|
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: 516.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 176 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRH--RCEMQSPSSCLVCEMSSLFQEF-YSGHRSPHIPYKLLHLVWTHA 252
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 253 RHLAGYEQQDAHEFLIAALDVLHRHCKGDDNgkKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 332
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN--EANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 333 GSSTPFWPLspgsegsvvnGESHASGTTTLTDCLRRFTRPEHLGSSAkIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 412
Cdd:cd02660 159 NKSTPSWAL----------GESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 413 EHSA-KLRRKITTYVSFPLELDMTPFMASSKesrmngQYQQPLDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQW 491
Cdd:cd02660 228 EHSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQW 301
|
330 340
....*....|....*....|....*..
gi 110625685 492 FKCDDAIITKASIKDVLDSEGYLLFYH 518
Cdd:cd02660 302 FKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
176-517 |
4.82e-87 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 270.85 E-value: 4.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 176 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCE--MQSPSSCLVCEMSSLFQEFYSGHRSPHI-PYKLLHLVWTHA 252
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEdsRYNKDINLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 253 RHLAGYEQQDAHEFLIAALDVLHRhckgddnGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP 332
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE-------DLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 333 GSSTPfwplspgsegsvvngeshaSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRF 412
Cdd:pfam00443 154 GDSAE-------------------LKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 413 EHSAKLRRKITTYVSFPLELDMTPFMASSKESRmngqyqqpldsLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKD-QW 491
Cdd:pfam00443 215 SYNRSTWEKLNTEVEFPLELDLSRYLAEELKPK-----------TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRW 283
|
330 340
....*....|....*....|....*..
gi 110625685 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 |
2.12e-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: 240.26 E-value: 2.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 176 RGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHL 255
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 256 AGYEQQDAHEFLIAALDVLHRHC-KGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGS 334
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAClDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 335 STpfwplspgsegsvvngeshasgtttLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFeh 414
Cdd:cd02661 162 DS-------------------------LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 415 SAKLRRKITTYVSFPLELDMTPFMASSKESrmngqyqqPLdslnndnKYSLFAVVNHQGT-LESGHYTSFIRQHKDQWFK 493
Cdd:cd02661 215 SNFRGGKINKQISFPETLDLSPYMSQPNDG--------PL-------KYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYN 279
|
330 340
....*....|....*....|....
gi 110625685 494 CDDAIITKASIKDVLDSEGYLLFY 517
Cdd:cd02661 280 MDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
177-517 |
3.14e-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: 227.75 E-value: 3.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 256
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 257 gyEQQDAHEFLIAALDVLHRHCKGddNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 336
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 337 PfwplspgsegsvvngeshasgTTTLTDCLRRFTRPEHLGSSAKIKCSgCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02257 97 P---------------------QVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 417 KLRR-KITTYVSFPLELDMTPFMASSKEsrmngqyqqPLDSLNNDNKYSLFAVVNHQGTL-ESGHYTSFIRQH-KDQWFK 493
Cdd:cd02257 155 DGTKeKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYK 225
|
330 340
....*....|....*....|....*....
gi 110625685 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 |
3.33e-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: 3.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHtpllrdfflsdrhrcemqspssclvcemsslfqefysghrsphipykllhlvwtharhla 256
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 257 gyEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 336
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 337 PFWPLspgsegsvvngeshasgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02674 80 DAPKV-------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 417 KLRRKITTYVSFPLE-LDMTPFMASSkesrmngqyqqpldSLNNDNKYSLFAVVNHQGTLESGHYTSFIR-QHKDQWFKC 494
Cdd:cd02674 141 GSTRKLTTPVTFPLNdLDLTPYVDTR--------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKnNETNDWYKF 206
|
330 340
....*....|....*....|...
gi 110625685 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 |
5.42e-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: 5.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRhrcemqspssclvcemSSLFQEFysghRSPHIPYKllhlvwtharhla 256
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP----------------KELFSQV----CRKAPQFK------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 257 GYEQQDAHEFLIAALDVLhrhckgddngkkannpnhcNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLdlpgsst 336
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 337 pfwPLSPGSEGSVvngeshasgttTLTDCLRRFTRPEHLGSSAKIKCSGChsyQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02667 102 ---PRSDEIKSEC-----------SIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 417 KLR-RKITTYVSFPLELDMTPFMASSKESrmngqyqqplDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQH-------- 487
Cdd:cd02667 165 SANlRKVSRHVSFPEILDLAPFCDPKCNS----------SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsd 234
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 110625685 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 |
8.59e-49 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 171.29 E-value: 8.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 174 GLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRcEMQSPSSCLVCEMSSLFQEFYSGHrSPHIPYKLLHLV----W 249
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLSE-SPVKTTELTDKTrsfgW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 250 THarhLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISL 329
Cdd:cd02659 79 DS---LNTFEQHDVQEFFRVLFDKL------EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 330 DLpgsstpfwplspgsegsvvngeshaSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHL 409
Cdd:cd02659 146 AV-------------------------KGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 410 KRFEHS--AKLRRKITTYVSFPLELDMTPFMASSkesrMNGQYQQPLDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQ- 486
Cdd:cd02659 201 KRFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDr 276
|
330 340
....*....|....*....|....
gi 110625685 487 HKDQWFKCDDAIITKASIKDVLDS 510
Cdd:cd02659 277 DDGKWYKFNDDVVTPFDPNDAEEE 300
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
163-517 |
4.60e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 155.04 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 163 KRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPS-----SCLVCEMSSLFQEFYSGHRS 237
Cdd:COG5560 253 DDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplgmhGSVASAYADLIKQLYDGNLH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 238 PHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHR--------------HCKGDDNGKKANNPNHC-------NC- 295
Cdd:COG5560 333 AFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKECwwehlkrNDs 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 296 IIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLP--------------------------GSST------------- 336
Cdd:COG5560 413 IITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPvsmvwkhtivvfpesgrrqplkieldASSTirglkklvdaeyg 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 337 ---------------------------------------------------------------------PFWPLSPGSEG 347
Cdd:COG5560 493 klgcfeikvmciyyggnynmlepadkvllqdipqtdfvylyetndngievpvvhlriekgykskrlfgdPFLQLNVLIKA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 348 SVVNG-------------------------------ESHASG-------------------------------------- 358
Cdd:COG5560 573 SIYDKlvkefeellvlvemkktdvdlvseqvrllreESSPSSwlkleteidtkreeqveeegqmnfndavvisceweekr 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 359 ---------------------TTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAK 417
Cdd:COG5560 653 ylslfsydplwtireigaaerTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 418 LRRKITTYVSFPL-ELDMTPFMASSKESRMNgqyqqpldslnndnkYSLFAVVNHQGTLESGHYTSFIRQHKDQ-WFKCD 495
Cdd:COG5560 733 FRDKIDDLVEYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFD 797
|
570 580
....*....|....*....|..
gi 110625685 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 |
4.97e-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: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPL---LRDFFlsdrhrcEMQSPSSCLVCEMSslfqefysghrsphiPYKLLHLVWTHAR 253
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLltcLKDLF-------ESISEQKKRTGVIS---------------PKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 254 HLAGYEQQDAHEFL-------IAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWD 326
Cdd:cd02663 59 LFDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 327 ISLDLPGSstpfwplspgsegsvvngeshasgtTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVAC 406
Cdd:cd02663 139 LSIDVEQN-------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 407 FHLKRFEHSAKLRR--KITTYVSFPLELdmTPFMASSkesrmngqyqqplDSLNNDNKYSLFAVVNHQG-TLESGHYTSF 483
Cdd:cd02663 194 LHLKRFKYDEQLNRyiKLFYRVVFPLEL--RLFNTTD-------------DAENPDRLYELVAVVVHIGgGPNHGHYVSI 258
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110625685 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 |
1.27e-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: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPLLRDFFL---SDRHRCEMQSPSSCL-----VCE-MSSLFQEFYSGHRSPHIPYKLLHl 247
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnSTEDAELKNMPPDKPhepqtIIDqLQLIFAQLQFGNRSVVDPSGFVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 248 vwthARHLAGYEQQDAHEFLIAALDVLhrhckgDDNGKKANNPNHCNcIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDI 327
Cdd:cd02668 80 ----ALGLDTGQQQDAQEFSKLFLSLL------EAKLSKSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 328 SLDLpgsstpfwplspgsegsvvngeshaSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACF 407
Cdd:cd02668 149 ELQL-------------------------KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 408 HLKRFEHSAKL--RRKITTYVSFPLELDMTPFMASSKEsrmngqyqqpldslnNDNKYSLFAVVNHQGT-LESGHYTSFI 484
Cdd:cd02668 204 QLLRFVFDRKTgaKKKLNASISFPEILDMGEYLAESDE---------------GSYVYELSGVLIHQGVsAYSGHYIAHI 268
|
330 340
....*....|....*....|..
gi 110625685 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 |
8.52e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 119.61 E-value: 8.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPllrDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSpHIPYKLLHLVWTHARHLA 256
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELAN-QAPRRLLNALREVNPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 257 GYEQQDAHEFLIAALDVLHRhckgddngkkannpnhcncIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSST 336
Cdd:cd02671 102 GYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 337 PfwplspGSEGSVVNGESHASGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02671 163 S------KSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 417 KLR------RKITTYVSFPLELDMtpFMASSKESRmngqyqqpldslnndNKYSLFAVVNHQG-TLESGHYTSFIRqhkd 489
Cdd:cd02671 237 SEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR---- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 110625685 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 |
2.14e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 114.72 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 65 VCGIHLNRLH--SCLYC--VFFGCFTKKHIHDHAKSKRHNLAIDLMYGGIYCfLCQDY-IYDK---DIEIIAKeeqrkaw 136
Cdd:cd02669 18 VCSVSLSNLNvyACLVCgkYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYC-LPDNYeIIDSsldDIKYVLN------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 137 kmqgvgekfstweP--TKRELELLKHNPKRRKITSNCT--IGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLS---DRH 209
Cdd:cd02669 90 -------------PtyTKEQISDLDRDPKLSRDLDGKPylPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 210 RCEMQSPsscLVCEMSSLFQEFYS-----GHRSPHipyKLLHLV--WTHARHLAGyEQQDAHEFLIAALDVLHRhckgDD 282
Cdd:cd02669 157 IKDRKSE---LVKRLSELIRKIWNprnfkGHVSPH---ELLQAVskVSKKKFSIT-EQSDPVEFLSWLLNTLHK----DL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 283 NGKKANNPNhcncIIDQIFTGGLQ--------------SDVTCQVCHGVSTTID-PFWDISLDLPgsstPFWPLSPGSEG 347
Cdd:cd02669 226 GGSKKPNSS----IIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVsPFLLLTLDLP----PPPLFKDGNEE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 348 SVVNgeshasgTTTLTDCLRRFTrpehlGSSakikcsgCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVS 427
Cdd:cd02669 298 NIIP-------QVPLKQLLKKYD-----GKT-------ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 428 FPLE-LDMTPFMAsskesrmngqyqQPLDSLNNDNKYSLFAVVNHQGT-LESGHYTSFIRQHK-DQWFKCDDAIITKASI 504
Cdd:cd02669 359 FPIKnLDLSDYVH------------FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKStNKWFEIQDLNVKEVLP 426
|
490
....*....|...
gi 110625685 505 KDVLDSEGYLLFY 517
Cdd:cd02669 427 QLIFLSESYIQIW 439
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
3.90e-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: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHR--CEMQSPSSCLVCEMSSLFQEFYSG-------HRSPHIPYKlLHL 247
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpSDVVDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQ-VGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 248 VWTHARHLAGY--------EQQDAHEFLIAALDVLHRHCKgddnGKKANNPNhcnciidQIFTGGLQSDVTCQVCHGVST 319
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESF----KNLGLNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 320 TIDPFWDISLDLPGSstpfwPLSPGSEGSVVNGEshasgtTTLTDCLRRFTRPEHLgssaKIKCSGCHSYQESTKQLTMK 399
Cdd:cd02658 149 TSELSEILSLPVPKD-----EATEKEEGELVYEP------VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 400 KLPIVACFHLKRFEHSA-KLRRKITTYVSFPLELDmtpfmasskesrmngqyqqpldslnnDNKYSLFAVVNHQGT-LES 477
Cdd:cd02658 214 TFPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG--------------------------PGKYELIAFISHKGTsVHS 267
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 110625685 478 GHYTSFIRQ---HKDQWFKCDDAIITKASIKDVLDSEGYLLFY 517
Cdd:cd02658 268 GHYVAHIKKeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
174-509 |
1.15e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 114.97 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 174 GLRGLINLGNTCFMNCIVQALTHTPLLRdfflSDRHRCEMQSPSSCLVCEMSsLFQEFYSGHRSPHiPYKLLHLV----W 249
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFR----KDVYGIPTDHPRGRDSVALA-LQRLFYNLQTGEE-PVDTTELTrsfgW 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 250 THARHlagYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNpnhcnciidqIFTGGLQSDVTCQVCHGVSTTIDPFWDISL 329
Cdd:COG5077 266 DSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENALNG----------IFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 330 DLPGSSTpfwplspgsegsvvngeshasgtttLTDCLRRFTRPEHLGSSAKIKCSGcHSYQESTKQLTMKKLPIVACFHL 409
Cdd:COG5077 333 NVKGMKN-------------------------LQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 410 KRFEHSAK--LRRKITTYVSFPLELDMTPFMasSKESrmngqyqqpLDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQH 487
Cdd:COG5077 387 KRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDA---------DKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPE 455
|
330 340
....*....|....*....|...
gi 110625685 488 KD-QWFKCDDAIITKASIKDVLD 509
Cdd:COG5077 456 KDgRWYKFDDTRVTRATEKEVLE 478
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
177-519 |
8.69e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.81 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALT-HTPLLRDffLSDRHRCEMQSpssclvcemsslFQEFYSGHRSP---HIPYKLLHLVWTHA 252
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDE--LLDDLSKELKV------------LKNVIRKPEPDlnqEEALKLFTALWSSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 253 RHLAG-----YEQQDAHEFLIAALDVLhrhckgddngkkaNNPNHcNCIIDQIF-TGGlqsdvtcqvcHGVSTTIDPFWD 326
Cdd:COG5533 67 EHKVGwippmGSQEDAHELLGKLLDEL-------------KLDLV-NSFTIRIFkTTK----------DKKKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 327 ISLDLPgsstpfwplspgsEGSVVNGEshasgtTTLTDCLRRFtrpEHLGSSAK-IKCS---GCHSYQESTKQLTMKKLP 402
Cdd:COG5533 123 IIIELP-------------DQTWVNNL------KTLQEFIDNM---EELVDDETgVKAKeneELEVQAKQEYEVSFVKLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 403 IVACFHLKRFEHSAKlRRKITTYVSFPLELDMTPfmASSKESRMNGQYQqpldslnndnkysLFAVVNHQGTLESGHYTS 482
Cdd:COG5533 181 KILTIQLKRFANLGG-NQKIDTEVDEKFELPVKH--DQILNIVKETYYD-------------LVGFVLHQGSLEGGHYIA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 110625685 483 FIRQhKDQWFKCDDAIITKASIKDVLDS---EGYLLFYHK 519
Cdd:COG5533 245 YVKK-GGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
1.13e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 105.53 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALthtpllrdfflsdrhrcemqspSSClvcemsslfqefysghrsphiPYKLLHLVWTharhla 256
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL----------------------ASL---------------------PSLIEYLEEF------ 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 257 gYEQQDAHEFLIAALDVLHRHCKgddngkkanNPnhcnciidqiFTGGLQSDVTCQVCHGVST-TIDPFWDISLDLPgss 335
Cdd:cd02662 32 -LEQQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 336 tpfwplspgsegsvvngESHASGTTTLTDCLRRFTRPEHLGSsakIKCSGChsyqestkQLTMKKLPIVACFHLKRFEHS 415
Cdd:cd02662 89 -----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 416 AK-LRRKITTYVSFPLELdmtpfmasskesrmngqyqqpldslnNDNKYSLFAVVNHQGTLESGHYTSFIRQH------- 487
Cdd:cd02662 141 GRgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdke 194
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110625685 488 --------------KDQWFKCDDAIITKASIKDVL-DSEGYLLFY 517
Cdd:cd02662 195 pgsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
1.90e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 106.81 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGhRSPHIPYKLLHLVWThARHLA 256
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQR-RAEAPPDYFLEASRP-PWFTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 257 GYeQQDAHEFLIAALDVLHrhckgddngkkannpnhcnCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPgsst 336
Cdd:cd02664 79 GS-QQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 337 pfwplspgsegsvvngeshasgttTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSA 416
Cdd:cd02664 135 ------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 417 K--LRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQP----LDSLNNDNKYSLFAVVNHQGT-LESGHYTSFIR---- 485
Cdd:cd02664 191 KthVREKIMDNVSINEVLSLPVRVESKSSESPLEKKEEEsgddGELVTRQVHYRLYAVVVHSGYsSESGHYFTYARdqtd 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 110625685 486 -----------------QHKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 517
Cdd:cd02664 271 adstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
1.37e-24 |
|
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: 103.95 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPLLRD---FFLSDRhRCEMQSPSScLVCEMSSLFQEFySGHRSPHIPYKLLHLVWTHAR 253
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPAR-RGANQSSDN-LTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 254 HLA------GYEQQDAHEFLIAALDVLHRHCKGDDNGKKAnnpnhcnciIDQIFTGGLQSDVTCQvchgvsttidpfwDI 327
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCT-------------ES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 328 SLDLPGSSTPFWPLSpgsegsvvngeSHASGTT---TLTDCLRrftrpEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIV 404
Cdd:cd02657 136 PDEEEVSTESEYKLQ-----------CHISITTevnYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 405 ACFHLKRF--EHSAKLRRKITTYVSFPLELDMTPFMASSkesrmngqyqqpldslnndNKYSLFAVVNHQG-TLESGHYT 481
Cdd:cd02657 200 LTVQFVRFfwKRDIQKKAKILRKVKFPFELDLYELCTPS-------------------GYYELVAVITHQGrSADSGHYV 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 110625685 482 SFIRQ-HKDQWFKCDDAIITKASIKDVLDSEG-------YLLFY 517
Cdd:cd02657 261 AWVRRkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
177-496 |
3.86e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 76.16 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQALTHTPLLRDFFLSdrHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHAR--- 253
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 254 -HLAGYEQQDAHEFLIAAL-DVLHR---HCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDIS 328
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 329 LDLPGSSTPfwplspgsegsvvngESHASGTTTLTDCLRRFTRPEhlgSSAKIKCSGCHSYQESTKQLTMKKLPIVACFH 408
Cdd:pfam13423 160 LIYPRKPSS---------------NNKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 409 LKRfeHSAKLRRKITTYVSFPLELDMTPfmasskesrmngqyQQPLDSLNNDNKYSLFAVVNH-QGTLESGHYTSFIR-- 485
Cdd:pfam13423 222 AAL--TNEEWRQLWKTPGWLPPEIGLTL--------------SDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVKva 285
|
330
....*....|....*..
gi 110625685 486 ------QHKDQWFKCDD 496
Cdd:pfam13423 286 dseledPTESQWYLFND 302
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
63-123 |
3.10e-12 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 61.51 E-value: 3.10e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625685 63 CHVCGIHLNrLHSCLYCVFFGCFTKK--HIHDHAKSKRHNLAIDLMYGGIYCFLCQDYIYDKD 123
Cdd:pfam02148 1 CSLCGNTSN-LWLCLTCGHVGCGRYQnsHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-517 |
8.77e-10 |
|
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: 60.20 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 177 GLINLGNTCFMNCIVQAL-THTPLlRDFFLS-DRHRCEMQSP-------------------SSCLVCEMSSLFQEF-YSG 234
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKPL-RDLVLNfDESKAELASDypterriggrevsrselqrSNQFVYELRSLFNDLiHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 235 HRSPHiPYKLLHLvwtharhlAGYEQQDAHEFLIAALDVLHRHCKGDDN---GKKANNPNHCNCIIDQIFTGGL-QSDVT 310
Cdd:cd02666 82 TRSVT-PSKELAY--------LALRQQDVTECIDNVLFQLEVALEPISNafaGPDTEDDKEQSDLIKRLFSGKTkQQLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 311 CQVCHGVSTTIDPFWDISLdlpgsstpfwPLSPGSEGSVVNGESHasgTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQ 390
Cdd:cd02666 153 ESMGNQPSVRTKTERFLSL----------LVDVGKKGREIVVLLE---PKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 391 -ESTKQLTMKK--LPIVAcfhlkrfEHSAKLRRKITTYVSFPLEldmtpfMASSKESRMNGQYQQPLDSLNNdNKYSLFA 467
Cdd:cd02666 220 pLQRELISMDRyeLPSSI-------DDIDELIREAIQSESSLVR------QAQNELAELKHEIEKQFDDLKS-YGYRLHA 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 110625685 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 ... |
260-517 |
2.60e-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: 54.84 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 260 QQDAHEFLIAALdvlhrHCKGDDNGKKANNPNHCNCIIDQI-----FTGGLQSDVTCQVCHGVSTTIDPFWDISLD---- 330
Cdd:cd02673 33 QQDAHEFLLTLL-----EAIDDIMQVNRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSFEENVSDVGNFLDVSmidn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 331 ----LPGSSTPFWPLSP-GSEGSVVNGESHASgtttltdCLRRFTRPEHLGSSAKikcsgCHSYQESTKQLTMKKLPIVA 405
Cdd:cd02673 108 kldiDELLISNFKTWSPiEKDCSSCKCESAIS-------SERIMTFPECLSINLK-----RYKLRIATSDYLKKNEEIMK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 406 CFHLKrfehsaklrrkittyvsfpleldmtpfmasskesrmngqyqqpldslnnDNKYSLFAVVNHQG-TLESGHYTSFI 484
Cdd:cd02673 176 KYCGT-------------------------------------------------DAKYSLVAVICHLGeSPYDGHYIAYT 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 110625685 485 RQ--HKDQWFKCDDAIITKASIKDVLD---SEGYLLFY 517
Cdd:cd02673 207 KElyNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
399-517 |
2.64e-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: 48.68 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 399 KKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPL-------DSLNNDNKYSLFAVVNH 471
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVcyddkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625685 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 ... |
400-517 |
3.01e-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: 45.24 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625685 400 KLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPfmasskesrmngqyqqpldslnndnkYSLFAVVNHQGTLESGH 479
Cdd:cd02665 127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQIIQQVP--------------------------YELHAVLVHEGQANAGH 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 110625685 480 YTSFI-RQHKDQWFKCDDAIITKASIKDVL-DSEG-------YLLFY 517
Cdd:cd02665 181 YWAYIyKQSRQEWEKYNDISVTESSWEEVErDSFGggrnpsaYCLMY 227
|
|
| |
