|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
152-683 |
1.01e-68 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 231.18 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 152 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 228
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 229 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 308
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 309 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 388
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 389 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 468
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 469 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfvvscvpswfWGPVVTLQDCLAAFF 548
Cdd:pfam00443 144 PFSDLSLPIPGDSA---------------------------------------------------ELKTASLQICFLQFS 172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 549 ARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV-- 626
Cdd:pfam00443 173 KLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnl 251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2201694637 627 -TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 683
Cdd:pfam00443 252 qDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-684 |
1.63e-60 |
|
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: 205.60 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 441 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 520
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 521 cfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKI 600
Cdd:cd02674 82 ---------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 601 GTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYV 680
Cdd:cd02674 147 TTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYI 226
|
....
gi 2201694637 681 LFYR 684
Cdd:cd02674 227 LFYE 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
147-687 |
2.10e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 176.23 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 147 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 220
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 221 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 300
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 301 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWqKEKISSNKLNRANSMEDLEKDTNSTSEAnefLNNQGT 367
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVW-KHTIVVFPESGRRQPLKIELDASSTIRG---LKKLVD 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 368 VKVQIHSRFSEYINDVHMNDVSGAqtlsSNEGTNTRLSSSPPKSCTSCSSSTPIHKKVSTVSSPKRKKCKKYRsVISDIF 447
Cdd:COG5560 489 AEYGKLGCFEIKVMCIYYGGNYNM----LEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVHLRIEKGYKSKR-LFGDPF 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 448 DGTIISSVQCLTCDRLSVTLETFQDLSLpipGKEDLAKLHSashQTSLVKTGScgeayAPQGWIAFFMEYFKRCF----- 522
Cdd:COG5560 564 LQLNVLIKASIYDKLVKEFEELLVLVEM---KKTDVDLVSE---QVRLLREES-----SPSSWLKLETEIDTKREeqvee 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 523 --------RFVVSCV-------------PSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCK 575
Cdd:COG5560 633 egqmnfndAVVISCEweekrylslfsydPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQME 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 576 VQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLN 654
Cdd:COG5560 713 LWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFAN 790
|
570 580 590
....*....|....*....|....*....|...
gi 2201694637 655 NLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 687
Cdd:COG5560 791 NGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
811-892 |
4.95e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.13 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 811 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 887
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2201694637 888 HRPPV 892
Cdd:smart00695 81 PRKVV 85
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
815-889 |
3.63e-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: 3.63e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201694637 815 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 889
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
30-90 |
4.56e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 4.56e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201694637 30 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148 1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
703-785 |
1.04e-16 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.86 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 703 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 776
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2201694637 777 HLYVCHTCQ 785
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
711-781 |
5.64e-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: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 711 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 780
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2201694637 781 C 781
Cdd:pfam06337 80 N 80
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-81 |
3.87e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.14 E-value: 3.87e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2201694637 29 SCQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 81
Cdd:smart00290 1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
152-683 |
1.01e-68 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 231.18 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 152 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 228
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 229 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 308
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 309 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 388
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 389 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 468
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 469 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfvvscvpswfWGPVVTLQDCLAAFF 548
Cdd:pfam00443 144 PFSDLSLPIPGDSA---------------------------------------------------ELKTASLQICFLQFS 172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 549 ARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV-- 626
Cdd:pfam00443 173 KLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnl 251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2201694637 627 -TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 683
Cdd:pfam00443 252 qDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-684 |
1.63e-60 |
|
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: 205.60 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 441 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 520
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 521 cfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKI 600
Cdd:cd02674 82 ---------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 601 GTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYV 680
Cdd:cd02674 147 TTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYI 226
|
....
gi 2201694637 681 LFYR 684
Cdd:cd02674 227 LFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
429-684 |
5.51e-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: 182.68 E-value: 5.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 429 SSPKRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapq 508
Cdd:cd02257 43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 509 gwiaffmeyfkrcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKlRNGVKFCKVQKFPEILCIHLK 588
Cdd:cd02257 97 ---------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 589 RFRH-ELMFSTKIGTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFD 661
Cdd:cd02257 149 RFSFnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFN 227
|
250 260
....*....|....*....|....*...
gi 2201694637 662 DQSVTEVSESTVQ-----NAEAYVLFYR 684
Cdd:cd02257 228 DDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-683 |
1.57e-45 |
|
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: 166.78 E-value: 1.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 442 VISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSASHQTSLVktgscgeayapqgwiaffmeyfkrc 521
Cdd:cd02660 122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTP------------------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 522 frfvvscvpswfwgpvvTLQDCLAaFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM-FSTKI 600
Cdd:cd02660 177 -----------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 601 GTHVSFPLEgLDLQPFLA--------KDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSEST 672
Cdd:cd02660 239 DTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEE 316
|
250
....*....|.
gi 2201694637 673 VQNAEAYVLFY 683
Cdd:cd02660 317 VLKSQAYLLFY 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
147-687 |
2.10e-45 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 176.23 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 147 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 220
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 221 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 300
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 301 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWqKEKISSNKLNRANSMEDLEKDTNSTSEAnefLNNQGT 367
Cdd:COG5560 413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVW-KHTIVVFPESGRRQPLKIELDASSTIRG---LKKLVD 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 368 VKVQIHSRFSEYINDVHMNDVSGAqtlsSNEGTNTRLSSSPPKSCTSCSSSTPIHKKVSTVSSPKRKKCKKYRsVISDIF 447
Cdd:COG5560 489 AEYGKLGCFEIKVMCIYYGGNYNM----LEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVHLRIEKGYKSKR-LFGDPF 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 448 DGTIISSVQCLTCDRLSVTLETFQDLSLpipGKEDLAKLHSashQTSLVKTGScgeayAPQGWIAFFMEYFKRCF----- 522
Cdd:COG5560 564 LQLNVLIKASIYDKLVKEFEELLVLVEM---KKTDVDLVSE---QVRLLREES-----SPSSWLKLETEIDTKREeqvee 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 523 --------RFVVSCV-------------PSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCK 575
Cdd:COG5560 633 egqmnfndAVVISCEweekrylslfsydPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQME 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 576 VQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLN 654
Cdd:COG5560 713 LWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFAN 790
|
570 580 590
....*....|....*....|....*....|...
gi 2201694637 655 NLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 687
Cdd:COG5560 791 NGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
427-683 |
4.96e-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: 161.67 E-value: 4.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 427 TVSSPKRKKCKKY------RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGkedlaklhsashqtslvktgs 500
Cdd:cd02661 102 KACLDRFKKLKAVdpssqeTTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 501 cgeayapqgwiaffmeyfkrcfrfvvscvpswfwgpVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFP 580
Cdd:cd02661 161 ------------------------------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 581 EILCIHLKRFrhELMFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRnNLNNLWYE 659
Cdd:cd02661 205 NVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYN 279
|
250 260
....*....|....*....|....
gi 2201694637 660 FDDQSVTEVSESTVQNAEAYVLFY 683
Cdd:cd02661 280 MDDSKVSPVSIETVLSQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-687 |
2.61e-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: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 443 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLaklhsashqtslvktgscgeayapqgwiaffmeyfkrcf 522
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 523 rfvvscvpswfwgpvvtlQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKI 600
Cdd:cd02659 154 ------------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 601 GTHVSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSE 670
Cdd:cd02659 216 NDRFEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDP 294
|
250 260 270
....*....|....*....|....*....|....*....
gi 2201694637 671 STVQNA----------------------EAYVLFYRKSN 687
Cdd:cd02659 295 NDAEEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
440-684 |
2.53e-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: 121.34 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 440 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfk 519
Cdd:cd02667 66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 520 rcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST- 598
Cdd:cd02667 109 ----------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLr 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 599 KIGTHVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL------------- 656
Cdd:cd02667 170 KVSRHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaade 244
|
250 260 270
....*....|....*....|....*....|....*
gi 2201694637 657 -------WYEFDDQSVTEVSESTVQNAEAYVLFYR 684
Cdd:cd02667 245 agpgsgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
435-683 |
2.32e-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: 113.17 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 435 KCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPgkedlaklhsashqtslvktgscgeayapqgwiaff 514
Cdd:cd02663 101 NAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE------------------------------------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 515 meyfkrcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL 594
Cdd:cd02663 145 ---------------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 595 MFS--TKIGTHVSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSE 670
Cdd:cd02663 204 QLNryIKLFYRVVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDE 278
|
250 260
....*....|....*....|.
gi 2201694637 671 STVQN--------AEAYVLFY 683
Cdd:cd02663 279 NAVEEffgdspnqATAYVLFY 299
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
811-892 |
4.95e-27 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 105.13 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 811 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 887
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*
gi 2201694637 888 HRPPV 892
Cdd:smart00695 81 PRKVV 85
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
437-667 |
1.68e-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: 111.36 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 437 KKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffme 516
Cdd:cd02668 112 PDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK----------------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 517 yfkrcfrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL-- 594
Cdd:cd02668 157 ----------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRkt 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201694637 595 MFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 667
Cdd:cd02668 215 GAKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-683 |
3.59e-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: 99.36 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 447 FDGTIISSVQCLTCDRLS-VTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffmeyfkrcfrfv 525
Cdd:cd02662 56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQS-------------------------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 526 vscvpswfWGPVVTLQDCLAAFFARDELKGdnmYSCGRCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKIGTHV 604
Cdd:cd02662 92 --------SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 605 SFPLegldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQS 664
Cdd:cd02662 153 SFPE-------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTT 219
|
250 260
....*....|....*....|
gi 2201694637 665 VTEVSESTV-QNAEAYVLFY 683
Cdd:cd02662 220 VKEVSESEVlEQKSAYMLFY 239
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
815-889 |
3.63e-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: 3.63e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201694637 815 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 889
Cdd:pfam06337 1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-684 |
3.78e-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: 92.55 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 441 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLpipgkedlaklhsashqtslvktgscgeayapqgwiaffmeyfkr 520
Cdd:cd02664 97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 521 cfrfvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFST 598
Cdd:cd02664 132 -------SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 599 KIGTHVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN-------- 651
Cdd:cd02664 197 KIMDNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstg 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2201694637 652 ------------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 684
Cdd:cd02664 276 qecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
440-684 |
1.52e-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: 90.72 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 440 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdLAKLHSASHQTSLVKTgscgeayapqgwiaffmeyfk 519
Cdd:cd02671 120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 520 rcfrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS-- 597
Cdd:cd02671 178 ----------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdc 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 598 ----TKIGTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV------- 665
Cdd:cd02671 242 ygglSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekd 311
|
250 260
....*....|....*....|.
gi 2201694637 666 --TEVSESTVQNAEAYVLFYR 684
Cdd:cd02671 312 flEALSPNTSSTSTPYLLFYK 332
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
539-673 |
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 2201694637 539 TLQDCLAAFFARDELKGDNMYSCGR--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KIGTHVSFPLEgLDLQ 614
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201694637 615 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 673
Cdd:COG5077 415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
30-90 |
4.56e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 4.56e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201694637 30 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148 1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
703-785 |
1.04e-16 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 75.86 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 703 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 776
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
....*....
gi 2201694637 777 HLYVCHTCQ 785
Cdd:smart00695 79 PIPRKVVCQ 87
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
580-684 |
3.71e-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: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 580 PEILCIHLKRF--RHELMFSTKIGTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 656
Cdd:cd02657 197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270
|
90 100 110
....*....|....*....|....*....|....*
gi 2201694637 657 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 684
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
578-685 |
2.94e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.15 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 578 KFPEILCIHLKRFRHELMFsTKIGTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlN 654
Cdd:COG5533 178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--G 249
|
90 100 110
....*....|....*....|....*....|....
gi 2201694637 655 NLWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 685
Cdd:COG5533 250 GKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
563-684 |
3.77e-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: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 563 RCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT- 639
Cdd:cd02669 316 TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTp 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2201694637 640 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 684
Cdd:cd02669 396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
711-781 |
5.64e-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: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 711 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 780
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 2201694637 781 C 781
Cdd:pfam06337 80 N 80
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-684 |
8.14e-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: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 443 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSAshqtslvktgscgEAYAPqgwiaffmeyfkrcf 522
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP--------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 523 rfvvscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMF-STKIG 601
Cdd:cd02658 178 ---------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 602 THVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSESTVQNAEA 678
Cdd:cd02658 239 VPIDVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKLG 305
|
....*.
gi 2201694637 679 YVLFYR 684
Cdd:cd02658 306 YIYFYQ 311
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
153-281 |
7.65e-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: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 153 GLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKNRPgsVVPTGLFQGIKSVNPT 230
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 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 ... |
628-683 |
3.16e-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: 3.16e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201694637 628 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 683
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-81 |
3.87e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.14 E-value: 3.87e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2201694637 29 SCQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 81
Cdd:smart00290 1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
153-259 |
6.93e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 57.89 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 153 GLKNIGNTCYMNAALQALS-NCPPLTHFFLDCGGLART-------DKKPAICKSYLKLMTELWHKNRPgsvvptglfqgi 224
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
|
90 100 110
....*....|....*....|....*....|....*
gi 2201694637 225 kSVNPTFRGYSQQDAQEFLRCLMDllheELKEPIV 259
Cdd:COG5533 69 -KVGWIPPMGSQEDAHELLGKLLD----ELKLDLV 98
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
561-683 |
3.12e-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: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 561 CGRCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKIGTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 634
Cdd:cd02673 129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2201694637 635 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 683
Cdd:cd02673 191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
578-683 |
6.60e-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: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 578 KFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 657
Cdd:cd02665 127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
|
90 100 110
....*....|....*....|....*....|....
gi 2201694637 658 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 683
Cdd:cd02665 194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
523-684 |
1.13e-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: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 523 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscgrckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIGT 602
Cdd:cd02670 65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 603 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 652
Cdd:cd02670 122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2201694637 653 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 684
Cdd:cd02670 201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
153-255 |
5.28e-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: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 153 GLKNIGNTCYMNAALQALSNCPPL-THFFLDCGGLARTDKKPAIC------------KS--YLKLMTELW-HKNRPGSVV 216
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2201694637 217 PTGLFQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELK 255
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
561-683 |
1.69e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 50.59 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 561 CGRCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKIGTHVSFPLEglDLQPFLAKDSPAQIVTYD 629
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2201694637 630 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 683
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
561-665 |
3.80e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 49.96 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201694637 561 CGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 639
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
|
90 100 110
....*....|....*....|....*....|...
gi 2201694637 640 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 665
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
|
|
| |
