|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
102-534 |
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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 610.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 102 YLETIDRTRLDFDFENLCSVSLSNNNVYACLTCGKYFQGRGKTSHAYFHSIDQDHHVYINLQSLKIYILPNGYEVDDPSL 181
Cdd:cd02669 2 YLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 182 DDIKYVANPIYTKAQVANLDKLAESSYDLFHNAYRPGFIGMNNIKENDYANVVVQALAHTTPLRNFLMLENLSER----- 256
Cdd:cd02669 82 DDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENikdrk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 257 PELVKRLSLLVRKIWNRKAFKPHVSPHELLQQVSQMSNKRFSSTVQKDPFDFMNWLLNNTHLALGGSKtKPFTSIVQFTF 336
Cdd:cd02669 162 SELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSK-KPNSSIIHDCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 337 QGKVEIQTQKITARAVPGDR--LKFEADELIQSKEVPFMFLSLELPPVPLFKGDLERNAIPQVSLTSLLKKYDGNQTQEL 414
Cdd:cd02669 241 QGKVQIETQKIKPHAEEEGSkdKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGKTETEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 415 AGHRKRYKIKKLPNYLVFHIKRFDKTNLDDGKNPTVVSFDPRGLDMSPYVD----NASKPIYYDLVANIVIDvnstSQGA 490
Cdd:cd02669 321 KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHfdkpSLNLSTKYNLVANIVHE----GTPQ 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1851233218 491 EKHSWAIQLLDKATNTWVQIQDLIVKDVRSELLFLNESYIQVWE 534
Cdd:cd02669 397 EDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
220-533 |
2.73e-32 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 126.02 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 220 IGMNNIKENDYANVVVQALAHTTPLRNFL--MLENLSERPE-----LVKRLSLLVRKIWNRKAFKpHVSPHELLQQVSqM 292
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLlrISPLSEDSRYnkdinLLCALRDLFKALQKNSKSS-SVSPKMFKKSLG-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 293 SNKRFSSTVQKDPFDFMNWLLNNTHLALGGSKTKPFTSIVQFTFQGKVEiqtqkitaravpgDRLKFEADELIQSKEVPF 372
Cdd:pfam00443 79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLK-------------SRLKCLSCGEVSETFEPF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 373 MFLSLELPPVP-LFKGDLERNAIPQVSLTSLLKKYDGNQTQELAGHR---KRYKIKKLPNYLVFHIKRFDKTNLDDGKNP 448
Cdd:pfam00443 146 SDLSLPIPGDSaELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQdaiKQLKISRLPPVLIIHLKRFSYNRSTWEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 449 TVVSFdPRGLDMSPYVDNASKP-----IYYDLVAnIVIDVNSTSQGaekHSWAIqLLDKATNTWVQIQDLIVKDVRSELL 523
Cdd:pfam00443 226 TEVEF-PLELDLSRYLAEELKPktnnlQDYRLVA-VVVHSGSLSSG---HYIAY-IKAYENNRWYKFDDEKVTEVDEETA 299
|
330
....*....|.
gi 1851233218 524 FLNES-YIQVW 533
Cdd:pfam00443 300 VLSSSaYILFY 310
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
119-166 |
2.66e-14 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 67.01 E-value: 2.66e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1851233218 119 CSVSLSNNNVYACLTCGKYFQGRGKTSHAYFHSIDQDHHVYINLQSLK 166
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQR 49
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
102-534 |
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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 610.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 102 YLETIDRTRLDFDFENLCSVSLSNNNVYACLTCGKYFQGRGKTSHAYFHSIDQDHHVYINLQSLKIYILPNGYEVDDPSL 181
Cdd:cd02669 2 YLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 182 DDIKYVANPIYTKAQVANLDKLAESSYDLFHNAYRPGFIGMNNIKENDYANVVVQALAHTTPLRNFLMLENLSER----- 256
Cdd:cd02669 82 DDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENikdrk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 257 PELVKRLSLLVRKIWNRKAFKPHVSPHELLQQVSQMSNKRFSSTVQKDPFDFMNWLLNNTHLALGGSKtKPFTSIVQFTF 336
Cdd:cd02669 162 SELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSK-KPNSSIIHDCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 337 QGKVEIQTQKITARAVPGDR--LKFEADELIQSKEVPFMFLSLELPPVPLFKGDLERNAIPQVSLTSLLKKYDGNQTQEL 414
Cdd:cd02669 241 QGKVQIETQKIKPHAEEEGSkdKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGKTETEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 415 AGHRKRYKIKKLPNYLVFHIKRFDKTNLDDGKNPTVVSFDPRGLDMSPYVD----NASKPIYYDLVANIVIDvnstSQGA 490
Cdd:cd02669 321 KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHfdkpSLNLSTKYNLVANIVHE----GTPQ 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1851233218 491 EKHSWAIQLLDKATNTWVQIQDLIVKDVRSELLFLNESYIQVWE 534
Cdd:cd02669 397 EDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
220-533 |
2.73e-32 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 126.02 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 220 IGMNNIKENDYANVVVQALAHTTPLRNFL--MLENLSERPE-----LVKRLSLLVRKIWNRKAFKpHVSPHELLQQVSqM 292
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLlrISPLSEDSRYnkdinLLCALRDLFKALQKNSKSS-SVSPKMFKKSLG-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 293 SNKRFSSTVQKDPFDFMNWLLNNTHLALGGSKTKPFTSIVQFTFQGKVEiqtqkitaravpgDRLKFEADELIQSKEVPF 372
Cdd:pfam00443 79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLK-------------SRLKCLSCGEVSETFEPF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 373 MFLSLELPPVP-LFKGDLERNAIPQVSLTSLLKKYDGNQTQELAGHR---KRYKIKKLPNYLVFHIKRFDKTNLDDGKNP 448
Cdd:pfam00443 146 SDLSLPIPGDSaELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQdaiKQLKISRLPPVLIIHLKRFSYNRSTWEKLN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 449 TVVSFdPRGLDMSPYVDNASKP-----IYYDLVAnIVIDVNSTSQGaekHSWAIqLLDKATNTWVQIQDLIVKDVRSELL 523
Cdd:pfam00443 226 TEVEF-PLELDLSRYLAEELKPktnnlQDYRLVA-VVVHSGSLSSG---HYIAY-IKAYENNRWYKFDDEKVTEVDEETA 299
|
330
....*....|.
gi 1851233218 524 FLNES-YIQVW 533
Cdd:pfam00443 300 VLSSSaYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
299-534 |
5.82e-29 |
|
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: 115.27 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 299 STVQKDPFDFMNWLLNNTHLALGGSK-----TKPFTSIVQFTFQGKVEIQTQKITARAVpgdrlkfeadeliQSKEVPFM 373
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdSSSLKSLIHDLFGGKLESTIVCLECGHE-------------SVSTEPEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 374 FLSLELPPVPlfkgdlernaIPQVSLTSLLKKYDGNQTQE-----------LAGHRKRYKIKKLPNYLVFHIKRFDKTNL 442
Cdd:cd02257 86 FLSLPLPVKG----------LPQVSLEDCLEKFFKEEILEgdncykcekkkKQEATKRLKIKKLPPVLIIHLKRFSFNED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 443 DDG-KNPTVVSFdPRGLDMSPYV-------DNASKPIYYDLVANIVIDVNSTSQGaekHSWAiQLLDKATNTWVQIQDLI 514
Cdd:cd02257 156 GTKeKLNTKVSF-PLELDLSPYLsegekdsDSDNGSYKYELVAVVVHSGTSADSG---HYVA-YVKDPSDGKWYKFNDDK 230
|
250 260
....*....|....*....|....*
gi 1851233218 515 VKDVRSELLFL-----NESYIQVWE 534
Cdd:cd02257 231 VTEVSEEEVLEfgslsSSAYILFYE 255
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
119-181 |
3.37e-21 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 86.93 E-value: 3.37e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851233218 119 CSVSLSNNNVYACLTCGKYFQGRGKTSHAYFHSIDQDHHVYINLQSLKIYILPNGYEVDDPSL 181
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
302-530 |
1.49e-15 |
|
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: 76.17 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 302 QKDPFDFMNWLLNNTHlalggsktkpftSIVQFTFQG----KVEIQTQKITARavpgdrlKFEadeliqskevPFMFLSL 377
Cdd:cd02674 22 QQDAQEFLLFLLDGLH------------SIIVDLFQGqlksRLTCLTCGKTST-------TFE----------PFTYLSL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 378 ELPpvplfkgdLERNAIPQVSLTSLLKKYdgNQTQELAGH--------------RKRYKIKKLPNYLVFHIKRFDKTNLD 443
Cdd:cd02674 73 PIP--------SGSGDAPKVTLEDCLRLF--TKEETLDGDnawkcpkckkkrkaTKKLTISRLPKVLIIHLKRFSFSRGS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 444 DGKNPTVVSFDPRGLDMSPYVDNASK--PIYYDLVAnIVIDVNSTSQGaekH--SWAiqlLDKATNTWVQIQDLIVKDVR 519
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVDTRSFtgPFKYDLYA-VVNHYGSLNGG---HytAYC---KNNETNDWYKFDDSRVTKVS 215
|
250
....*....|.
gi 1851233218 520 SELLFLNESYI 530
Cdd:cd02674 216 ESSVVSSSAYI 226
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
221-524 |
2.13e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 74.33 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 221 GMNNIKENDYANVVVQALAHTTPLRNFlMLENLSERPELVKR----LSLLVRKIWNRKAFKPHVSPHELLQQVSQM--SN 294
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNY-FLSDRHSCTCLSCSpnscLSCAMDEIFQEFYYSGDRSPYGPINLLYLSwkHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 295 KRFSSTVQKDPFDFMNWLLNNTHLALGGSKTKPFTS-----IVQFTFQGKVEIQTQKITARAVpgdrlkfeadeliqSKE 369
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDEshcncIIHQTFSGSLQSSVTCQRCGGV--------------STT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 370 V-PFMFLSLELPPVPLFKGDLERN-AIPQVSLTSLLKKYDG--------------NQTQELaghRKRYKIKKLPNYLVFH 433
Cdd:cd02660 147 VdPFLDLSLDIPNKSTPSWALGESgVSGTPTLSDCLDRFTRpeklgdfaykcsgcGSTQEA---TKQLSIKKLPPVLCFQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 434 IKRFDKTNLD-DGKNPTVVSFdPRGLDMSPYVDNASKP----------IYYDLVAnIVIDVNSTSQGaekHSWAI----- 497
Cdd:cd02660 224 LKRFEHSLNKtSRKIDTYVQF-PLELNMTPYTSSSIGDtqdsnsldpdYTYDLFA-VVVHKGTLDTG---HYTAYcrqgd 298
|
330 340 350
....*....|....*....|....*....|
gi 1851233218 498 ---QLLDKATNTWVQIQDliVKDVRSELLF 524
Cdd:cd02660 299 gqwFKFDDAMITRVSEEE--VLKSQAYLLF 326
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
119-166 |
2.66e-14 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 67.01 E-value: 2.66e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1851233218 119 CSVSLSNNNVYACLTCGKYFQGRGKTSHAYFHSIDQDHHVYINLQSLK 166
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQR 49
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
221-530 |
2.01e-12 |
|
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: 68.07 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 221 GMNNIKENDYANVVVQALAHTTPLRNFLMLENLS-----ERPELVKRLSLLV-RKIWN-RKAFKPHVSPHELLQQVSQMS 293
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSkdccnEGFCMMCALEAHVeRALASsGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 294 NKRfsstvQKDPFDFMNWLLNNTHLA----LGGSKTKPF----TSIVQFTFQGKVEIQTQKITARAVPGdrlKFEadeli 365
Cdd:cd02661 83 IGR-----QEDAHEFLRYLLDAMQKAcldrFKKLKAVDPssqeTTLVQQIFGGYLRSQVKCLNCKHVSN---TYD----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 366 qskevPFMFLSLELPPVPlfkgdlernaipqvSLTSLLKKY------DGNQTQ------ELAGHRKRYKIKKLPNYLVFH 433
Cdd:cd02661 150 -----PFLDLSLDIKGAD--------------SLEDALEQFtkpeqlDGENKYkcerckKKVKASKQLTIHRAPNVLTIH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 434 IKRFdkTNLDDGKNPTVVSFDPRgLDMSPYV-DNASKPIYYDLVANIVIDVNSTSQGaekHSWAIqlLDKATNTWVQIQD 512
Cdd:cd02661 211 LKRF--SNFRGGKINKQISFPET-LDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSG---HYYCY--VKSSNGKWYNMDD 282
|
330
....*....|....*...
gi 1851233218 513 LIVKDVRSELLFLNESYI 530
Cdd:cd02661 283 SKVSPVSIETVLSQKAYI 300
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
221-480 |
9.63e-11 |
|
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: 63.10 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 221 GMNNIKENDYANVVVQALAHTTplrnflmlenlserpeLVKRLSLLVRKIWNRKAFKPHVSPHELLQQVSQmSNKRFSST 300
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRTGVISPKKFITRLKR-ENELFDNY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 301 VQKDPFDFMNWLLNN--------------THLALGGSKTKPFTSIVQFTFQGKVEIQTQKITAravpgdrlkfeadELIQ 366
Cdd:cd02663 64 MHQDAHEFLNFLLNEiaeildaerkaekaNRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTC-------------ETVS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 367 SKEVPFMFLSLelppvplfkgDLERNaipqVSLTSLLKKYdgNQTQELAGH--------------RKRYKIKKLPNYLVF 432
Cdd:cd02663 131 SRDETFLDLSI----------DVEQN----TSITSCLRQF--SATETLCGRnkfycdeccslqeaEKRMKIKKLPKILAL 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1851233218 433 HIKRFdKTNLDDGKNPTV---VSFdPRGLDMSPYVDNASKP-IYYDLVANIV 480
Cdd:cd02663 195 HLKRF-KYDEQLNRYIKLfyrVVF-PLELRLFNTTDDAENPdRLYELVAVVV 244
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
218-465 |
9.85e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 44.56 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 218 GFIGMNNIKENDYANVVVQALAHTTPLRN--FLMLENLSERPELVKRLSLLVRKIWNRKAFKPhVSPHELLQQVSQMSNK 295
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLALQRLFLFLQLSESP-VKTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 296 RFSSTVQKDPFDFMNWLLNNTHLALGGSKTKPftsIVQFTFQGKVEIQtqkitaravpgdrlkfeadelIQSKEVP---- 371
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEG---LIKNLFGGKLVNY---------------------IICKECPhese 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 372 ----FMFLSLELPPvplfKGDLERnaipqvSLTSLLKK--YDGNQTQELAGH------RKRYKIKKLPNYLVFHIKRF-- 437
Cdd:cd02659 136 reeyFLDLQVAVKG----KKNLEE------SLDAYVQGetLEGDNKYFCEKCgkkvdaEKGVCFKKLPPVLTLQLKRFef 205
|
250 260
....*....|....*....|....*...
gi 1851233218 438 DKTNLDDGKNPTVVSFdPRGLDMSPYVD 465
Cdd:cd02659 206 DFETMMRIKINDRFEF-PLELDMEPYTE 232
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
370-534 |
1.56e-04 |
|
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: 43.53 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 370 VPFMFLSLELPPVPLfkgdlernAIPQVSLTSLLKKYDGNQTQELAG---------HRKRYKIKKLPNYLVFHIKRFDKT 440
Cdd:cd02667 92 VYEPFLDLSLPRSDE--------IKSECSIESCLKQFTEVEILEGNNkfacenctkAKKQYLISKLPPVLVIHLKRFQQP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 441 NLDDG-KNPTVVSFdPRGLDMSPYVD------NASKPIYYDLVANIV-------------IDVNSTSQGAEKHSWAIQLL 500
Cdd:cd02667 164 RSANLrKVSRHVSF-PEILDLAPFCDpkcnssEDKSSVLYRLYGVVEhsgtmrsghyvayVKVRPPQQRLSDLTKSKPAA 242
|
170 180 190
....*....|....*....|....*....|....*..
gi 1851233218 501 DKATN---TWVQIQDLIVKDVRSELLFLNESYIQVWE 534
Cdd:cd02667 243 DEAGPgsgQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
221-479 |
3.61e-04 |
|
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: 42.70 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 221 GMNNIKENDYANVVVQALAhTTP--LRNFLMLENLSERP----------ELVK--------RLSLLVRKIWNRKAFKPHV 280
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLF-SIPsfQWRYDDLENKFPSDvvdpandlncQLIKladgllsgRYSKPASLKSENDPYQVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 281 SPHELLQQVSQmSNKRFSSTVQKDPFDFMNWLLNNTHLALGGSKTKPFTSIVQFTFQGKVEIQTQKitaravpgdRLKFe 360
Cdd:cd02658 80 KPSMFKALIGK-GHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMIEDRLECLSCK---------KVKY- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233218 361 ADELIqskevpfMFLSLELPPVPLFKGDLERNAIPQVSLTSLLKKYDGNQT--------QELAGHRKRYKIKKLPNYLVF 432
Cdd:cd02658 149 TSELS-------EILSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETiedfcstcKEKTTATKTTGFKTFPDYLVI 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1851233218 433 HIKRFDktnlddgknpTVVSFDPRGLDMSPYVDNASKPIYYDLVANI 479
Cdd:cd02658 222 NMKRFQ----------LLENWVPKKLDVPIDVPEELGPGKYELIAFI 258
|
|
| |
