|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-488 |
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: 681.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 39 PYLDTINRNLLDFDFEKLCSISLTRINVYACLVCGKYFQGRGTNTHAYTHSVGEAHHVFLNLHTLRFYCLPDNYEIIDSS 118
Cdd:cd02669 1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 119 LDDIKYVLNPTFTRQEISKLDQlQPKHSRTVDGVLYLPGVVGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVR 198
Cdd:cd02669 81 LDDIKYVLNPTYTKEQISDLDR-DPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 199 PPGdsvfTLVQRFGELMRKMWNPRNFKSHVSPHEMLQAVVLWSSKRFQITEQGDPIDFLSWFLNTLHRALKGNKHPNSSI 278
Cdd:cd02669 160 RKS----ELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 279 LYKIFLGEMKIYTRKMPPVELDDAAKaQLLATEEYKDQVEDKNFIYLTCDLPPPPLFTDEFRENIIPQVNLYQLLSKFNG 358
Cdd:cd02669 236 IHDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 359 TAEKEYKTYkanfMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPIKHVDFGDILGMRQRDKDVKdTKYNLVANI 438
Cdd:cd02669 315 KTETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLS-TKYNLVANI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 18859907 439 VHDGDP-KKGTYRAHILHKANGQWYEMQDLHVTEILPQMITLTESYIQIYE 488
Cdd:cd02669 390 VHEGTPqEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
159-487 |
8.37e-47 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 164.92 E-value: 8.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 159 VGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVRPPGDSvfTLVQRFGELMRKMWnPRNFKSHVSPHeMLQAVV 238
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI--NLLCALRDLFKALQ-KNSKSSSVSPK-MFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 239 LWSSKRFQITEQGDPIDFLSWFLNTLHRALKGNKH-PNSSILYKIFLGEMKiytrkmppvelddaakaQLLATEEYKDQV 317
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHStENESLITDLFRGQLK-----------------SRLKCLSCGEVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 318 EDKNFIYLTCDLPPPPLFTDEFRENIIPQVNLYQLLSKFNGTAEKEYKTY-KANFMKRFEITRLPQFIILYIKRFTKNTF 396
Cdd:pfam00443 140 ETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGcKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 397 FLEKNPTIVNFPIKhVDFGDILGMRQRDKDVKDTKYNLVANIVHDGDPKKGTYRAHILHKANGQWYEMQDLHVTEILPQM 476
Cdd:pfam00443 220 TWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET 298
|
330
....*....|..
gi 18859907 477 ITLTES-YIQIY 487
Cdd:pfam00443 299 AVLSSSaYILFY 310
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
57-105 |
9.69e-13 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 62.77 E-value: 9.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 18859907 57 CSISLTRINVYACLVCGKYFQGRGTNTHAYTHSVGEAHHVFLNLHTLRF 105
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
371-490 |
6.92e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 67.99 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 371 FMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPIKHVDFGDILGMrqrdKDVKDTKYNLVANIVHDGDPKKGTYR 450
Cdd:COG5560 707 ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYM----VDDPRLIYDLYAVDNHYGGLSGGHYT 782
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18859907 451 AHILHKANGQWYEMQDLHVTEILPQMITLTESYIQIYERC 490
Cdd:COG5560 783 AYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-488 |
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: 681.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 39 PYLDTINRNLLDFDFEKLCSISLTRINVYACLVCGKYFQGRGTNTHAYTHSVGEAHHVFLNLHTLRFYCLPDNYEIIDSS 118
Cdd:cd02669 1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 119 LDDIKYVLNPTFTRQEISKLDQlQPKHSRTVDGVLYLPGVVGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVR 198
Cdd:cd02669 81 LDDIKYVLNPTYTKEQISDLDR-DPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 199 PPGdsvfTLVQRFGELMRKMWNPRNFKSHVSPHEMLQAVVLWSSKRFQITEQGDPIDFLSWFLNTLHRALKGNKHPNSSI 278
Cdd:cd02669 160 RKS----ELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 279 LYKIFLGEMKIYTRKMPPVELDDAAKaQLLATEEYKDQVEDKNFIYLTCDLPPPPLFTDEFRENIIPQVNLYQLLSKFNG 358
Cdd:cd02669 236 IHDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 359 TAEKEYKTYkanfMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPIKHVDFGDILGMRQRDKDVKdTKYNLVANI 438
Cdd:cd02669 315 KTETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLS-TKYNLVANI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 18859907 439 VHDGDP-KKGTYRAHILHKANGQWYEMQDLHVTEILPQMITLTESYIQIYE 488
Cdd:cd02669 390 VHEGTPqEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
159-487 |
8.37e-47 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 164.92 E-value: 8.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 159 VGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVRPPGDSvfTLVQRFGELMRKMWnPRNFKSHVSPHeMLQAVV 238
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI--NLLCALRDLFKALQ-KNSKSSSVSPK-MFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 239 LWSSKRFQITEQGDPIDFLSWFLNTLHRALKGNKH-PNSSILYKIFLGEMKiytrkmppvelddaakaQLLATEEYKDQV 317
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHStENESLITDLFRGQLK-----------------SRLKCLSCGEVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 318 EDKNFIYLTCDLPPPPLFTDEFRENIIPQVNLYQLLSKFNGTAEKEYKTY-KANFMKRFEITRLPQFIILYIKRFTKNTF 396
Cdd:pfam00443 140 ETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGcKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 397 FLEKNPTIVNFPIKhVDFGDILGMRQRDKDVKDTKYNLVANIVHDGDPKKGTYRAHILHKANGQWYEMQDLHVTEILPQM 476
Cdd:pfam00443 220 TWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET 298
|
330
....*....|..
gi 18859907 477 ITLTES-YIQIY 487
Cdd:pfam00443 299 AVLSSSaYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
249-488 |
1.12e-34 |
|
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: 130.68 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 249 EQGDPIDFLSWFLNTLHRALKGNK------HPNSSILYKIFLGEMKIYTRKmppvelddaakaqllaTEEYKDQVEDKNF 322
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKSSkrtsdsSSLKSLIHDLFGGKLESTIVC----------------LECGHESVSTEPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 323 IYLTCDLPPPPlftdefreniIPQVNLYQLLSKFNGT-------AEKEYKTYKANFMKRFEITRLPQFIILYIKRFTKN- 394
Cdd:cd02257 85 LFLSLPLPVKG----------LPQVSLEDCLEKFFKEeilegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 395 TFFLEKNPTIVNFPIKHVDFGDIL-GMRQRDKDVKDTKYNLVANIVHDGD-PKKGTYRAHILHKANGQWYEMQDLHVTEI 472
Cdd:cd02257 155 DGTKEKLNTKVSFPLELDLSPYLSeGEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEV 234
|
250 260
....*....|....*....|.
gi 18859907 473 LPQMITL-----TESYIQIYE 488
Cdd:cd02257 235 SEEEVLEfgslsSSAYILFYE 255
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
57-119 |
3.89e-22 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 89.63 E-value: 3.89e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18859907 57 CSISLTRINVYACLVCGKYFQGRGTNTHAYTHSVGEAHHVFLNLHTLRFYCLPDNYEIIDSSL 119
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
368-488 |
2.27e-13 |
|
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: 69.62 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 368 KANFMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPIKHVDFGDILGMRQrdkDVKDTKYNLVANIVHDGDPKKG 447
Cdd:cd02674 113 KRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRS---FTGPFKYDLYAVVNHYGSLNGG 189
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18859907 448 TYRAHILHKANGQWYEMQDLHVTEILPQMITLTESYIQIYE 488
Cdd:cd02674 190 HYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
57-105 |
9.69e-13 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 62.77 E-value: 9.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 18859907 57 CSISLTRINVYACLVCGKYFQGRGTNTHAYTHSVGEAHHVFLNLHTLRF 105
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
371-490 |
6.92e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 67.99 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 371 FMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPIKHVDFGDILGMrqrdKDVKDTKYNLVANIVHDGDPKKGTYR 450
Cdd:COG5560 707 ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYM----VDDPRLIYDLYAVDNHYGGLSGGHYT 782
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18859907 451 AHILHKANGQWYEMQDLHVTEILPQMITLTESYIQIYERC 490
Cdd:COG5560 783 AYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-472 |
2.99e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 64.70 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 160 GLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVRPPGDSVFTLVqrfgelMRKMWNPRNFKSHVSPHEMLQAVVL 239
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCA------MDEIFQEFYYSGDRSPYGPINLLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 240 W--SSKRFQITEQGDPIDFLSWFLNTLHRALKGNKHPNSS------ILYKIFLGEMkiytrkmppvelddaaKAQLLATE 311
Cdd:cd02660 76 SwkHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDeshcncIIHQTFSGSL----------------QSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 312 EYKDQVEDKNFIYLTCDLPPPPLFTDEFRENIIP-QVNLYQLLSKFNGTAEKEYKTYK-------ANFMKRFEITRLPQF 383
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSgTPTLSDCLDRFTRPEKLGDFAYKcsgcgstQEATKQLSIKKLPPV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 384 IILYIKRFtkntfflEKNPTIVNFPI-KHVDFGDILGMRQ-----------RDKDVKDTKYNLVANIVHDGDPKKGTYRA 451
Cdd:cd02660 220 LCFQLKRF-------EHSLNKTSRKIdTYVQFPLELNMTPytsssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTA 292
|
330 340
....*....|....*....|.
gi 18859907 452 HILHKaNGQWYEMQDLHVTEI 472
Cdd:cd02660 293 YCRQG-DGQWFKFDDAMITRV 312
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
157-472 |
3.47e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 64.59 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 157 GVVGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVvrPPGDSVFTLVQR-FGELmrkmwnprnfksHVSPHEMLQ 235
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDD--DDNKSVPLALQRlFLFL------------QLSESPVKT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 236 AVVLWSSKRF-----QITEQGDPIDFLSWFLNTLHRALKGNKHPNssILYKIFLGEMK----------IYTRKmppveld 300
Cdd:cd02659 67 TELTDKTRSFgwdslNTFEQHDVQEFFRVLFDKLEEKLKGTGQEG--LIKNLFGGKLVnyiickecphESERE------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 301 daakaqllatEEYKD-QVEDKNFIYLTcdlpppplftDEFRENIIPQV----NLYqllskfngTAEKEYKTYKANfmKRF 375
Cdd:cd02659 138 ----------EYFLDlQVAVKGKKNLE----------ESLDAYVQGETlegdNKY--------FCEKCGKKVDAE--KGV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 376 EITRLPQFIILYIKRFTkntFFLEKNPTI-VN----FPIK------HVDFGDILGMRQRDKDVKDTKYNLVANIVHDGDP 444
Cdd:cd02659 188 CFKKLPPVLTLQLKRFE---FDFETMMRIkINdrfeFPLEldmepyTEKGLAKKEGDSEKKDSESYIYELHGVLVHSGDA 264
|
330 340
....*....|....*....|....*...
gi 18859907 445 KKGTYRAHILHKANGQWYEMQDLHVTEI 472
Cdd:cd02659 265 HGGHYYSYIKDRDDGKWYKFNDDVVTPF 292
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-487 |
4.46e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 57.67 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 160 GLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVRPPGDSVFTL---VQRFGELMRKMWNPRNFKSHVSphemlqa 236
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALeahVERALASSGPGSAPRIFSSNLK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 237 vvlWSSKRFQITEQGDPIDFLSWFLNTLHRA----LKGNKHPN-----SSILYKIFLGEMKiytrkmppvelddaakAQL 307
Cdd:cd02661 76 ---QISKHFRIGRQEDAHEFLRYLLDAMQKAcldrFKKLKAVDpssqeTTLVQQIFGGYLR----------------SQV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 308 LATEEYKdqVEDK--NFIYLTCDlpppplftdefreniIPQVN-LYQLLSKFngTAEKE------YKTYKANFM----KR 374
Cdd:cd02661 137 KCLNCKH--VSNTydPFLDLSLD---------------IKGADsLEDALEQF--TKPEQldgenkYKCERCKKKvkasKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 375 FEITRLPQFIILYIKRFTKNTFflEKnptivnfPIKHVDFGDILGMRQRDKDVKD--TKYNLVANIVHDG-DPKKGTYRA 451
Cdd:cd02661 198 LTIHRAPNVLTIHLKRFSNFRG--GK-------INKQISFPETLDLSPYMSQPNDgpLKYKLYAVLVHSGfSPHSGHYYC 268
|
330 340 350
....*....|....*....|....*....|....*.
gi 18859907 452 HIlHKANGQWYEMQDLHVTEILPQMITLTESYIQIY 487
Cdd:cd02661 269 YV-KSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
157-471 |
1.49e-06 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 51.02 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 157 GVVGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHvvrPPGDSVFTLVQRFGELMRKMWNPrnfkshVSPHEMLQA 236
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHP---RGRDSVALALQRLFYNLQTGEEP------VDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 237 VVlWSSkrFQITEQGDPIDFLSWFLNTLHRALKGNKHPNSsiLYKIFLGEMKIYtrkmppVELDDAAKAQLLATEEYKDQ 316
Cdd:COG5077 263 FG-WDS--DDSFMQHDIQEFNRVLQDNLEKSMRGTVVENA--LNGIFVGKMKSY------IKCVNVNYESARVEDFWDIQ 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 317 VEDKNFIYLTcdlpppplftDEFRENIipQVnlyQLLSKFNGTAEKEYKTYKANFMKRFEitRLPQFIILYIKRFtkNTF 396
Cdd:COG5077 332 LNVKGMKNLQ----------ESFRRYI--QV---ETLDGDNRYNAEKHGLQDAKKGVIFE--SLPPVLHLQLKRF--EYD 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859907 397 FLEKNPTIVN----FPIKhVDFGDILGMRQRDKDVKDTKYNLVANIVHDGDPKKGTYRAHILHKANGQWYEMQDLHVTE 471
Cdd:COG5077 393 FERDMMVKINdryeFPLE-IDLLPFLDRDADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTR 470
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-472 |
2.69e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 49.34 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 160 GLNNIKANDYCNVVLHALSHVGPLRDYFLQ---KQSYAHVVRPPGD--SVFTLVQRFGELMRKMWNPRnfKSHVSPHEML 234
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsTEDAELKNMPPDKphEPQTIIDQLQLIFAQLQFGN--RSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 235 QAVvlwsskRFQITEQGDPIDFLSWFLNTLHRALKGNKHPN-SSILYKIFLGEMkIYT-------RKMPPVELDDAAKAQ 306
Cdd:cd02668 79 KAL------GLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDlKNIVQDLFRGEY-SYVtqcskcgRESSLPSKFYELELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 307 LLATEEYKDQVEDknfiYLTcdlppPPLFTDEfreniipqvNLY---QLLSKFNGTaekeyktykanfmKRFEITRLPQF 383
Cdd:cd02668 152 LKGHKTLEECIDE----FLK-----EEQLTGD---------NQYfceSCNSKTDAT-------------RRIRLTTLPPT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 384 IILYIKRFTKNTFFLEKNPtiVNFPIkhvDFGDILGMRQR--DKDVKDTKYNLVANIVHDG-DPKKGTYRAHILHKANGQ 460
Cdd:cd02668 201 LNFQLLRFVFDRKTGAKKK--LNASI---SFPEILDMGEYlaESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGE 275
|
330
....*....|..
gi 18859907 461 WYEMQDLHVTEI 472
Cdd:cd02668 276 WYKFNDEDVEEM 287
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
346-471 |
9.55e-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: 43.70 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 346 QVNLYQLL------SKFNGTAEKEYKTYKANFMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPikhvdfgdilg 419
Cdd:cd02665 88 QVNGYGNLhecleaAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKLEFP----------- 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18859907 420 mrqrdKDVKDTKYNLVANIVHDGDPKKGTYRAHILHKANGQWYEMQDLHVTE 471
Cdd:cd02665 157 -----QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTE 203
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-488 |
8.32e-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 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: 41.55 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 160 GLNNIKANDYCNVVLHALSHVGPLRDYFLQkqsYAHVVRPPGDSVFTLVQRFGELMRKMwnpRNFKSHVSPHEMLQAVvL 239
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN---YNPARRGANQSSDNLTNALRDLFDTM---DKKQEPVPPIEFLQLL-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 240 WSSKRF-QITEQG-----DPIDFLSWFLNTLHRALKGNKHPNSSIlYKIFLGEMKIytrKMPPVELDDaakaqllateEY 313
Cdd:cd02657 74 MAFPQFaEKQNQGgyaqqDAEECWSQLLSVLSQKLPGAGSKGSFI-DQLFGIELET---KMKCTESPD----------EE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 314 KDQVEDKNFIYLTCDLPPPPLFTDEfreniipqvnlyQLLSKFNGTAEKEYKTYKAN--FMKRFEITRLPQFIILYIKRF 391
Cdd:cd02657 140 EVSTESEYKLQCHISITTEVNYLQD------------GLKKGLEEEIEKHSPTLGRDaiYTKTSRISRLPKYLTVQFVRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 392 ------TKNTFFLEKnptiVNFPIKhVDFGDILGMrqrdkdvkDTKYNLVANIVHDG-DPKKGTYRAHILHKANGQWYEM 464
Cdd:cd02657 208 fwkrdiQKKAKILRK----VKFPFE-LDLYELCTP--------SGYYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKF 274
|
330 340 350
....*....|....*....|....*....|.
gi 18859907 465 QDLHVTEILPQMITLTE-------SYIQIYE 488
Cdd:cd02657 275 DDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
131-268 |
2.00e-03 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 41.02 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859907 131 TRQEISKLDQLQPKHSRTVDgvlYLPGVVGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVRPPGDSVFTLVQR 210
Cdd:COG5560 241 TRNPDWLVDSIVDDHNRSIN---KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVAS 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18859907 211 -FGELMRKMWNPRNfksHVSPHEMLQAVVLWSSKRFQITEQGDPIDFLSWFLNTLHRAL 268
Cdd:COG5560 318 aYADLIKQLYDGNL---HAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDL 373
|
|
| |
