|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
108-639 |
4.78e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 231.18 E-value: 4.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 108 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 184
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 185 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 264
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 265 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 344
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 345 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 424
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 425 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfvvscvpswfWGPVVTLQDCLAAFF 504
Cdd:pfam00443 144 PFSDLSLPIPGDSA---------------------------------------------------ELKTASLQICFLQFS 172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 505 ARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV-- 582
Cdd:pfam00443 173 KLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnl 251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024516673 583 -TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 639
Cdd:pfam00443 252 qDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
397-640 |
7.29e-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: 205.98 E-value: 7.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 397 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 476
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 477 cfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKI 556
Cdd:cd02674 82 ---------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 557 GTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYV 636
Cdd:cd02674 147 TTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYI 226
|
....
gi 2024516673 637 LFYR 640
Cdd:cd02674 227 LFYE 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
103-643 |
1.62e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 176.23 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 103 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 176
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 177 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 256
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 257 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWqKEKISSNKLNRANSMEDLEKDTNSTSEAnefLNNQGT 323
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVW-KHTIVVFPESGRRQPLKIELDASSTIRG---LKKLVD 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 324 VKVQIHSRFSEYINDVHMNDVSGAqtlsSNEGTNTRLSSSPPKSCTSCSSSTPIHKKVSTVSSPKRKKCKKYRsVISDIF 403
Cdd:COG5560 489 AEYGKLGCFEIKVMCIYYGGNYNM----LEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVHLRIEKGYKSKR-LFGDPF 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 404 DGTIISSVQCLTCDRLSVTLETFQDLSLpipGKEDLAKLHSashQTSLVKTGScgeayAPQGWIAFFMEYFKRCF----- 478
Cdd:COG5560 564 LQLNVLIKASIYDKLVKEFEELLVLVEM---KKTDVDLVSE---QVRLLREES-----SPSSWLKLETEIDTKREeqvee 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 479 --------RFVVSCV-------------PSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCK 531
Cdd:COG5560 633 egqmnfndAVVISCEweekrylslfsydPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQME 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 532 VQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLN 610
Cdd:COG5560 713 LWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFAN 790
|
570 580 590
....*....|....*....|....*....|...
gi 2024516673 611 NLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 643
Cdd:COG5560 791 NGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
767-848 |
4.40e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.52 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 767 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 843
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2024516673 844 HRPPV 848
Cdd:smart00695 81 PRKVV 85
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
771-845 |
3.62e-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: 3.62e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024516673 771 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 845
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
659-741 |
9.30e-17 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.86 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 659 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 732
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2024516673 733 HLYVCHTCQ 741
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
667-737 |
5.57e-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: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 667 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 736
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2024516673 737 C 737
Cdd:pfam06337 80 N 80
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
4-46 |
2.88e-12 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 62.28 E-value: 2.88e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2024516673 4 CTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 46
Cdd:pfam02148 16 CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
4-37 |
2.58e-05 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 42.35 E-value: 2.58e-05
10 20 30
....*....|....*....|....*....|....
gi 2024516673 4 CTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 37
Cdd:smart00290 17 CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
108-639 |
4.78e-69 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 231.18 E-value: 4.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 108 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 184
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 185 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 264
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 265 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 344
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 345 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 424
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 425 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfvvscvpswfWGPVVTLQDCLAAFF 504
Cdd:pfam00443 144 PFSDLSLPIPGDSA---------------------------------------------------ELKTASLQICFLQFS 172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 505 ARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV-- 582
Cdd:pfam00443 173 KLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnl 251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024516673 583 -TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 639
Cdd:pfam00443 252 qDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
397-640 |
7.29e-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: 205.98 E-value: 7.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 397 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 476
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 477 cfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKI 556
Cdd:cd02674 82 ---------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 557 GTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYV 636
Cdd:cd02674 147 TTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYI 226
|
....
gi 2024516673 637 LFYR 640
Cdd:cd02674 227 LFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
385-640 |
2.89e-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: 183.07 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 385 SSPKRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapq 464
Cdd:cd02257 43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 465 gwiaffmeyfkrcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKlRNGVKFCKVQKFPEILCIHLK 544
Cdd:cd02257 97 ---------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 545 RFRH-ELMFSTKIGTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFD 617
Cdd:cd02257 149 RFSFnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFN 227
|
250 260
....*....|....*....|....*...
gi 2024516673 618 DQSVTEVSESTVQ-----NAEAYVLFYR 640
Cdd:cd02257 228 DDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
398-639 |
8.45e-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: 167.55 E-value: 8.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 398 VISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSASHQTSLVktgscgeayapqgwiaffmeyfkrc 477
Cdd:cd02660 122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTP------------------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 478 frfvvscvpswfwgpvvTLQDCLAaFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM-FSTKI 556
Cdd:cd02660 177 -----------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 557 GTHVSFPLEgLDLQPFLA--------KDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSEST 628
Cdd:cd02660 239 DTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEE 316
|
250
....*....|.
gi 2024516673 629 VQNAEAYVLFY 639
Cdd:cd02660 317 VLKSQAYLLFY 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
103-643 |
1.62e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 176.23 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 103 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 176
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 177 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 256
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 257 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWqKEKISSNKLNRANSMEDLEKDTNSTSEAnefLNNQGT 323
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVW-KHTIVVFPESGRRQPLKIELDASSTIRG---LKKLVD 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 324 VKVQIHSRFSEYINDVHMNDVSGAqtlsSNEGTNTRLSSSPPKSCTSCSSSTPIHKKVSTVSSPKRKKCKKYRsVISDIF 403
Cdd:COG5560 489 AEYGKLGCFEIKVMCIYYGGNYNM----LEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVHLRIEKGYKSKR-LFGDPF 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 404 DGTIISSVQCLTCDRLSVTLETFQDLSLpipGKEDLAKLHSashQTSLVKTGScgeayAPQGWIAFFMEYFKRCF----- 478
Cdd:COG5560 564 LQLNVLIKASIYDKLVKEFEELLVLVEM---KKTDVDLVSE---QVRLLREES-----SPSSWLKLETEIDTKREeqvee 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 479 --------RFVVSCV-------------PSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCK 531
Cdd:COG5560 633 egqmnfndAVVISCEweekrylslfsydPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQME 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 532 VQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLN 610
Cdd:COG5560 713 LWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFAN 790
|
570 580 590
....*....|....*....|....*....|...
gi 2024516673 611 NLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 643
Cdd:COG5560 791 NGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-639 |
2.45e-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: 162.45 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 108 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDcGGLARTDKKPAICKS-YLKLMTELWHKNRPGSVVPTGLFQGIKSVNPT 186
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 187 FRGYSQQDAQEFLRCLMDLLHEelkepivevedaqtmsveesmevdksqsdvgfqpceSCgtcdkiendavfkpvledpa 266
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQK------------------------------------AC-------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 267 ettmliqddennsitskdwqkekissnkLNRANSMEDLEKDTNSTSeaneflnnqgtvkvqihsrfseyindvhmndvsg 346
Cdd:cd02661 105 ----------------------------LDRFKKLKAVDPSSQETT---------------------------------- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 347 aqtlssnegtntrlsssppksctscssstpihkkvstvsspkrkkckkyrsVISDIFDGTIISSVQCLTCDRLSVTLETF 426
Cdd:cd02661 123 ---------------------------------------------------LVQQIFGGYLRSQVKCLNCKHVSNTYDPF 151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 427 QDLSLPIPGkedlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfvvscvpswfwgpVVTLQDCLAAFFAR 506
Cdd:cd02661 152 LDLSLDIKG---------------------------------------------------------ADSLEDALEQFTKP 174
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 507 DELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFrhELMFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDL 586
Cdd:cd02661 175 EQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKL 250
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2024516673 587 LSVICHHGT-ASSGHYIAYCRnNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 639
Cdd:cd02661 251 YAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
399-643 |
2.76e-35 |
|
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: 137.39 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 399 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLaklhsashqtslvktgscgeayapqgwiaffmeyfkrcf 478
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 479 rfvvscvpswfwgpvvtlQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKI 556
Cdd:cd02659 154 ------------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 557 GTHVSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSE 626
Cdd:cd02659 216 NDRFEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDP 294
|
250 260 270
....*....|....*....|....*....|....*....
gi 2024516673 627 STVQNA----------------------EAYVLFYRKSN 643
Cdd:cd02659 295 NDAEEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-640 |
1.62e-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: 121.72 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 396 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfk 475
Cdd:cd02667 66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 476 rcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST- 554
Cdd:cd02667 109 ----------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLr 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 555 KIGTHVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL------------- 612
Cdd:cd02667 170 KVSRHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaade 244
|
250 260 270
....*....|....*....|....*....|....*
gi 2024516673 613 -------WYEFDDQSVTEVSESTVQNAEAYVLFYR 640
Cdd:cd02667 245 agpgsgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
391-639 |
1.90e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 113.56 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 391 KCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPgkedlaklhsashqtslvktgscgeayapqgwiaff 470
Cdd:cd02663 101 NAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE------------------------------------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 471 meyfkrcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL 550
Cdd:cd02663 145 ---------------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 551 MFS--TKIGTHVSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSE 626
Cdd:cd02663 204 QLNryIKLFYRVVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDE 278
|
250 260
....*....|....*....|.
gi 2024516673 627 STVQN--------AEAYVLFY 639
Cdd:cd02663 279 NAVEEffgdspnqATAYVLFY 299
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
767-848 |
4.40e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.52 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 767 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 843
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2024516673 844 HRPPV 848
Cdd:smart00695 81 PRKVV 85
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
393-623 |
1.24e-26 |
|
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: 111.74 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 393 KKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffme 472
Cdd:cd02668 112 PDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK----------------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 473 yfkrcfrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL-- 550
Cdd:cd02668 157 ----------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRkt 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024516673 551 MFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 623
Cdd:cd02668 215 GAKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
403-639 |
1.94e-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: 100.13 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 403 FDGTIISSVQCLTCDRLS-VTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfv 481
Cdd:cd02662 56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQS-------------------------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 482 vscvpswfWGPVVTLQDCLAAFFARDELKGdnmYSCGRCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKIGTHV 560
Cdd:cd02662 92 --------SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 561 SFPLegldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQS 620
Cdd:cd02662 153 SFPE-------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTT 219
|
250 260
....*....|....*....|
gi 2024516673 621 VTEVSESTV-QNAEAYVLFY 639
Cdd:cd02662 220 VKEVSESEVlEQKSAYMLFY 239
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
771-845 |
3.62e-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: 3.62e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024516673 771 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 845
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
397-640 |
2.96e-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: 92.94 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 397 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLpipgkedlaklhsashqtslvktgscgeayapqgwiaffmeyfkr 476
Cdd:cd02664 97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 477 cfrfvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFST 554
Cdd:cd02664 132 -------SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 555 KIGTHVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN-------- 607
Cdd:cd02664 197 KIMDNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstg 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2024516673 608 ------------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 640
Cdd:cd02664 276 qecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-640 |
1.16e-19 |
|
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: 91.11 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 396 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdLAKLHSASHQTSLVKTgscgeayapqgwiaffmeyfk 475
Cdd:cd02671 120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 476 rcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS-- 553
Cdd:cd02671 178 ----------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdc 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 554 ----TKIGTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV------- 621
Cdd:cd02671 242 ygglSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekd 311
|
250 260
....*....|....*....|.
gi 2024516673 622 --TEVSESTVQNAEAYVLFYR 640
Cdd:cd02671 312 flEALSPNTSSTSTPYLLFYK 332
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
495-629 |
2.58e-17 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 87.23 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 495 TLQDCLAAFFARDELKGDNMYSCGR--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KIGTHVSFPLEgLDLQ 570
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024516673 571 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 629
Cdd:COG5077 415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
659-741 |
9.30e-17 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.86 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 659 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 732
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2024516673 733 HLYVCHTCQ 741
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
536-640 |
3.48e-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: 80.45 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 536 PEILCIHLKRF--RHELMFSTKIGTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 612
Cdd:cd02657 197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270
|
90 100 110
....*....|....*....|....*....|....*
gi 2024516673 613 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 640
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
534-641 |
2.78e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.15 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 534 KFPEILCIHLKRFRHELMFsTKIGTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlN 610
Cdd:COG5533 178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--G 249
|
90 100 110
....*....|....*....|....*....|....
gi 2024516673 611 NLWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 641
Cdd:COG5533 250 GKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
519-640 |
3.63e-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: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 519 RCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT- 595
Cdd:cd02669 316 TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTp 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024516673 596 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 640
Cdd:cd02669 396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
667-737 |
5.57e-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: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 667 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 736
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2024516673 737 C 737
Cdd:pfam06337 80 N 80
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
399-640 |
7.56e-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: 70.43 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 399 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSAshqtslvktgscgEAYAPqgwiaffmeyfkrcf 478
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP--------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 479 rfvvscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMF-STKIG 557
Cdd:cd02658 178 ---------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 558 THVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSESTVQNAEA 634
Cdd:cd02658 239 VPIDVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKLG 305
|
....*.
gi 2024516673 635 YVLFYR 640
Cdd:cd02658 306 YIYFYQ 311
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
4-46 |
2.88e-12 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 62.28 E-value: 2.88e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2024516673 4 CTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 46
Cdd:pfam02148 16 CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
109-237 |
7.19e-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: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 109 GLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKNRPgsVVPTGLFQGIKSVNPT 186
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 187 F------RGYSQQDAQEFLRCLMDLLHEELKEPIVE---VEDAQTMSVEESMEVDKSQSD 237
Cdd:cd02657 79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLPGAGSKgsfIDQLFGIELETKMKCTESPDE 138
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
584-639 |
2.97e-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: 2.97e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024516673 584 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 639
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
109-215 |
6.52e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 57.89 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 109 GLKNIGNTCYMNAALQALS-NCPPLTHFFLDCGGLART-------DKKPAICKSYLKLMTELWHKNRPgsvvptglfqgi 180
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
|
90 100 110
....*....|....*....|....*....|....*
gi 2024516673 181 kSVNPTFRGYSQQDAQEFLRCLMDllheELKEPIV 215
Cdd:COG5533 69 -KVGWIPPMGSQEDAHELLGKLLD----ELKLDLV 98
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
517-639 |
2.34e-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: 56.00 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 517 CGRCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKIGTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 590
Cdd:cd02673 129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2024516673 591 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 639
Cdd:cd02673 191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
534-639 |
6.23e-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: 54.49 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 534 KFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 613
Cdd:cd02665 127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
|
90 100 110
....*....|....*....|....*....|....
gi 2024516673 614 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 639
Cdd:cd02665 194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
479-640 |
1.10e-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: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 479 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscgrckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIGT 558
Cdd:cd02670 65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 559 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 608
Cdd:cd02670 122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024516673 609 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 640
Cdd:cd02670 201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
109-211 |
4.97e-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: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 109 GLKNIGNTCYMNAALQALSNCPPL-THFFLDCGGLARTDKKPAIC------------KS--YLKLMTELW-HKNRPGSVV 172
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024516673 173 PTGLFQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELK 211
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
517-639 |
1.52e-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: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 517 CGRCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKIGTHVSFPLEglDLQPFLAKDSPAQIVTYD 585
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024516673 586 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 639
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
517-621 |
3.27e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 49.96 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024516673 517 CGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 595
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
|
90 100 110
....*....|....*....|....*....|...
gi 2024516673 596 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 621
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
4-37 |
2.58e-05 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 42.35 E-value: 2.58e-05
10 20 30
....*....|....*....|....*....|....
gi 2024516673 4 CTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 37
Cdd:smart00290 17 CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
