|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
200-728 |
3.78e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 232.72 E-value: 3.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 200 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 276
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 277 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 356
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 357 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 436
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 437 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 516
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 517 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 596
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 597 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 673
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024516659 674 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 728
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
489-729 |
5.09e-61 |
|
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: 207.14 E-value: 5.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 489 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 568
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 569 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTH 648
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 649 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 728
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 2024516659 729 R 729
Cdd:cd02674 230 E 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
195-732 |
5.74e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 175.07 E-value: 5.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 195 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 268
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 269 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 348
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 349 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWQKE-------------KISSNKLNRANSMEDL-----E 397
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVWKHTivvfpesgrrqplKIELDASSTIRGLKKLvdaeyG 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 398 KDTNSTSEANE--------FLNNQG-TVKVQIHSR-----FSEYIND-----VHMNDVSGAQT-------------LSSN 445
Cdd:COG5560 493 KLGCFEIKVMCiyyggnynMLEPADkVLLQDIPQTdfvylYETNDNGievpvVHLRIEKGYKSkrlfgdpflqlnvLIKA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 446 EGTNTRLSSSppKSCTSCSSSTPIHKKVSTVSSPkrkkCKKYRSVISDIFDgtiissvqCLTcDRLSVTLETFQDLS-LP 524
Cdd:COG5560 573 SIYDKLVKEF--EELLVLVEMKKTDVDLVSEQVR----LLREESSPSSWLK--------LET-EIDTKREEQVEEEGqMN 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 525 IPGKEDLAKLHSASHQTSLVKTGSCGeayaPQGWIAFFMeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMY 604
Cdd:COG5560 638 FNDAVVISCEWEEKRYLSLFSYDPLW----TIREIGAAE-----------------RTITLQDCLNEFSKPEQLGLSDSW 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 605 SCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHG 683
Cdd:COG5560 697 YCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYG 774
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2024516659 684 TASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 732
Cdd:COG5560 775 GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
856-937 |
6.51e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.13 E-value: 6.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 856 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 932
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2024516659 933 HRPPV 937
Cdd:smart00695 81 PRKVV 85
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
860-934 |
3.70e-21 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 88.19 E-value: 3.70e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024516659 860 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 934
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
78-138 |
3.28e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.53 E-value: 3.28e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024516659 78 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 138
Cdd:pfam02148 1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
748-830 |
1.33e-16 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.47 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 748 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 821
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2024516659 822 HLYVCHTCQ 830
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
756-826 |
5.81e-13 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 65.08 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 756 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 825
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2024516659 826 C 826
Cdd:pfam06337 80 N 80
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
77-129 |
3.28e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.52 E-value: 3.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2024516659 77 SCQDCKvRGPNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 129
Cdd:smart00290 1 RCSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
200-728 |
3.78e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 232.72 E-value: 3.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 200 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 276
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 277 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 356
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 357 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 436
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 437 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 516
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 517 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 596
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 597 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 673
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024516659 674 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 728
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
489-729 |
5.09e-61 |
|
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: 207.14 E-value: 5.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 489 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 568
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 569 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTH 648
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 649 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 728
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 2024516659 729 R 729
Cdd:cd02674 230 E 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
477-729 |
1.61e-52 |
|
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: 184.22 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 477 SSPKRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapq 556
Cdd:cd02257 43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 557 gwiaffmeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKlRNGVKFCKVQKFPEILCIHLKRFR 636
Cdd:cd02257 97 ------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 637 H-ELMFSTKIGTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQS 709
Cdd:cd02257 152 FnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDK 230
|
250 260
....*....|....*....|....*
gi 2024516659 710 VTEVSESTVQ-----NAEAYVLFYR 729
Cdd:cd02257 231 VTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
490-728 |
7.22e-46 |
|
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: 167.93 E-value: 7.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 490 VISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSASHQTSLVktgscgeayapqgwiaffmeyfkrf 569
Cdd:cd02660 122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTP------------------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 570 vvscvpswfwgpvvTLQDCLAaFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM-FSTKIGTH 648
Cdd:cd02660 177 --------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 649 VSFPLEgLDLQPFLA--------KDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSESTVQN 720
Cdd:cd02660 242 VQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLK 319
|
....*...
gi 2024516659 721 AEAYVLFY 728
Cdd:cd02660 320 SQAYLLFY 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
195-732 |
5.74e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 175.07 E-value: 5.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 195 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 268
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 269 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 348
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 349 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWQKE-------------KISSNKLNRANSMEDL-----E 397
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVWKHTivvfpesgrrqplKIELDASSTIRGLKKLvdaeyG 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 398 KDTNSTSEANE--------FLNNQG-TVKVQIHSR-----FSEYIND-----VHMNDVSGAQT-------------LSSN 445
Cdd:COG5560 493 KLGCFEIKVMCiyyggnynMLEPADkVLLQDIPQTdfvylYETNDNGievpvVHLRIEKGYKSkrlfgdpflqlnvLIKA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 446 EGTNTRLSSSppKSCTSCSSSTPIHKKVSTVSSPkrkkCKKYRSVISDIFDgtiissvqCLTcDRLSVTLETFQDLS-LP 524
Cdd:COG5560 573 SIYDKLVKEF--EELLVLVEMKKTDVDLVSEQVR----LLREESSPSSWLK--------LET-EIDTKREEQVEEEGqMN 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 525 IPGKEDLAKLHSASHQTSLVKTGSCGeayaPQGWIAFFMeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMY 604
Cdd:COG5560 638 FNDAVVISCEWEEKRYLSLFSYDPLW----TIREIGAAE-----------------RTITLQDCLNEFSKPEQLGLSDSW 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 605 SCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHG 683
Cdd:COG5560 697 YCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYG 774
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2024516659 684 TASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 732
Cdd:COG5560 775 GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
475-728 |
1.87e-44 |
|
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: 163.22 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 475 TVSSPKRKKCKKY------RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGkedlaklhsashqtslvktgs 548
Cdd:cd02661 102 KACLDRFKKLKAVdpssqeTTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 549 cgeayapqgwiaffmeyfkrfvvscvpswfwgpVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEIL 628
Cdd:cd02661 161 ---------------------------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 629 CIHLKRFrhELMFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRnNLNNLWYEFDD 707
Cdd:cd02661 208 TIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDD 282
|
250 260
....*....|....*....|.
gi 2024516659 708 QSVTEVSESTVQNAEAYVLFY 728
Cdd:cd02661 283 SKVSPVSIETVLSQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
491-732 |
5.41e-36 |
|
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: 139.31 E-value: 5.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 491 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmEYFKRFV 570
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLE-------------------------------ESLDAYV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 571 VScvpswfwgpvvtlqdclaaffarDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKIGTH 648
Cdd:cd02659 162 QG-----------------------ETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 649 VSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 718
Cdd:cd02659 219 FEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDA 297
|
250 260 270
....*....|....*....|....*....|....*.
gi 2024516659 719 QNA----------------------EAYVLFYRKSN 732
Cdd:cd02659 298 EEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
488-729 |
1.08e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 122.50 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 488 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfk 567
Cdd:cd02667 66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 568 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST-KIG 646
Cdd:cd02667 109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 647 THVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL---------------- 701
Cdd:cd02667 173 RHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagp 247
|
250 260 270
....*....|....*....|....*....|..
gi 2024516659 702 ----WYEFDDQSVTEVSESTVQNAEAYVLFYR 729
Cdd:cd02667 248 gsgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
483-728 |
7.20e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 114.71 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 483 KCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPgkedlaklhsashqtslvktgscgeayapqgwiaff 562
Cdd:cd02663 101 NAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE------------------------------------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 563 meyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS 642
Cdd:cd02663 145 ------------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 643 --TKIGTHVSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTV 718
Cdd:cd02663 207 ryIKLFYRVVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAV 281
|
250
....*....|....*...
gi 2024516659 719 QN--------AEAYVLFY 728
Cdd:cd02663 282 EEffgdspnqATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
485-712 |
6.12e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 112.51 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 485 KKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffme 564
Cdd:cd02668 112 PDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK----------------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 565 yfkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL--MFS 642
Cdd:cd02668 157 -------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAK 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024516659 643 TKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 712
Cdd:cd02668 218 KKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
856-937 |
6.51e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.13 E-value: 6.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 856 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 932
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2024516659 933 HRPPV 937
Cdd:smart00695 81 PRKVV 85
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
495-728 |
1.60e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 100.52 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 495 FDGTIISSVQCLTCDRLS-VTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvsc 573
Cdd:cd02662 56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQS-------------------------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 574 vpswfWGPVVTLQDCLAAFFARDELKGdnmYSCGRCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKIGTHVSFP 652
Cdd:cd02662 92 -----SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 653 LegldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTE 712
Cdd:cd02662 156 E-------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKE 222
|
250
....*....|....*..
gi 2024516659 713 VSESTV-QNAEAYVLFY 728
Cdd:cd02662 223 VSESEVlEQKSAYMLFY 239
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
860-934 |
3.70e-21 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 88.19 E-value: 3.70e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024516659 860 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 934
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
489-729 |
1.76e-20 |
|
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: 93.71 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 489 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLpipgkedlaklhsashqtslvktgscgeayapqgwiaffmeyfkr 568
Cdd:cd02664 97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 569 fvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFSTKIG 646
Cdd:cd02664 132 ----SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 647 THVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN----------- 696
Cdd:cd02664 200 DNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqec 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024516659 697 ---------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 729
Cdd:cd02664 279 pepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
488-729 |
6.72e-20 |
|
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: 91.88 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 488 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdLAKLHSASHQTSLVKTgscgeayapqgwiaffmeyfk 567
Cdd:cd02671 120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 568 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS----- 642
Cdd:cd02671 178 -------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygg 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 643 -TKIGTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------T 711
Cdd:cd02671 245 lSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflE 314
|
250
....*....|....*...
gi 2024516659 712 EVSESTVQNAEAYVLFYR 729
Cdd:cd02671 315 ALSPNTSSTSTPYLLFYK 332
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
584-718 |
2.13e-17 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 87.62 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 584 TLQDCLAAFFARDELKGDNMYSCGR--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KIGTHVSFPLEgLDLQ 659
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024516659 660 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 718
Cdd:COG5077 415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
78-138 |
3.28e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.53 E-value: 3.28e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024516659 78 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 138
Cdd:pfam02148 1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
748-830 |
1.33e-16 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.47 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 748 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 821
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2024516659 822 HLYVCHTCQ 830
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
625-729 |
4.42e-16 |
|
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: 80.07 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 625 PEILCIHLKRF--RHELMFSTKIGTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 701
Cdd:cd02657 197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270
|
90 100 110
....*....|....*....|....*....|....*
gi 2024516659 702 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 729
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
623-730 |
3.12e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.15 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 623 KFPEILCIHLKRFRHELMFsTKIGTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlN 699
Cdd:COG5533 178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--G 249
|
90 100 110
....*....|....*....|....*....|....
gi 2024516659 700 NLWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 730
Cdd:COG5533 250 GKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
608-729 |
3.79e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 78.90 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 608 RCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT- 684
Cdd:cd02669 316 TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTp 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024516659 685 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 729
Cdd:cd02669 396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
491-729 |
3.05e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 71.59 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 491 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSAshqtslvktgscgEAYAPqgwiaffmeyfkrfv 570
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP--------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 571 vscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMF-STKIGTHV 649
Cdd:cd02658 178 ------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 650 SFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSESTVQNAEAYVL 726
Cdd:cd02658 242 DVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKLGYIY 308
|
...
gi 2024516659 727 FYR 729
Cdd:cd02658 309 FYQ 311
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
756-826 |
5.81e-13 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 65.08 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 756 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 825
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2024516659 826 C 826
Cdd:pfam06337 80 N 80
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
201-329 |
8.74e-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 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: 64.27 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 201 GLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKNRPgsVVPTGLFQGIKSVNPT 278
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 279 F------RGYSQQDAQEFLRCLMDLLHEELKEPIVE---VEDAQTMSVEESMEVDKSQSD 329
Cdd:cd02657 79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLPGAGSKgsfIDQLFGIELETKMKCTESPDE 138
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
673-728 |
3.36e-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: 62.89 E-value: 3.36e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024516659 673 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 728
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
77-129 |
3.28e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.52 E-value: 3.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2024516659 77 SCQDCKvRGPNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 129
Cdd:smart00290 1 RCSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
201-307 |
7.35e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 57.89 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 201 GLKNIGNTCYMNAALQALS-NCPPLTHFFLDCGGLART-------DKKPAICKSYLKLMTELWHKNRPgsvvptglfqgi 272
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
|
90 100 110
....*....|....*....|....*....|....*
gi 2024516659 273 kSVNPTFRGYSQQDAQEFLRCLMDllheELKEPIV 307
Cdd:COG5533 69 -KVGWIPPMGSQEDAHELLGKLLD----ELKLDLV 98
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
606-728 |
2.88e-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: 55.61 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 606 CGRCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKIGTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 679
Cdd:cd02673 129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2024516659 680 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 728
Cdd:cd02673 191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
623-728 |
8.10e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 54.10 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 623 KFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 702
Cdd:cd02665 127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
|
90 100 110
....*....|....*....|....*....|....
gi 2024516659 703 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 728
Cdd:cd02665 194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
568-729 |
9.30e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 54.07 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 568 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscgrckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIGT 647
Cdd:cd02670 65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 648 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 697
Cdd:cd02670 122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024516659 698 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 729
Cdd:cd02670 201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
201-303 |
5.17e-07 |
|
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: 52.71 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 201 GLKNIGNTCYMNAALQALSNCPPL-THFFLDCGGLARTDKKPAIC------------KS--YLKLMTELW-HKNRPGSVV 264
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024516659 265 PTGLFQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELK 303
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
606-728 |
1.67e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 50.59 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 606 CGRCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKIGTHVSFPLEglDLQPFLAKDSPAQIVTYD 674
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024516659 675 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 728
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
606-710 |
4.10e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 49.58 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516659 606 CGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 684
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
|
90 100 110
....*....|....*....|....*....|...
gi 2024516659 685 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 710
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
|
|
| |
