsgTTTLTDCLRRFTRPEHLGSSAKIKCSgCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 403
Cdd:cd02257 97 P---------------------QVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 404 KLRR-KITTYVSFPLELDMTPFMASSKEsrmngqyqqPTDSLNNDNKYSLFAVVNHQGTL-ESGHYTSFIRQH-KDQWFK 480
Cdd:cd02257 155 DGTKeKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYK 225
|
330 340
....*....|....*....|....*....
gi 84569929 481 CDDAIITKASIKDVLD-----SEGYLLFY 504
Cdd:cd02257 226 FNDDKVTEVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
8.22e-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: 222.93 E-value: 8.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 243
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 244 gyEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 323
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 324 PFWPLspgsegnvvngeshvsgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 403
Cdd:cd02674 80 DAPKV-------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 404 KLRRKITTYVSFPLE-LDMTPFMASSkesrmngqyqqptdSLNNDNKYSLFAVVNHQGTLESGHYTSFIR-QHKDQWFKC 481
Cdd:cd02674 141 GSTRKLTTPVTFPLNdLDLTPYVDTR--------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKnNETNDWYKF 206
|
330 340
....*....|....*....|...
gi 84569929 482 DDAIITKASIKDVLDSEGYLLFY 504
Cdd:cd02674 207 DDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
2.12e-54 |
|
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: 184.51 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRhrcemqspssclvcemSSLFQEFysghRSPHIPYKllhlvwtharhla 243
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP----------------KELFSQV----CRKAPQFK------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 244 GYEQQDAHEFLIAALDVLhrhckgddngkkannpnhcNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISldLPGSST 323
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLS--LPRSDE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 324 PFWPlspgsegnvvngeshvsgtTTLTDCLRRFTRPEHLGSSAKIKCSGChsyQESTKQLTMKKLPIVACFHLKRFEHSA 403
Cdd:cd02667 107 IKSE-------------------CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 404 KLR-RKITTYVSFPLELDMTPFMASSKESrmngqyqqptDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQH-------- 474
Cdd:cd02667 165 SANlRKVSRHVSFPEILDLAPFCDPKCNS----------SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsd 234
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 84569929 475 --------------KDQWFKCDDAIITKASIKDVLDSEGYLLFY 504
Cdd:cd02667 235 ltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
161-497 |
1.04e-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: 176.29 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 161 GLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRcEMQSPSSCLVCEMSSLFQEFYSGHrSPHIPYKLLHLV----W 236
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLSE-SPVKTTELTDKTrsfgW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 237 THarhLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISL 316
Cdd:cd02659 79 DS---LNTFEQHDVQEFFRVLFDKL------EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 317 DlpgsstpfwplspgsegnvvngeshVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHL 396
Cdd:cd02659 146 A-------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 397 KRFEHS--AKLRRKITTYVSFPLELDMTPFMASSkesrMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQ- 473
Cdd:cd02659 201 KRFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDr 276
|
330 340
....*....|....*....|....
gi 84569929 474 HKDQWFKCDDAIITKASIKDVLDS 497
Cdd:cd02659 277 DDGKWYKFNDDVVTPFDPNDAEEE 300
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
150-504 |
3.33e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 155.04 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 150 KRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPS-----SCLVCEMSSLFQEFYSGHRS 224
Cdd:COG5560 253 DDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplgmhGSVASAYADLIKQLYDGNLH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 225 PHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHR--------------HCKGDDNGKKANNPNHC-------NC- 282
Cdd:COG5560 333 AFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKECwwehlkrNDs 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 283 IIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST---------PFWPLSP----------------------- 330
Cdd:COG5560 413 IITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtivvfpESGRRQPlkieldasstirglkklvdaeyg 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 331 -----------------------------------------GSEGN-----VVNG------------------------- 339
Cdd:COG5560 493 klgcfeikvmciyyggnynmlepadkvllqdipqtdfvylyETNDNgievpVVHLriekgykskrlfgdpflqlnvlika 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 340 ------------------------------------ESHVSG-------------------------------------- 345
Cdd:COG5560 573 siydklvkefeellvlvemkktdvdlvseqvrllreESSPSSwlkleteidtkreeqveeegqmnfndavvisceweekr 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 346 ---------------------TTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAK 404
Cdd:COG5560 653 ylslfsydplwtireigaaerTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 405 LRRKITTYVSFPL-ELDMTPFMASSKESRMNgqyqqptdslnndnkYSLFAVVNHQGTLESGHYTSFIRQHKDQ-WFKCD 482
Cdd:COG5560 733 FRDKIDDLVEYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFD 797
|
570 580
....*....|....*....|..
gi 84569929 483 DAIITKASIKDVLDSEGYLLFY 504
Cdd:COG5560 798 DSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
1.29e-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: 145.53 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPL---LRDFFlsdrhrcEMQSPSSCLVCEMSslfqefysghrsphiPYKLLHLVWTHAR 240
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLltcLKDLF-------ESISEQKKRTGVIS---------------PKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 241 HLAGYEQQDAHEFL-------IAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWD 313
Cdd:cd02663 59 LFDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 314 ISLDLPGSstpfwplspgsegnvvngeshvsgtTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVAC 393
Cdd:cd02663 139 LSIDVEQN-------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 394 FHLKRFEHSAKLRR--KITTYVSFPLELdmTPFMASSkesrmngqyqqptDSLNNDNKYSLFAVVNHQG-TLESGHYTSF 470
Cdd:cd02663 194 LHLKRFKYDEQLNRyiKLFYRVVFPLEL--RLFNTTD-------------DAENPDRLYELVAVVVHIGgGPNHGHYVSI 258
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 84569929 471 IRqHKDQWFKCDDAIITKASIKDVLD--------SEGYLLFY 504
Cdd:cd02663 259 VK-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-492 |
8.69e-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: 124.84 E-value: 8.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPLLRDFFL---SDRHRCEMQSPSSCL-----VCE-MSSLFQEFYSGHRSPHIPYKLLHl 234
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnSTEDAELKNMPPDKPhepqtIIDqLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 235 vwthARHLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNHCNcIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDI 314
Cdd:cd02668 80 ----ALGLDTGQQQDAQEFSKLFLSLL------EAKLSKSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 315 SLDLpgsstpfwplspgsegnvvngeshvSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACF 394
Cdd:cd02668 149 ELQL-------------------------KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 395 HLKRFEHSAKL--RRKITTYVSFPLELDMTPFMASSKEsrmngqyqqptdslnNDNKYSLFAVVNHQGT-LESGHYTSFI 471
Cdd:cd02668 204 QLLRFVFDRKTgaKKKLNASISFPEILDMGEYLAESDE---------------GSYVYELSGVLIHQGVsAYSGHYIAHI 268
|
330 340
....*....|....*....|..
gi 84569929 472 R-QHKDQWFKCDDAIITKASIK 492
Cdd:cd02668 269 KdEQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
1.99e-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: 118.07 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPllrDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSpHIPYKLLHLVWTHARHLA 243
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELAN-QAPRRLLNALREVNPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 244 GYEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 323
Cdd:cd02671 102 GYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 324 PfwplspGSEGNVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 403
Cdd:cd02671 163 S------KSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 404 KLR------RKITTYVSFPLELDMtpFMASSKESRmngqyqqptdslnndNKYSLFAVVNHQG-TLESGHYTSFIRqhkd 476
Cdd:cd02671 237 SEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR---- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 84569929 477 qWFKCDDAIITKASIKDVLD---------SEGYLLFY 504
Cdd:cd02671 296 -WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-504 |
3.26e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 119.73 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 52 VCGVHLNRLH--SCLYC--VFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCfLCQDY-IYDKDMEIIAkeeqrkawkmq 126
Cdd:cd02669 18 VCSVSLSNLNvyACLVCgkYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYC-LPDNYeIIDSSLDDIK----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 127 gvgekfSTWEP--TKRELELLKHNPKRRKITSNCT--IGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLS---DRHRCE 199
Cdd:cd02669 86 ------YVLNPtyTKEQISDLDRDPKLSRDLDGKPylPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 200 MQSPsscLVCEMSSLFQEFYS-----GHRSPHipyKLLHLV--WTHARHLAGyEQQDAHEFLIAALDVLHRhckgDDNGK 272
Cdd:cd02669 160 RKSE---LVKRLSELIRKIWNprnfkGHVSPH---ELLQAVskVSKKKFSIT-EQSDPVEFLSWLLNTLHK----DLGGS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 273 KANNPNhcncIIDQIFTGGLQ--------------SDVTCQVCHGVSTTID-PFWDISLDLPgsstPFWPLSPGSEGNVV 337
Cdd:cd02669 229 KKPNSS----IIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVsPFLLLTLDLP----PPPLFKDGNEENII 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 338 ngeSHVsgttTLTDCLRRFTrpehlGSSakikcsgCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPL 417
Cdd:cd02669 301 ---PQV----PLKQLLKKYD-----GKT-------ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 418 E-LDMTPFMAsskesrmngqyqQPTDSLNNDNKYSLFAVVNHQGT-LESGHYTSFIRQHK-DQWFKCDDAIITKASIKDV 494
Cdd:cd02669 362 KnLDLSDYVH------------FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKStNKWFEIQDLNVKEVLPQLI 429
|
490
....*....|
gi 84569929 495 LDSEGYLLFY 504
Cdd:cd02669 430 FLSESYIQIW 439
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
3.77e-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: 111.26 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHR--CEMQSPSSCLVCEMSSLFQEFYSG-------HRSPHIPYKlLHL 234
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpSDVVDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQ-VGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 235 VWTHARHLAGY--------EQQDAHEFLIAALDVLHRHCKgddnGKKANNPNhcnciidQIFTGGLQSDVTCQVCHGVST 306
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESF----KNLGLNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 307 TIDPFWDISLDLPGSstpfwPLSPGSEGNVVNGEshvsgtTTLTDCLRRFTRPEHLgssaKIKCSGCHSYQESTKQLTMK 386
Cdd:cd02658 149 TSELSEILSLPVPKD-----EATEKEEGELVYEP------VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 387 KLPIVACFHLKRFEHSA-KLRRKITTYVSFPLELDmtpfmasskesrmngqyqqptdslnnDNKYSLFAVVNHQGT-LES 464
Cdd:cd02658 214 TFPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG--------------------------PGKYELIAFISHKGTsVHS 267
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 84569929 465 GHYTSFIRQ---HKDQWFKCDDAIITKASIKDVLDSEGYLLFY 504
Cdd:cd02658 268 GHYVAHIKKeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
161-496 |
4.96e-27 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 115.74 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 161 GLRGLINLGNTCFMNCIVQALTHTPLLRdfflSDRHRCEMQSPSS--CLVCEMSSLFQEFYSGHrsphIPYKLLHLV--- 235
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFR----KDVYGIPTDHPRGrdSVALALQRLFYNLQTGE----EPVDTTELTrsf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 236 -WTHARHlagYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNpnhcnciidqIFTGGLQSDVTCQVCHGVSTTIDPFWDI 314
Cdd:COG5077 264 gWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENALNG----------IFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 315 SLDLPGSSTpfwplspgsegnvvngeshvsgtttLTDCLRRFTRPEHLGSSAKIKCSGcHSYQESTKQLTMKKLPIVACF 394
Cdd:COG5077 331 QLNVKGMKN-------------------------LQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 395 HLKRFEHSAK--LRRKITTYVSFPLELDMTPFMasSKESRmngqyqqptDSLNNDNKYSLFAVVNHQGTLESGHYTSFIR 472
Cdd:COG5077 385 QLKRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDAD---------KSENSDAVYVLYGVLVHSGDLHEGHYYALLK 453
|
330 340
....*....|....*....|....*
gi 84569929 473 QHKD-QWFKCDDAIITKASIKDVLD 496
Cdd:COG5077 454 PEKDgRWYKFDDTRVTRATEKEVLE 478
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
6.35e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 108.35 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGhRSPHIPYKLLHLVWThARHLA 243
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQR-RAEAPPDYFLEASRP-PWFTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 244 GYeQQDAHEFLIAALDVLHrhckgddngkkannpnhcnCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPgsst 323
Cdd:cd02664 79 GS-QQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 324 pfwplspgsegnvvngeshvsgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 403
Cdd:cd02664 135 ------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 404 K--LRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQP--TDSLNNDNK--YSLFAVVNHQGT-LESGHYTSFIR---- 472
Cdd:cd02664 191 KthVREKIMDNVSINEVLSLPVRVESKSSESPLEKKEEEsgDDGELVTRQvhYRLYAVVVHSGYsSESGHYFTYARdqtd 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 84569929 473 -----------------QHKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 504
Cdd:cd02664 271 adstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
6.71e-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: 105.91 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALthtpllrdfflsdrhrcemqspSSClvcemsslfqefysghrsphiPYKLLHLVWTharhla 243
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL----------------------ASL---------------------PSLIEYLEEF------ 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 244 gYEQQDAHEFLIAALDVLHRHCKgddngkkanNPnhcnciidqiFTGGLQSDVTCQVCHGVST-TIDPFWDISLDLPgss 322
Cdd:cd02662 32 -LEQQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 323 tpfwplspgsegnvvngESHVSGTTTLTDCLRRFTRPEHLGSsakIKCSGChsyqestkQLTMKKLPIVACFHLKRFEHS 402
Cdd:cd02662 89 -----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 403 AK-LRRKITTYVSFPLELdmtpfmasskesrmngqyqqptdslnNDNKYSLFAVVNHQGTLESGHYTSFIRQH------- 474
Cdd:cd02662 141 GRgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdke 194
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 84569929 475 --------------KDQWFKCDDAIITKASIKDVL-DSEGYLLFY 504
Cdd:cd02662 195 pgsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
164-506 |
9.20e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.81 E-value: 9.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALT-HTPLLRDffLSDRHRCEMQSpssclvcemsslFQEFYSGHRSP---HIPYKLLHLVWTHA 239
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDE--LLDDLSKELKV------------LKNVIRKPEPDlnqEEALKLFTALWSSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 240 RHLAG-----YEQQDAHEFLIAALDVLhrhckgddngkkaNNPNHcNCIIDQIF-TGGlqsdvtcqvcHGVSTTIDPFWD 313
Cdd:COG5533 67 EHKVGwippmGSQEDAHELLGKLLDEL-------------KLDLV-NSFTIRIFkTTK----------DKKKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 314 ISLDLPGsstpfwplspgsegnvvngESHVSGTTTLTDCLRRFtrpEHLGSSAK-IKCS---GCHSYQESTKQLTMKKLP 389
Cdd:COG5533 123 IIIELPD-------------------QTWVNNLKTLQEFIDNM---EELVDDETgVKAKeneELEVQAKQEYEVSFVKLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 390 IVACFHLKRFEHSAKlRRKITTYVSFPLELDMTPfmasskesrmngqyqQPTDSLNNDNKYSLFAVVNHQGTLESGHYTS 469
Cdd:COG5533 181 KILTIQLKRFANLGG-NQKIDTEVDEKFELPVKH---------------DQILNIVKETYYDLVGFVLHQGSLEGGHYIA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 84569929 470 FIRQhKDQWFKCDDAIITKASIKDVLDS---EGYLLFYHK 506
Cdd:COG5533 245 YVKK-GGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
2.89e-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: 105.88 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPLLRD---FFLSDRhRCEMQSPSScLVCEMSSLFQEFySGHRSPHIPYKLLHLVWTHAR 240
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPAR-RGANQSSDN-LTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 241 HLA------GYEQQDAHEFLIAALDVLHRHCKGDDNGKKAnnpnhcnciIDQIFTGGLQSDVTCQvchgvsttidpfwDI 314
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCT-------------ES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 315 SLDLPGSSTPFWPLSpgsegnvvngeSHVSGTT---TLTDCLRrftrpEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIV 391
Cdd:cd02657 136 PDEEEVSTESEYKLQ-----------CHISITTevnYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 392 ACFHLKRF--EHSAKLRRKITTYVSFPLELDMTPFMASSkesrmngqyqqptdslnndNKYSLFAVVNHQG-TLESGHYT 468
Cdd:cd02657 200 LTVQFVRFfwKRDIQKKAKILRKVKFPFELDLYELCTPS-------------------GYYELVAVITHQGrSADSGHYV 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 84569929 469 SFIRQ-HKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 504
Cdd:cd02657 261 AWVRRkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
164-483 |
6.04e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 75.38 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQALTHTPLLRDFFLSdrHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHAR--- 240
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 241 -HLAGYEQQDAHEFLIAAL-DVLHR---HCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDIS 315
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 316 LDLPGSSTPfwplspgsegnvvngESHVSGTTTLTDCLRRFTRPEhlgSSAKIKCSGCHSYQESTKQLTMKKLPIVACFH 395
Cdd:pfam13423 160 LIYPRKPSS---------------NNKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 396 LKRfeHSAKLRRKITTYVSFPLELDMTPFMASSKEsrmngqyqqptdslNNDNKYSLFAVVNH-QGTLESGHYTSFIR-- 472
Cdd:pfam13423 222 AAL--TNEEWRQLWKTPGWLPPEIGLTLSDDLQGD--------------NEIVKYELRGVVVHiGDSGTSGHLVSFVKva 285
|
330
....*....|....*..
gi 84569929 473 ------QHKDQWFKCDD 483
Cdd:pfam13423 286 dseledPTESQWYLFND 302
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
50-110 |
6.64e-13 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 63.43 E-value: 6.64e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84569929 50 CHVCGVHLNrLHSCLYCVFFGCFTKK--HIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIYDKD 110
Cdd:pfam02148 1 CSLCGNTSN-LWLCLTCGHVGCGRYQnsHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
164-504 |
2.75e-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: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 164 GLINLGNTCFMNCIVQAL-THTPLlRDFFLS-DRHRCEMQSP-------------------SSCLVCEMSSLFQEF-YSG 221
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKPL-RDLVLNfDESKAELASDypterriggrevsrselqrSNQFVYELRSLFNDLiHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 222 HRSPHiPYKLLHLvwtharhlAGYEQQDAHEFLIAALDVLHRHCKGDDN---GKKANNPNHCNCIIDQIFTGGL-QSDVT 297
Cdd:cd02666 82 TRSVT-PSKELAY--------LALRQQDVTECIDNVLFQLEVALEPISNafaGPDTEDDKEQSDLIKRLFSGKTkQQLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 298 CQVCHGVSTTIDPFWDISLdlpgsstpfwPLSPGSEGNVVNGESHvsgTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQ 377
Cdd:cd02666 153 ESMGNQPSVRTKTERFLSL----------LVDVGKKGREIVVLLE---PKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 378 -ESTKQLTMKK--LPIVAcfhlkrfEHSAKLRRKITTYVSFPLEldmtpfMASSKESRMNGQYQQPTDSLNNdNKYSLFA 454
Cdd:cd02666 220 pLQRELISMDRyeLPSSI-------DDIDELIREAIQSESSLVR------QAQNELAELKHEIEKQFDDLKS-YGYRLHA 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 84569929 455 VVNHQGTLESGHYTSFIRQH-KDQWFKCDDAIIT-KASIKDVLDSEG-----YLLFY 504
Cdd:cd02666 286 VFIHRGEASSGHYWVYIKDFeENVWRKYNDETVTvVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
247-504 |
1.50e-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: 55.61 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 247 QQDAHEFLIAALdvlhrHCKGDDNGKKANNPNHCNCIIDQI-----FTGGLQSDVTCQVCHGVSTTIDPFWDISLD---- 317
Cdd:cd02673 33 QQDAHEFLLTLL-----EAIDDIMQVNRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSFEENVSDVGNFLDVSmidn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 318 ----LPGSSTPFWPLSP-GSEGNVVNGESHVSgtttltdCLRRFTRPEHLGSSAKikcsgCHSYQESTKQLTMKKLPIVA 392
Cdd:cd02673 108 kldiDELLISNFKTWSPiEKDCSSCKCESAIS-------SERIMTFPECLSINLK-----RYKLRIATSDYLKKNEEIMK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 393 CFHLKrfehsaklrrkittyvsfpleldmtpfmasskesrmngqyqqptdslnnDNKYSLFAVVNHQG-TLESGHYTSFI 471
Cdd:cd02673 176 KYCGT-------------------------------------------------DAKYSLVAVICHLGeSPYDGHYIAYT 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 84569929 472 RQ--HKDQWFKCDDAIITKASIKDVLD---SEGYLLFY 504
Cdd:cd02673 207 KElyNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
386-504 |
1.64e-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: 49.45 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 386 KKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPT-------DSLNNDNKYSLFAVVNH 458
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVcyddkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84569929 459 QGT-LESGHYTSFIRQHKD------------QWFKCDD-----AIITKASIKDVLDSE-GYLLFY 504
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
343-504 |
1.33e-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: 46.40 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 343 VSGTTTLTDCLRRFT---RPEHLGSSAKIKCSGCHSYQEstkqltmkkLPIVACFHLKRFEHSAKLRRKITTYVSFPLEL 419
Cdd:cd02665 89 VNGYGNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQII 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84569929 420 DMTPfmasskesrmngqyqqptdslnndnkYSLFAVVNHQGTLESGHYTSFI-RQHKDQWFKCDDAIITKASIKDVL-DS 497
Cdd:cd02665 160 QQVP--------------------------YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVErDS 213
|
170
....*....|....
gi 84569929 498 EG-------YLLFY 504
Cdd:cd02665 214 FGggrnpsaYCLMY 227
|
|
| |
