|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
105-552 |
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: 718.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 105 PYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSS 184
Cdd:cd02669 1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 185 LEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKrp 264
Cdd:cd02669 81 LDDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIK-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 265 pgDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIV 344
Cdd:cd02669 159 --DRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 345 NDVFQGSMRIFTKKLPHPDLPAEEKeQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGI 424
Cdd:cd02669 237 HDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 425 TEKEYKTYkenfLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVH 504
Cdd:cd02669 316 TETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 20070404 505 DGKPSE-GSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWK 552
Cdd:cd02669 392 EGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
224-551 |
1.09e-51 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 179.18 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 224 VGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLvqRFGELMRKLWnPRNFKAHVSPHeMLQAVV 303
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLC--ALRDLFKALQ-KNSKSSSVSPK-MFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 304 LCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKT-IVNDVFQGSMRIFTKKLphpdlpaeekeqllhNDEYQETm 382
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENEsLITDLFRGQLKSRLKCL---------------SCGEVSE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 383 VESTFMYLTLDLPTAPlYKDEKEQLIIPQVPLFNILAKFNGITEKEYKTY-KENFLKRFQLTKLPPYLIFCIKRFTKNNF 461
Cdd:pfam00443 141 TFEPFSDLSLPIPGDS-AELKTASLQICFLQFSKLEELDDEEKYYCDKCGcKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 462 FVEKNPTIVNFPITnVDLREYLSEEVQAVHKN-TTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQM 540
Cdd:pfam00443 220 TWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET 298
|
330
....*....|..
gi 20070404 541 ITLSE-AYIQIW 551
Cdd:pfam00443 299 AVLSSsAYILFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
367-554 |
3.21e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 72.61 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 367 EEKEQLLHND------EYQETMVESTFMYltldlptAPLYKDEKEQLIIPQVPLFNILAKFN-----GITEKEY-KTYKE 434
Cdd:COG5560 631 EEEGQMNFNDavviscEWEEKRYLSLFSY-------DPLWTIREIGAAERTITLQDCLNEFSkpeqlGLSDSWYcPGCKE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 435 N--FLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYlseEVQAVHKNTTYDLIANIVHDGKPSEGS 512
Cdd:COG5560 704 FrqASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGV---EYMVDDPRLIYDLYAVDNHYGGLSGGH 780
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 20070404 513 YRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWKRR 554
Cdd:COG5560 781 YTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
123-171 |
9.98e-12 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 59.69 E-value: 9.98e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 20070404 123 CSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKF 171
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
105-552 |
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: 718.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 105 PYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSS 184
Cdd:cd02669 1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 185 LEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKrp 264
Cdd:cd02669 81 LDDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIK-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 265 pgDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIV 344
Cdd:cd02669 159 --DRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 345 NDVFQGSMRIFTKKLPHPDLPAEEKeQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGI 424
Cdd:cd02669 237 HDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 425 TEKEYKTYkenfLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVH 504
Cdd:cd02669 316 TETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 20070404 505 DGKPSE-GSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWK 552
Cdd:cd02669 392 EGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
224-551 |
1.09e-51 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 179.18 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 224 VGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLvqRFGELMRKLWnPRNFKAHVSPHeMLQAVV 303
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLC--ALRDLFKALQ-KNSKSSSVSPK-MFKKSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 304 LCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKT-IVNDVFQGSMRIFTKKLphpdlpaeekeqllhNDEYQETm 382
Cdd:pfam00443 77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENEsLITDLFRGQLKSRLKCL---------------SCGEVSE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 383 VESTFMYLTLDLPTAPlYKDEKEQLIIPQVPLFNILAKFNGITEKEYKTY-KENFLKRFQLTKLPPYLIFCIKRFTKNNF 461
Cdd:pfam00443 141 TFEPFSDLSLPIPGDS-AELKTASLQICFLQFSKLEELDDEEKYYCDKCGcKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 462 FVEKNPTIVNFPITnVDLREYLSEEVQAVHKN-TTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQM 540
Cdd:pfam00443 220 TWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET 298
|
330
....*....|..
gi 20070404 541 ITLSE-AYIQIW 551
Cdd:pfam00443 299 AVLSSsAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
225-552 |
3.74e-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: 129.91 E-value: 3.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNvpplrnyfleednyknikrppgdimfllvqrfgelmrklwnprnfkahvsphemlqavvl 304
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 305 cskktfqitKQGDGVDFLSWFLNALHSALGGTKKKKKT------IVNDVFQGSMRIFTKKLphpdlpaeekeqllhnDEY 378
Cdd:cd02257 21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRTSDssslksLIHDLFGGKLESTIVCL----------------ECG 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 379 QETMVESTFMYLTLDLPTAPlykdekeqliIPQVPLFNILAKFNG--ITEKEYKTY-----KENFLKRFQLTKLPPYLIF 451
Cdd:cd02257 76 HESVSTEPELFLSLPLPVKG----------LPQVSLEDCLEKFFKeeILEGDNCYKcekkkKQEATKRLKIKKLPPVLII 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 452 CIKRFTKNN-FFVEKNPTIVNFPITNVDLREYLSEEVQAV--HKNTTYDLIANIVHDGK-PSEGSYRIHVLHHGTGKWYE 527
Cdd:cd02257 146 HLKRFSFNEdGTKEKLNTKVSFPLELDLSPYLSEGEKDSDsdNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYK 225
|
330 340 350
....*....|....*....|....*....|
gi 20070404 528 LQDLQVTDILPQMITL-----SEAYIQIWK 552
Cdd:cd02257 226 FNDDKVTEVSEEEVLEfgslsSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
314-548 |
4.63e-23 |
|
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: 97.74 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 314 KQGDGVDFLSWFLNALHSalggtkkkkktIVNDVFQGSMRIFTKKLphpdlpaeekeqllhNDEYQETMVEsTFMYLTLD 393
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHS-----------IIVDLFQGQLKSRLTCL---------------TCGKTSTTFE-PFTYLSLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 394 LPtaplykdeKEQLIIPQVPLF---------NILAKFNGITEKEYKTyKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVE 464
Cdd:cd02674 74 IP--------SGSGDAPKVTLEdclrlftkeETLDGDNAWKCPKCKK-KRKATKKLTISRLPKVLIIHLKRFSFSRGSTR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 465 KNPTIVNFPITNVDLREYLSEEVQAvhKNTTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQMITLS 544
Cdd:cd02674 145 KLTTPVTFPLNDLDLTPYVDTRSFT--GPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSS 222
|
....
gi 20070404 545 EAYI 548
Cdd:cd02674 223 SAYI 226
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
123-185 |
3.29e-21 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 87.32 E-value: 3.29e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070404 123 CSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSSL 185
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-548 |
1.97e-17 |
|
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: 83.09 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLVQRfgeLMRKLWNPRNFKAHVSPHEMLQavvl 304
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAH---VERALASSGPGSAPRIFSSNLK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 305 CSKKTFQITKQGDGVDFLSWFLNALHSAlGGTKKKKKTIVNDVFQGSM---RIFTKKLphpdlpaeeKEQLL-HN----- 375
Cdd:cd02661 76 QISKHFRIGRQEDAHEFLRYLLDAMQKA-CLDRFKKLKAVDPSSQETTlvqQIFGGYL---------RSQVKcLNckhvs 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 376 DEYQEtmvestFMYLTLDLPTAPLYKDEKEQLIIPQvplfnILAKFNgitekEYKTYKENFL----KRFQLTKLPPYLIF 451
Cdd:cd02661 146 NTYDP------FLDLSLDIKGADSLEDALEQFTKPE-----QLDGEN-----KYKCERCKKKvkasKQLTIHRAPNVLTI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 452 CIKRFTknNFFVEKNPTIVNFPITnVDLREYLSeevQAVHKNTTYDLIANIVHDG-KPSEGSYRIHVlHHGTGKWYELQD 530
Cdd:cd02661 210 HLKRFS--NFRGGKINKQISFPET-LDLSPYMS---QPNDGPLKYKLYAVLVHSGfSPHSGHYYCYV-KSSNGKWYNMDD 282
|
330
....*....|....*....
gi 20070404 531 LQVTDILPQMItLSE-AYI 548
Cdd:cd02661 283 SKVSPVSIETV-LSQkAYI 300
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-547 |
3.24e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 77.03 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKN--IKRPPGDIMFLLVQRFGELmrklwnprNFKAHVSPHEMLqAV 302
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTclSCSPNSCLSCAMDEIFQEF--------YYSGDRSPYGPI-NL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 303 VLCS---KKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKT------IVNDVFQGSMRiftkklphpdlpaeekEQLL 373
Cdd:cd02660 73 LYLSwkhSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDeshcncIIHQTFSGSLQ----------------SSVT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 374 HNDEYQETMVESTFMYLTLDLP-TAPLYKDEKEQLIIPQVPLFNILAKFngiTEKEYKTY----------KENFLKRFQL 442
Cdd:cd02660 137 CQRCGGVSTTVDPFLDLSLDIPnKSTPSWALGESGVSGTPTLSDCLDRF---TRPEKLGDfaykcsgcgsTQEATKQLSI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 443 TKLPPYLIFCIKRFTKNNFFV-EKNPTIVNFPITnVDLREYLSEEVQAVH------KNTTYDLIANIVHDGKPSEGSYrI 515
Cdd:cd02660 214 KKLPPVLCFQLKRFEHSLNKTsRKIDTYVQFPLE-LNMTPYTSSSIGDTQdsnsldPDYTYDLFAVVVHKGTLDTGHY-T 291
|
330 340 350
....*....|....*....|....*....|..
gi 20070404 516 HVLHHGTGKWYELQDLQVTDILPQMITLSEAY 547
Cdd:cd02660 292 AYCRQGDGQWFKFDDAMITRVSEEEVLKSQAY 323
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
367-554 |
3.21e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 72.61 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 367 EEKEQLLHND------EYQETMVESTFMYltldlptAPLYKDEKEQLIIPQVPLFNILAKFN-----GITEKEY-KTYKE 434
Cdd:COG5560 631 EEEGQMNFNDavviscEWEEKRYLSLFSY-------DPLWTIREIGAAERTITLQDCLNEFSkpeqlGLSDSWYcPGCKE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 435 N--FLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYlseEVQAVHKNTTYDLIANIVHDGKPSEGS 512
Cdd:COG5560 704 FrqASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGV---EYMVDDPRLIYDLYAVDNHYGGLSGGH 780
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 20070404 513 YRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWKRR 554
Cdd:COG5560 781 YTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
123-171 |
9.98e-12 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 59.69 E-value: 9.98e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 20070404 123 CSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKF 171
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-536 |
4.96e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 63.98 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNVPPLRNYFL-----EEDNYKNIKRPPGDIMFLLVQRFGELMRKLWNPRnfKAHVSPHEML 299
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGN--RSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 300 QAVVLCSkktfqiTKQGDGVDFLSWFLNALHSALGGTK-KKKKTIVNDVFQGSMRIFTKklphpdlpaeekeqllHNDEY 378
Cdd:cd02668 79 KALGLDT------GQQQDAQEFSKLFLSLLEAKLSKSKnPDLKNIVQDLFRGEYSYVTQ----------------CSKCG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 379 QETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQvplfnilaKFNGitEKEYK----TYKENFLKRFQLTKLPPYLIFCIK 454
Cdd:cd02668 137 RESSLPSKFYELELQLKGHKTLEECIDEFLKEE--------QLTG--DNQYFcescNSKTDATRRIRLTTLPPTLNFQLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 455 RFT--KNNFFVEKNPTIVNFPiTNVDLREYLSEEVQAVHkntTYDLIANIVHDG-KPSEGSYRIHVLHHGTGKWYELQDL 531
Cdd:cd02668 207 RFVfdRKTGAKKKLNASISFP-EILDMGEYLAESDEGSY---VYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDE 282
|
....*
gi 20070404 532 QVTDI 536
Cdd:cd02668 283 DVEEM 287
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
220-402 |
1.74e-08 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 57.59 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 220 LPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRP-PGDIMFLLVQRFGELMRKLWNPRNfkaHVSPHEM 298
Cdd:COG5560 262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEnPLGMHGSVASAYADLIKQLYDGNL---HAFTPSG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 299 LQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIVNDVFQGSMRIFTKKlphpdlpAEEK--EQLLHND 376
Cdd:COG5560 339 FKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKK-------AKECwwEHLKRND 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 20070404 377 E---------YQETMVEST----------FMYLTLDLPTAPLYKD 402
Cdd:COG5560 412 SiitdlfqgmYKSTLTCPGcgsvsitfdpFMDLTLPLPVSMVWKH 456
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
222-534 |
1.07e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 50.72 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 222 GIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNiKRPPGDIMFLLVQRFGELmrklwnprnfkaHVSPHEMLQA 301
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED-DDDNKSVPLALQRLFLFL------------QLSESPVKTT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 302 VVLCSKKTFQITK-----QGDGVDFLSWFLNALHSALGGTKKKKktIVNDVFQGSMR--IFTKKLPHpdlpaeekeqllh 374
Cdd:cd02659 68 ELTDKTRSFGWDSlntfeQHDVQEFFRVLFDKLEEKLKGTGQEG--LIKNLFGGKLVnyIICKECPH------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 375 ndEYQEtmvESTFMYLTLDLptaplyKDEKeqliipqvplfNILAKFNGITEKE-------YKTYKENF----LKRFQLT 443
Cdd:cd02659 133 --ESER---EEYFLDLQVAV------KGKK-----------NLEESLDAYVQGEtlegdnkYFCEKCGKkvdaEKGVCFK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 444 KLPPYLIFCIKRFTKNnfFVEKNPTIVN----FPITnVDLREYLSEEVQA--------VHKNTTYDLIANIVHDGKPSEG 511
Cdd:cd02659 191 KLPPVLTLQLKRFEFD--FETMMRIKINdrfeFPLE-LDMEPYTEKGLAKkegdsekkDSESYIYELHGVLVHSGDAHGG 267
|
330 340
....*....|....*....|...
gi 20070404 512 SYRIHVLHHGTGKWYELQDLQVT 534
Cdd:cd02659 268 HYYSYIKDRDDGKWYKFNDDVVT 290
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-552 |
1.16e-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 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: 50.41 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNVPPLRNYFLeedNYKNIKRPPGDIMFLLVQRFGELMRKLWNPRNfkaHVSPHEMLQAVVL 304
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALK---NYNPARRGANQSSDNLTNALRDLFDTMDKKQE---PVPPIEFLQLLRM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 305 C----SKKTFQ-ITKQGDGVDFLSWFLNALHSALGGTKKKkktivNDVFQGSMRI-FTKKLPHPDLPAEEkeqllhndey 378
Cdd:cd02657 75 AfpqfAEKQNQgGYAQQDAEECWSQLLSVLSQKLPGAGSK-----GSFIDQLFGIeLETKMKCTESPDEE---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 379 QETMVESTFMYLTLDLPTAPLYKDEKeqliipqvplfnILAKFNGITEKEYKTYKEN--FLKRFQLTKLPPYLIFCIKRF 456
Cdd:cd02657 140 EVSTESEYKLQCHISITTEVNYLQDG------------LKKGLEEEIEKHSPTLGRDaiYTKTSRISRLPKYLTVQFVRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 457 tknnFFVE---KNPTI---VNFPItNVDLREYLSEevqavhkNTTYDLIANIVHDGKPSE-GSYRIHVLHHGTGKWYELQ 529
Cdd:cd02657 208 ----FWKRdiqKKAKIlrkVKFPF-ELDLYELCTP-------SGYYELVAVITHQGRSADsGHYVAWVRRKNDGKWIKFD 275
|
330 340 350
....*....|....*....|....*....|
gi 20070404 530 DLQVTDILPQMI-TLS------EAYIQIWK 552
Cdd:cd02657 276 DDKVSEVTEEDIlKLSgggdwhIAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-525 |
1.41e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 50.40 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNVPPLRNYFLEEDN--YKNIKRPPGDIMF--------LLVQRFGELMRKLWNPRNFKAHVS 294
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfPSDVVDPANDLNCqlikladgLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 295 PhEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKtivNDVFQGSMriftkklphpdlpaEEKEQLLH 374
Cdd:cd02658 81 P-SMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNP---NDLFKFMI--------------EDRLECLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 375 NDEYQETMVEStfMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGITEKEY--KTYKE--NFLKRFQLTKLPPYLI 450
Cdd:cd02658 143 CKKVKYTSELS--EILSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDfcSTCKEktTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20070404 451 FCIKRFTknnFFVEKNPTIVNFPITnVDlreylseEVQAVHKnttYDLIANIVHDGK-PSEGSYRIHVL--HHGTGKW 525
Cdd:cd02658 221 INMKRFQ---LLENWVPKKLDVPID-VP-------EELGPGK---YELIAFISHKGTsVHSGHYVAHIKkeIDGEGKW 284
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-548 |
4.10e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 45.46 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 225 GLNNIKANDYANAVLQALSNVPPLRNYFLEednyknikrppgdimfllvqrfgelmrklwNPRNFKAHVsphemlqavvl 304
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------TPKELFSQV----------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 305 CSKKT-FQITKQGDGVDFLSWFLNALHSalggtkkkkktIVNDVFQG---SMRIFtkklphpdlpaEEKEQLLHNDEYqe 380
Cdd:cd02667 40 CRKAPqFKGYQQQDSHELLRYLLDGLRT-----------FIDSIFGGeltSTIMC-----------ESCGTVSLVYEP-- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 381 tmvestfmYLTLDLPTAPLYKDEKeqliipqvplfNILAKFNGITEKEYKTYKENFL--------KRFQLTKLPPYLIFC 452
Cdd:cd02667 96 --------FLDLSLPRSDEIKSEC-----------SIESCLKQFTEVEILEGNNKFAcenctkakKQYLISKLPPVLVIH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 453 IKRFTKNNFF-VEKNPTIVNFPiTNVDLREYLSEEVQAVHKNTT--YDLIANIVHDGKPSEGSYRIHVLHH--------- 520
Cdd:cd02667 157 LKRFQQPRSAnLRKVSRHVSFP-EILDLAPFCDPKCNSSEDKSSvlYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdl 235
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 20070404 521 ------------GTGKWYELQDLQVTDILPQMITLSEAYI 548
Cdd:cd02667 236 tkskpaadeagpGSGQWYYISDSDVREVSLEEVLKSEAYL 275
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
445-534 |
2.43e-04 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 44.09 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 445 LPPYLIFCIKRFtkNNFFVEKNPTIVN----FPITnVDLREYLSEEV-QAVHKNTTYDLIANIVHDGKPSEGSYRIHVLH 519
Cdd:COG5077 378 LPPVLHLQLKRF--EYDFERDMMVKINdryeFPLE-IDLLPFLDRDAdKSENSDAVYVLYGVLVHSGDLHEGHYYALLKP 454
|
90
....*....|....*
gi 20070404 520 HGTGKWYELQDLQVT 534
Cdd:COG5077 455 EKDGRWYKFDDTRVT 469
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
419-534 |
1.33e-03 |
|
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: 40.62 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070404 419 AKFNGITEKEYKTYKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPitnvdlreylsEEVQAVhkntTYDL 498
Cdd:cd02665 102 AMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKLEFP-----------QIIQQV----PYEL 166
|
90 100 110
....*....|....*....|....*....|....*.
gi 20070404 499 IANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVT 534
Cdd:cd02665 167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVT 202
|
|
| |
