|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-518 |
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 150010639 176 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRH--RCEMQSPSSCLVCEMSSLFQEF-YSGHRSPHIPYKLLHLVWTHA 252
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 253 RHLAGYEQQDAHEFLIAALDVLHRHCKGDDNgkKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 332
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN--EANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 333 GSSTPFWPLspgsegnvvnGESHVSGTTTLTDCLRRFTRPEHLGSSAkIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 412
Cdd:cd02660 159 NKSTPSWAL----------GESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 413 EHSA-KLRRKITTYVSFPLELDMTPFMASSKesrmngQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQW 491
Cdd:cd02660 228 EHSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQW 301
|
330 340
....*....|....*....|....*..
gi 150010639 492 FKCDDAIITKASIKDVLDSEGYLLFYH 518
Cdd:cd02660 302 FKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
176-517 |
3.60e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 270.85 E-value: 3.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 176 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCE--MQSPSSCLVCEMSSLFQEFYSGHRSPHI-PYKLLHLVWTHA 252
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEdsRYNKDINLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 253 RHLAGYEQQDAHEFLIAALDVLHRhckgddnGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 332
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE-------DLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 333 GSSTPfwplspgsegnvvngeshvSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 412
Cdd:pfam00443 154 GDSAE-------------------LKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 413 EHSAKLRRKITTYVSFPLELDMTPFMASSKESRmngqyqqptdsLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKD-QW 491
Cdd:pfam00443 215 SYNRSTWEKLNTEVEFPLELDLSRYLAEELKPK-----------TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRW 283
|
330 340
....*....|....*....|....*..
gi 150010639 492 FKCDDAIITKAS-IKDVLDSEGYLLFY 517
Cdd:pfam00443 284 YKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-517 |
1.79e-75 |
|
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: 240.64 E-value: 1.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 176 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHL 255
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 256 AGYEQQDAHEFLIAALDVLHRHC-KGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGS 334
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAClDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 335 STpfwplspgsegnvvngeshvsgtttLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFeh 414
Cdd:cd02661 162 DS-------------------------LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 415 SAKLRRKITTYVSFPLELDMTPFMASSKESrmngqyqqPTdslnndnKYSLFAVVNHQGT-LESGHYTSFIRQHKDQWFK 493
Cdd:cd02661 215 SNFRGGKINKQISFPETLDLSPYMSQPNDG--------PL-------KYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYN 279
|
330 340
....*....|....*....|....
gi 150010639 494 CDDAIITKASIKDVLDSEGYLLFY 517
Cdd:cd02661 280 MDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
177-517 |
1.65e-71 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 228.52 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 256
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 257 gyEQQDAHEFLIAALDVLHRHCKGddNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 336
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 337 PfwplspgsegnvvngeshvsgTTTLTDCLRRFTRPEHLGSSAKIKCSgCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02257 97 P---------------------QVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 417 KLRR-KITTYVSFPLELDMTPFMASSKEsrmngqyqqPTDSLNNDNKYSLFAVVNHQGTL-ESGHYTSFIRQH-KDQWFK 493
Cdd:cd02257 155 DGTKeKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYK 225
|
330 340
....*....|....*....|....*....
gi 150010639 494 CDDAIITKASIKDVLD-----SEGYLLFY 517
Cdd:cd02257 226 FNDDKVTEVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
3.06e-69 |
|
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: 221.78 E-value: 3.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 256
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 257 gyEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 336
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 337 PFWPLspgsegnvvngeshvsgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02674 80 DAPKV-------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 417 KLRRKITTYVSFPLE-LDMTPFMASSkesrmngqyqqptdSLNNDNKYSLFAVVNHQGTLESGHYTSFIR-QHKDQWFKC 494
Cdd:cd02674 141 GSTRKLTTPVTFPLNdLDLTPYVDTR--------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKnNETNDWYKF 206
|
330 340
....*....|....*....|...
gi 150010639 495 DDAIITKASIKDVLDSEGYLLFY 517
Cdd:cd02674 207 DDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
4.93e-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: 183.74 E-value: 4.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRhrcemqspssclvcemSSLFQEFysghRSPHIPYKllhlvwtharhla 256
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP----------------KELFSQV----CRKAPQFK------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 257 GYEQQDAHEFLIAALDVLhrhckgddngkkannpnhcNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISldLPGSST 336
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLS--LPRSDE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 337 PFWPlspgsegnvvngeshvsgtTTLTDCLRRFTRPEHLGSSAKIKCSGChsyQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02667 107 IKSE-------------------CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 417 KLR-RKITTYVSFPLELDMTPFMASSKESrmngqyqqptDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQH-------- 487
Cdd:cd02667 165 SANlRKVSRHVSFPEILDLAPFCDPKCNS----------SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsd 234
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 150010639 488 --------------KDQWFKCDDAIITKASIKDVLDSEGYLLFY 517
Cdd:cd02667 235 ltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
174-510 |
5.00e-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: 174.75 E-value: 5.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 174 GLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRcEMQSPSSCLVCEMSSLFQEFYSGHrSPHIPYKLLHLV----W 249
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLSE-SPVKTTELTDKTrsfgW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 250 THarhLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISL 329
Cdd:cd02659 79 DS---LNTFEQHDVQEFFRVLFDKL------EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 330 DlpgsstpfwplspgsegnvvngeshVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHL 409
Cdd:cd02659 146 A-------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 410 KRFEHS--AKLRRKITTYVSFPLELDMTPFMASSkesrMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQ- 486
Cdd:cd02659 201 KRFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDr 276
|
330 340
....*....|....*....|....
gi 150010639 487 HKDQWFKCDDAIITKASIKDVLDS 510
Cdd:cd02659 277 DDGKWYKFNDDVVTPFDPNDAEEE 300
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
163-517 |
1.64e-39 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 153.50 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 163 KRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPS-----SCLVCEMSSLFQEFYSGHRS 237
Cdd:COG5560 253 DDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplgmhGSVASAYADLIKQLYDGNLH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 238 PHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHR--------------HCKGDDNGKKANNPNHC-------NC- 295
Cdd:COG5560 333 AFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKECwwehlkrNDs 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 296 IIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST---------PFWPLSP----------------------- 343
Cdd:COG5560 413 IITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtivvfpESGRRQPlkieldasstirglkklvdaeyg 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 344 -----------------------------------------GSEGN-----VVNG------------------------- 352
Cdd:COG5560 493 klgcfeikvmciyyggnynmlepadkvllqdipqtdfvylyETNDNgievpVVHLriekgykskrlfgdpflqlnvlika 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 353 ------------------------------------ESHVSG-------------------------------------- 358
Cdd:COG5560 573 siydklvkefeellvlvemkktdvdlvseqvrllreESSPSSwlkleteidtkreeqveeegqmnfndavvisceweekr 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 359 ---------------------TTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAK 417
Cdd:COG5560 653 ylslfsydplwtireigaaerTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 418 LRRKITTYVSFPL-ELDMTPFMASSKESRMNgqyqqptdslnndnkYSLFAVVNHQGTLESGHYTSFIRQHKDQ-WFKCD 495
Cdd:COG5560 733 FRDKIDDLVEYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFD 797
|
570 580
....*....|....*....|..
gi 150010639 496 DAIITKASIKDVLDSEGYLLFY 517
Cdd:COG5560 798 DSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
5.68e-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: 143.99 E-value: 5.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPL---LRDFFlsdrhrcEMQSPSSCLVCEMSslfqefysghrsphiPYKLLHLVWTHAR 253
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLltcLKDLF-------ESISEQKKRTGVIS---------------PKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 254 HLAGYEQQDAHEFL-------IAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWD 326
Cdd:cd02663 59 LFDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 327 ISLDLPGSstpfwplspgsegnvvngeshvsgtTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVAC 406
Cdd:cd02663 139 LSIDVEQN-------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 407 FHLKRFEHSAKLRR--KITTYVSFPLELdmTPFMASSkesrmngqyqqptDSLNNDNKYSLFAVVNHQG-TLESGHYTSF 483
Cdd:cd02663 194 LHLKRFKYDEQLNRyiKLFYRVVFPLEL--RLFNTTD-------------DAENPDRLYELVAVVVHIGgGPNHGHYVSI 258
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 150010639 484 IRqHKDQWFKCDDAIITKASIKDVLD--------SEGYLLFY 517
Cdd:cd02663 259 VK-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-505 |
1.25e-31 |
|
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: 124.46 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPLLRDFFL---SDRHRCEMQSPSSCL-----VCE-MSSLFQEFYSGHRSPHIPYKLLHl 247
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnSTEDAELKNMPPDKPhepqtIIDqLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 248 vwthARHLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNHCNcIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDI 327
Cdd:cd02668 80 ----ALGLDTGQQQDAQEFSKLFLSLL------EAKLSKSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 328 SLDLpgsstpfwplspgsegnvvngeshvSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACF 407
Cdd:cd02668 149 ELQL-------------------------KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 408 HLKRFEHSAKL--RRKITTYVSFPLELDMTPFMASSKEsrmngqyqqptdslnNDNKYSLFAVVNHQGT-LESGHYTSFI 484
Cdd:cd02668 204 QLLRFVFDRKTgaKKKLNASISFPEILDMGEYLAESDE---------------GSYVYELSGVLIHQGVsAYSGHYIAHI 268
|
330 340
....*....|....*....|..
gi 150010639 485 R-QHKDQWFKCDDAIITKASIK 505
Cdd:cd02668 269 KdEQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
3.29e-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: 117.69 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPllrDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSpHIPYKLLHLVWTHARHLA 256
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELAN-QAPRRLLNALREVNPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 257 GYEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 336
Cdd:cd02671 102 GYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 337 PfwplspGSEGNVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02671 163 S------KSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 417 KLR------RKITTYVSFPLELDMtpFMASSKESRmngqyqqptdslnndNKYSLFAVVNHQG-TLESGHYTSFIRqhkd 489
Cdd:cd02671 237 SEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR---- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 150010639 490 qWFKCDDAIITKASIKDVLD---------SEGYLLFY 517
Cdd:cd02671 296 -WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
65-517 |
1.35e-28 |
|
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: 118.19 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 65 VCGVHLNRLH--SCLYC--VFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCfLCQDY-IYDKDMEIIAkeeqrkawkmq 139
Cdd:cd02669 18 VCSVSLSNLNvyACLVCgkYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYC-LPDNYeIIDSSLDDIK----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 140 gvgekfSTWEP--TKRELELLKHNPKRRKITSNCT--IGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLS---DRHRCE 212
Cdd:cd02669 86 ------YVLNPtyTKEQISDLDRDPKLSRDLDGKPylPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 213 MQSPsscLVCEMSSLFQEFYS-----GHRSPHipyKLLHLV--WTHARHLAGyEQQDAHEFLIAALDVLHRhckgDDNGK 285
Cdd:cd02669 160 RKSE---LVKRLSELIRKIWNprnfkGHVSPH---ELLQAVskVSKKKFSIT-EQSDPVEFLSWLLNTLHK----DLGGS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 286 KANNPNhcncIIDQIFTGGLQ--------------SDVTCQVCHGVSTTID-PFWDISLDLPgsstPFWPLSPGSEGNVV 350
Cdd:cd02669 229 KKPNSS----IIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVsPFLLLTLDLP----PPPLFKDGNEENII 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 351 ngeSHVsgttTLTDCLRRFTrpehlGSSakikcsgCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPL 430
Cdd:cd02669 301 ---PQV----PLKQLLKKYD-----GKT-------ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 431 E-LDMTPFMAsskesrmngqyqQPTDSLNNDNKYSLFAVVNHQGT-LESGHYTSFIRQHK-DQWFKCDDAIITKASIKDV 507
Cdd:cd02669 362 KnLDLSDYVH------------FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKStNKWFEIQDLNVKEVLPQLI 429
|
490
....*....|
gi 150010639 508 LDSEGYLLFY 517
Cdd:cd02669 430 FLSESYIQIW 439
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
7.63e-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: 110.49 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHR--CEMQSPSSCLVCEMSSLFQEFYSG-------HRSPHIPYKlLHL 247
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpSDVVDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQ-VGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 248 VWTHARHLAGY--------EQQDAHEFLIAALDVLHRHCKgddnGKKANNPNhcnciidQIFTGGLQSDVTCQVCHGVST 319
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESF----KNLGLNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 320 TIDPFWDISLDLPGSstpfwPLSPGSEGNVVNGEshvsgtTTLTDCLRRFTRPEHLgssaKIKCSGCHSYQESTKQLTMK 399
Cdd:cd02658 149 TSELSEILSLPVPKD-----EATEKEEGELVYEP------VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 400 KLPIVACFHLKRFEHSA-KLRRKITTYVSFPLELDmtpfmasskesrmngqyqqptdslnnDNKYSLFAVVNHQGT-LES 477
Cdd:cd02658 214 TFPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG--------------------------PGKYELIAFISHKGTsVHS 267
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 150010639 478 GHYTSFIRQ---HKDQWFKCDDAIITKASIKDVLDSEGYLLFY 517
Cdd:cd02658 268 GHYVAHIKKeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
174-509 |
1.93e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 114.20 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 174 GLRGLINLGNTCFMNCIVQALTHTPLLRdfflSDRHRCEMQSPSS--CLVCEMSSLFQEFYSGHrsphIPYKLLHLV--- 248
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFR----KDVYGIPTDHPRGrdSVALALQRLFYNLQTGE----EPVDTTELTrsf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 249 -WTHARHlagYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNpnhcnciidqIFTGGLQSDVTCQVCHGVSTTIDPFWDI 327
Cdd:COG5077 264 gWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENALNG----------IFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 328 SLDLPGSSTpfwplspgsegnvvngeshvsgtttLTDCLRRFTRPEHLGSSAKIKCSGcHSYQESTKQLTMKKLPIVACF 407
Cdd:COG5077 331 QLNVKGMKN-------------------------LQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 408 HLKRFEHSAK--LRRKITTYVSFPLELDMTPFMasSKESRmngqyqqptDSLNNDNKYSLFAVVNHQGTLESGHYTSFIR 485
Cdd:COG5077 385 QLKRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDAD---------KSENSDAVYVLYGVLVHSGDLHEGHYYALLK 453
|
330 340
....*....|....*....|....*
gi 150010639 486 QHKD-QWFKCDDAIITKASIKDVLD 509
Cdd:COG5077 454 PEKDgRWYKFDDTRVTRATEKEVLE 478
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
8.30e-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: 107.96 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGhRSPHIPYKLLHLVWThARHLA 256
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQR-RAEAPPDYFLEASRP-PWFTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 257 GYeQQDAHEFLIAALDVLHrhckgddngkkannpnhcnCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPgsst 336
Cdd:cd02664 79 GS-QQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 337 pfwplspgsegnvvngeshvsgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02664 135 ------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 417 K--LRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQP--TDSLNNDNK--YSLFAVVNHQGT-LESGHYTSFIR---- 485
Cdd:cd02664 191 KthVREKIMDNVSINEVLSLPVRVESKSSESPLEKKEEEsgDDGELVTRQvhYRLYAVVVHSGYsSESGHYFTYARdqtd 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 150010639 486 -----------------QHKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 517
Cdd:cd02664 271 adstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
9.16e-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: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALthtpllrdfflsdrhrcemqspSSClvcemsslfqefysghrsphiPYKLLHLVWTharhla 256
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL----------------------ASL---------------------PSLIEYLEEF------ 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 257 gYEQQDAHEFLIAALDVLHRHCKgddngkkanNPnhcnciidqiFTGGLQSDVTCQVCHGVST-TIDPFWDISLDLPgss 335
Cdd:cd02662 32 -LEQQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 336 tpfwplspgsegnvvngESHVSGTTTLTDCLRRFTRPEHLGSsakIKCSGChsyqestkQLTMKKLPIVACFHLKRFEHS 415
Cdd:cd02662 89 -----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 416 AK-LRRKITTYVSFPLELdmtpfmasskesrmngqyqqptdslnNDNKYSLFAVVNHQGTLESGHYTSFIRQH------- 487
Cdd:cd02662 141 GRgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdke 194
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 150010639 488 --------------KDQWFKCDDAIITKASIKDVL-DSEGYLLFY 517
Cdd:cd02662 195 pgsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
177-519 |
1.01e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.81 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALT-HTPLLRDffLSDRHRCEMQSpssclvcemsslFQEFYSGHRSP---HIPYKLLHLVWTHA 252
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDE--LLDDLSKELKV------------LKNVIRKPEPDlnqEEALKLFTALWSSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 253 RHLAG-----YEQQDAHEFLIAALDVLhrhckgddngkkaNNPNHcNCIIDQIF-TGGlqsdvtcqvcHGVSTTIDPFWD 326
Cdd:COG5533 67 EHKVGwippmGSQEDAHELLGKLLDEL-------------KLDLV-NSFTIRIFkTTK----------DKKKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 327 ISLDLPGsstpfwplspgsegnvvngESHVSGTTTLTDCLRRFtrpEHLGSSAK-IKCS---GCHSYQESTKQLTMKKLP 402
Cdd:COG5533 123 IIIELPD-------------------QTWVNNLKTLQEFIDNM---EELVDDETgVKAKeneELEVQAKQEYEVSFVKLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 403 IVACFHLKRFEHSAKlRRKITTYVSFPLELDMTPfmasskesrmngqyqQPTDSLNNDNKYSLFAVVNHQGTLESGHYTS 482
Cdd:COG5533 181 KILTIQLKRFANLGG-NQKIDTEVDEKFELPVKH---------------DQILNIVKETYYDLVGFVLHQGSLEGGHYIA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 150010639 483 FIRQhKDQWFKCDDAIITKASIKDVLDS---EGYLLFYHK 519
Cdd:COG5533 245 YVKK-GGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
3.86e-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: 105.49 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPLLRD---FFLSDRhRCEMQSPSScLVCEMSSLFQEFySGHRSPHIPYKLLHLVWTHAR 253
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPAR-RGANQSSDN-LTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 254 HLA------GYEQQDAHEFLIAALDVLHRHCKGDDNGKKAnnpnhcnciIDQIFTGGLQSDVTCQvchgvsttidpfwDI 327
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCT-------------ES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 328 SLDLPGSSTPFWPLSpgsegnvvngeSHVSGTT---TLTDCLRrftrpEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIV 404
Cdd:cd02657 136 PDEEEVSTESEYKLQ-----------CHISITTevnYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 405 ACFHLKRF--EHSAKLRRKITTYVSFPLELDMTPFMASSkesrmngqyqqptdslnndNKYSLFAVVNHQG-TLESGHYT 481
Cdd:cd02657 200 LTVQFVRFfwKRDIQKKAKILRKVKFPFELDLYELCTPS-------------------GYYELVAVITHQGrSADSGHYV 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 150010639 482 SFIRQ-HKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 517
Cdd:cd02657 261 AWVRRkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
177-496 |
8.10e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 75.38 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSdrHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHAR--- 253
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 254 -HLAGYEQQDAHEFLIAAL-DVLHR---HCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDIS 328
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 329 LDLPGSSTPfwplspgsegnvvngESHVSGTTTLTDCLRRFTRPEhlgSSAKIKCSGCHSYQESTKQLTMKKLPIVACFH 408
Cdd:pfam13423 160 LIYPRKPSS---------------NNKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 409 LKRfeHSAKLRRKITTYVSFPLELDMTPFMASSKEsrmngqyqqptdslNNDNKYSLFAVVNH-QGTLESGHYTSFIR-- 485
Cdd:pfam13423 222 AAL--TNEEWRQLWKTPGWLPPEIGLTLSDDLQGD--------------NEIVKYELRGVVVHiGDSGTSGHLVSFVKva 285
|
330
....*....|....*..
gi 150010639 486 ------QHKDQWFKCDD 496
Cdd:pfam13423 286 dseledPTESQWYLFND 302
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
63-123 |
1.21e-12 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 62.66 E-value: 1.21e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150010639 63 CHVCGVHLNrLHSCLYCVFFGCFTKK--HIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIYDKD 123
Cdd:pfam02148 1 CSLCGNTSN-LWLCLTCGHVGCGRYQnsHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
2.86e-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: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 177 GLINLGNTCFMNCIVQAL-THTPLlRDFFLS-DRHRCEMQSP-------------------SSCLVCEMSSLFQEF-YSG 234
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKPL-RDLVLNfDESKAELASDypterriggrevsrselqrSNQFVYELRSLFNDLiHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 235 HRSPHiPYKLLHLvwtharhlAGYEQQDAHEFLIAALDVLHRHCKGDDN---GKKANNPNHCNCIIDQIFTGGL-QSDVT 310
Cdd:cd02666 82 TRSVT-PSKELAY--------LALRQQDVTECIDNVLFQLEVALEPISNafaGPDTEDDKEQSDLIKRLFSGKTkQQLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 311 CQVCHGVSTTIDPFWDISLdlpgsstpfwPLSPGSEGNVVNGESHvsgTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQ 390
Cdd:cd02666 153 ESMGNQPSVRTKTERFLSL----------LVDVGKKGREIVVLLE---PKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 391 -ESTKQLTMKK--LPIVAcfhlkrfEHSAKLRRKITTYVSFPLEldmtpfMASSKESRMNGQYQQPTDSLNNdNKYSLFA 467
Cdd:cd02666 220 pLQRELISMDRyeLPSSI-------DDIDELIREAIQSESSLVR------QAQNELAELKHEIEKQFDDLKS-YGYRLHA 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 150010639 468 VVNHQGTLESGHYTSFIRQH-KDQWFKCDDAIIT-KASIKDVLDSEG-----YLLFY 517
Cdd:cd02666 286 VFIHRGEASSGHYWVYIKDFeENVWRKYNDETVTvVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
460-517 |
3.19e-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: 3.19e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150010639 460 DNKYSLFAVVNHQG-TLESGHYTSFIRQ--HKDQWFKCDDAIITKASIKDVLD---SEGYLLFY 517
Cdd:cd02673 181 DAKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
399-517 |
2.28e-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: 49.06 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 399 KKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPT-------DSLNNDNKYSLFAVVNH 471
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVcyddkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150010639 472 QGT-LESGHYTSFIRQHKD------------QWFKCDD-----AIITKASIKDVLDSE-GYLLFY 517
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
356-517 |
1.40e-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: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 356 VSGTTTLTDCLRRFT---RPEHLGSSAKIKCSGCHSYQEstkqltmkkLPIVACFHLKRFEHSAKLRRKITTYVSFPLEL 432
Cdd:cd02665 89 VNGYGNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQII 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010639 433 DMTPfmasskesrmngqyqqptdslnndnkYSLFAVVNHQGTLESGHYTSFI-RQHKDQWFKCDDAIITKASIKDVL-DS 510
Cdd:cd02665 160 QQVP--------------------------YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVErDS 213
|
170
....*....|....
gi 150010639 511 EG-------YLLFY 517
Cdd:cd02665 214 FGggrnpsaYCLMY 227
|
|
| |
