|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
152-680 |
3.18e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 232.33 E-value: 3.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 152 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 228
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 229 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 308
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 309 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 388
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 389 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 468
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 469 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 548
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 549 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 625
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024516669 626 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 680
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-681 |
4.42e-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: 4.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 441 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 520
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 521 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTH 600
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 601 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 680
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 2024516669 681 R 681
Cdd:cd02674 230 E 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
147-684 |
4.54e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 175.07 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 147 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 220
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 221 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 300
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 301 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWQKE-------------KISSNKLNRANSMEDL-----E 349
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVWKHTivvfpesgrrqplKIELDASSTIRGLKKLvdaeyG 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 350 KDTNSTSEANE--------FLNNQG-TVKVQIHSR-----FSEYIND-----VHMNDVSGAQT-------------LSSN 397
Cdd:COG5560 493 KLGCFEIKVMCiyyggnynMLEPADkVLLQDIPQTdfvylYETNDNGievpvVHLRIEKGYKSkrlfgdpflqlnvLIKA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 398 EGTNTRLSSSppKSCTSCSSSTPIHKKVSTVSSPkrkkCKKYRSVISDIFDgtiissvqCLTcDRLSVTLETFQDLS-LP 476
Cdd:COG5560 573 SIYDKLVKEF--EELLVLVEMKKTDVDLVSEQVR----LLREESSPSSWLK--------LET-EIDTKREEQVEEEGqMN 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 477 IPGKEDLAKLHSASHQTSLVKTGSCGeayaPQGWIAFFMeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMY 556
Cdd:COG5560 638 FNDAVVISCEWEEKRYLSLFSYDPLW----TIREIGAAE-----------------RTITLQDCLNEFSKPEQLGLSDSW 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 557 SCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHG 635
Cdd:COG5560 697 YCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYG 774
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2024516669 636 TASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 684
Cdd:COG5560 775 GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
808-889 |
4.89e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.13 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 808 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 884
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2024516669 885 HRPPV 889
Cdd:smart00695 81 PRKVV 85
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
812-886 |
3.76e-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: 3.76e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024516669 812 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 886
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
30-90 |
3.71e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 3.71e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024516669 30 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148 1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
700-782 |
1.03e-16 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.86 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 700 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 773
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2024516669 774 HLYVCHTCQ 782
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
708-778 |
5.73e-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: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 708 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 777
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2024516669 778 C 778
Cdd:pfam06337 80 N 80
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-81 |
3.11e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.52 E-value: 3.11e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2024516669 29 SCQDCKvRGPNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 81
Cdd:smart00290 1 RCSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
152-680 |
3.18e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 232.33 E-value: 3.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 152 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 228
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 229 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 308
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 309 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 388
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 389 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 468
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 469 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 548
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 549 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 625
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024516669 626 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 680
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-681 |
4.42e-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: 4.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 441 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 520
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 521 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTH 600
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 601 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 680
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 2024516669 681 R 681
Cdd:cd02674 230 E 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
429-681 |
1.75e-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: 1.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 429 SSPKRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapq 508
Cdd:cd02257 43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 509 gwiaffmeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKlRNGVKFCKVQKFPEILCIHLKRFR 588
Cdd:cd02257 97 ------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 589 H-ELMFSTKIGTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQS 661
Cdd:cd02257 152 FnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDK 230
|
250 260
....*....|....*....|....*
gi 2024516669 662 VTEVSESTVQ-----NAEAYVLFYR 681
Cdd:cd02257 231 VTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-680 |
5.16e-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: 168.32 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 442 VISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSASHQTSLVktgscgeayapqgwiaffmeyfkrf 521
Cdd:cd02660 122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTP------------------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 522 vvscvpswfwgpvvTLQDCLAaFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM-FSTKIGTH 600
Cdd:cd02660 177 --------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 601 VSFPLEgLDLQPFLA--------KDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSESTVQN 672
Cdd:cd02660 242 VQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLK 319
|
....*...
gi 2024516669 673 AEAYVLFY 680
Cdd:cd02660 320 SQAYLLFY 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
147-684 |
4.54e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 175.07 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 147 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 220
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 221 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 300
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 301 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWQKE-------------KISSNKLNRANSMEDL-----E 349
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVWKHTivvfpesgrrqplKIELDASSTIRGLKKLvdaeyG 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 350 KDTNSTSEANE--------FLNNQG-TVKVQIHSR-----FSEYIND-----VHMNDVSGAQT-------------LSSN 397
Cdd:COG5560 493 KLGCFEIKVMCiyyggnynMLEPADkVLLQDIPQTdfvylYETNDNGievpvVHLRIEKGYKSkrlfgdpflqlnvLIKA 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 398 EGTNTRLSSSppKSCTSCSSSTPIHKKVSTVSSPkrkkCKKYRSVISDIFDgtiissvqCLTcDRLSVTLETFQDLS-LP 476
Cdd:COG5560 573 SIYDKLVKEF--EELLVLVEMKKTDVDLVSEQVR----LLREESSPSSWLK--------LET-EIDTKREEQVEEEGqMN 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 477 IPGKEDLAKLHSASHQTSLVKTGSCGeayaPQGWIAFFMeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMY 556
Cdd:COG5560 638 FNDAVVISCEWEEKRYLSLFSYDPLW----TIREIGAAE-----------------RTITLQDCLNEFSKPEQLGLSDSW 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 557 SCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHG 635
Cdd:COG5560 697 YCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYG 774
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2024516669 636 TASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 684
Cdd:COG5560 775 GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
427-680 |
1.59e-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: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 427 TVSSPKRKKCKKY------RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGkedlaklhsashqtslvktgs 500
Cdd:cd02661 102 KACLDRFKKLKAVdpssqeTTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 501 cgeayapqgwiaffmeyfkrfvvscvpswfwgpVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEIL 580
Cdd:cd02661 161 ---------------------------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 581 CIHLKRFrhELMFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRnNLNNLWYEFDD 659
Cdd:cd02661 208 TIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDD 282
|
250 260
....*....|....*....|.
gi 2024516669 660 QSVTEVSESTVQNAEAYVLFY 680
Cdd:cd02661 283 SKVSPVSIETVLSQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-684 |
8.55e-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: 138.93 E-value: 8.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 443 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmEYFKRFV 522
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLE-------------------------------ESLDAYV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 523 VScvpswfwgpvvtlqdclaaffarDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKIGTH 600
Cdd:cd02659 162 QG-----------------------ETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 601 VSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 670
Cdd:cd02659 219 FEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDA 297
|
250 260 270
....*....|....*....|....*....|....*.
gi 2024516669 671 QNA----------------------EAYVLFYRKSN 684
Cdd:cd02659 298 EEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
440-681 |
8.82e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 122.50 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 440 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfk 519
Cdd:cd02667 66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 520 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST-KIG 598
Cdd:cd02667 109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 599 THVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL---------------- 653
Cdd:cd02667 173 RHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagp 247
|
250 260 270
....*....|....*....|....*....|..
gi 2024516669 654 ----WYEFDDQSVTEVSESTVQNAEAYVLFYR 681
Cdd:cd02667 248 gsgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
435-680 |
8.61e-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: 114.33 E-value: 8.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 435 KCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPgkedlaklhsashqtslvktgscgeayapqgwiaff 514
Cdd:cd02663 101 NAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE------------------------------------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 515 meyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS 594
Cdd:cd02663 145 ------------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 595 --TKIGTHVSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTV 670
Cdd:cd02663 207 ryIKLFYRVVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAV 281
|
250
....*....|....*...
gi 2024516669 671 QN--------AEAYVLFY 680
Cdd:cd02663 282 EEffgdspnqATAYVLFY 299
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
808-889 |
4.89e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.13 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 808 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 884
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2024516669 885 HRPPV 889
Cdd:smart00695 81 PRKVV 85
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
437-664 |
6.52e-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: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 437 KKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffme 516
Cdd:cd02668 112 PDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK----------------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 517 yfkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL--MFS 594
Cdd:cd02668 157 -------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAK 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024516669 595 TKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 664
Cdd:cd02668 218 KKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-680 |
1.26e-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: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 447 FDGTIISSVQCLTCDRLS-VTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvsc 525
Cdd:cd02662 56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQS-------------------------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 526 vpswfWGPVVTLQDCLAAFFARDELKGdnmYSCGRCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKIGTHVSFP 604
Cdd:cd02662 92 -----SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 605 LegldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTE 664
Cdd:cd02662 156 E-------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKE 222
|
250
....*....|....*..
gi 2024516669 665 VSESTV-QNAEAYVLFY 680
Cdd:cd02662 223 VSESEVlEQKSAYMLFY 239
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
812-886 |
3.76e-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: 3.76e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024516669 812 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 886
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-681 |
1.39e-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: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 441 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLpipgkedlaklhsashqtslvktgscgeayapqgwiaffmeyfkr 520
Cdd:cd02664 97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 521 fvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFSTKIG 598
Cdd:cd02664 132 ----SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 599 THVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN----------- 648
Cdd:cd02664 200 DNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqec 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024516669 649 ---------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 681
Cdd:cd02664 279 pepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
440-681 |
6.28e-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: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 440 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdLAKLHSASHQTSLVKTgscgeayapqgwiaffmeyfk 519
Cdd:cd02671 120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 520 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS----- 594
Cdd:cd02671 178 -------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygg 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 595 -TKIGTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------T 663
Cdd:cd02671 245 lSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflE 314
|
250
....*....|....*...
gi 2024516669 664 EVSESTVQNAEAYVLFYR 681
Cdd:cd02671 315 ALSPNTSSTSTPYLLFYK 332
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
536-670 |
2.18e-17 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 87.62 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 536 TLQDCLAAFFARDELKGDNMYSCGR--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KIGTHVSFPLEgLDLQ 611
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024516669 612 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 670
Cdd:COG5077 415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
30-90 |
3.71e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 3.71e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024516669 30 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148 1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
700-782 |
1.03e-16 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.86 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 700 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 773
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2024516669 774 HLYVCHTCQ 782
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
577-681 |
3.84e-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: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 577 PEILCIHLKRF--RHELMFSTKIGTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 653
Cdd:cd02657 197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270
|
90 100 110
....*....|....*....|....*....|....*
gi 2024516669 654 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 681
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
575-682 |
2.92e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.15 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 575 KFPEILCIHLKRFRHELMFsTKIGTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlN 651
Cdd:COG5533 178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--G 249
|
90 100 110
....*....|....*....|....*....|....
gi 2024516669 652 NLWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 682
Cdd:COG5533 250 GKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
560-681 |
3.72e-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: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 560 RCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT- 636
Cdd:cd02669 316 TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTp 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024516669 637 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 681
Cdd:cd02669 396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-681 |
3.36e-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: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 443 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSAshqtslvktgscgEAYAPqgwiaffmeyfkrfv 522
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP--------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 523 vscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMF-STKIGTHV 601
Cdd:cd02658 178 ------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 602 SFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSESTVQNAEAYVL 678
Cdd:cd02658 242 DVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKLGYIY 308
|
...
gi 2024516669 679 FYR 681
Cdd:cd02658 309 FYQ 311
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
708-778 |
5.73e-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: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 708 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 777
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2024516669 778 C 778
Cdd:pfam06337 80 N 80
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
153-281 |
7.62e-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: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 153 GLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKNRPgsVVPTGLFQGIKSVNPT 230
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 231 F------RGYSQQDAQEFLRCLMDLLHEELKEPIVE---VEDAQTMSVEESMEVDKSQSD 281
Cdd:cd02657 79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLPGAGSKgsfIDQLFGIELETKMKCTESPDE 138
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
625-680 |
3.15e-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: 3.15e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024516669 625 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 680
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-81 |
3.11e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.52 E-value: 3.11e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2024516669 29 SCQDCKvRGPNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 81
Cdd:smart00290 1 RCSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
153-259 |
6.90e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 57.89 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 153 GLKNIGNTCYMNAALQALS-NCPPLTHFFLDCGGLART-------DKKPAICKSYLKLMTELWHKNRPgsvvptglfqgi 224
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
|
90 100 110
....*....|....*....|....*....|....*
gi 2024516669 225 kSVNPTFRGYSQQDAQEFLRCLMDllheELKEPIV 259
Cdd:COG5533 69 -KVGWIPPMGSQEDAHELLGKLLD----ELKLDLV 98
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
558-680 |
2.97e-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: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 558 CGRCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKIGTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 631
Cdd:cd02673 129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2024516669 632 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 680
Cdd:cd02673 191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
575-680 |
6.70e-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: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 575 KFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 654
Cdd:cd02665 127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
|
90 100 110
....*....|....*....|....*....|....
gi 2024516669 655 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 680
Cdd:cd02665 194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
520-681 |
1.08e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 53.68 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 520 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscgrckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIGT 599
Cdd:cd02670 65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 600 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 649
Cdd:cd02670 122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024516669 650 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 681
Cdd:cd02670 201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
153-255 |
5.26e-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: 52.33 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 153 GLKNIGNTCYMNAALQALSNCPPL-THFFLDCGGLARTDKKPAIC------------KS--YLKLMTELW-HKNRPGSVV 216
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024516669 217 PTGLFQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELK 255
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
558-680 |
1.64e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 50.59 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 558 CGRCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKIGTHVSFPLEglDLQPFLAKDSPAQIVTYD 626
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024516669 627 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 680
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
558-662 |
3.65e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 49.96 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516669 558 CGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 636
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
|
90 100 110
....*....|....*....|....*....|...
gi 2024516669 637 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 662
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
|
|
| |
