|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-519 |
7.01e-65 |
|
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: 215.23 E-value: 7.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 279 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvkr 358
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 359 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTH 438
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 439 VSFPLEGLDLQPFLAKDSPVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 518
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 528943998 519 R 519
Cdd:cd02674 230 E 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1-518 |
1.48e-62 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 211.92 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 1 MNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDA 77
Cdd:pfam00443 12 MNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 78 QEFLRCLMDLLHEELKeqvmeveedpqtimteetmeedksqsdvdfqscescsssdkaenengsrsfsednnettmliqd 157
Cdd:pfam00443 92 QEFLLFLLDGLHEDLN---------------------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 158 dennsemskdwqkekmcnkinkvhsegeldkdrdsvsetadlnnqetvkvqihsraseyitdvhlndlstpqilpsnegv 237
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 238 nprlsasppksgnlwpglppthkkvqsalspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPG 317
Cdd:pfam00443 108 ---------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 318 KEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDELKGDNMYSCE 397
Cdd:pfam00443 155 DSA------------------------------------------------ELKTASLQICFLQFSKLEELDDEEKYYCD 186
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 398 KCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKD---SPVQIVTYDLLSVICHHGT 474
Cdd:pfam00443 187 KCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEElkpKTNNLQDYRLVAVVVHSGS 265
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 528943998 475 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 518
Cdd:pfam00443 266 LSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-522 |
5.78e-39 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 155.04 E-value: 5.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 1 MNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPTTLFQGIKTVNPTFRGYSQ 74
Cdd:COG5560 277 MNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGFKKTIGSFNEEFSGYDQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 75 QDAQEFLRCLMDLLHEELK--------EQVMEVEEDPQTI--MTEETMEEDKSQSD---VD-FQSCEScSSSDKAENENG 140
Cdd:COG5560 356 QDSQEFIAFLLDGLHEDLNriikkpytSKPDLSPGDDVVVkkKAKECWWEHLKRNDsiiTDlFQGMYK-STLTCPGCGSV 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 141 SRSFSEDNNETTMLiqddennsEMSKDWQKekmcnKINKVHSEG-------ELDKDrdsvSETADLNNQETVKVQIHSRA 213
Cdd:COG5560 435 SITFDPFMDLTLPL--------PVSMVWKH-----TIVVFPESGrrqplkiELDAS----STIRGLKKLVDAEYGKLGCF 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 214 SEYITDVHLN---DLSTPQILPSNEGVNPRLSA---SPPKSGNLWPGLpptHKKVQSALSPKRKKQHKKYRSVISD---I 284
Cdd:COG5560 498 EIKVMCIYYGgnyNMLEPADKVLLQDIPQTDFVylyETNDNGIEVPVV---HLRIEKGYKSKRLFGDPFLQLNVLIkasI 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 285 FDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssSHPTSIVKAGSCG----EAYAPQGWIAFFMEYV---- 356
Cdd:COG5560 575 YDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREE--------SSPSSWLKLETEIdtkrEEQVEEEGQMNFNDAVvisc 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 357 ----KR--FVVSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKR 424
Cdd:COG5560 647 eweeKRylSLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 425 FRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPVQIvtYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEV 503
Cdd:COG5560 727 FSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEV 804
|
570
....*....|....*....
gi 528943998 504 SESTVQNAEAYVLFYRKSS 522
Cdd:COG5560 805 DPEDSVTSSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
646-730 |
3.63e-29 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 111.30 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 646 EEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVILRQGADSGQISEETWNFLQSIYGGGPEVI 722
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*...
gi 528943998 723 LRPPVVHV 730
Cdd:smart00695 81 PRKVVCQG 88
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
652-724 |
1.13e-20 |
|
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: 86.65 E-value: 1.13e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528943998 652 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVI---LRQGADSGQISEETWNFLQSIYGGGPEVILR 724
Cdd:pfam06337 3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
374-508 |
1.43e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 90.70 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 374 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 449
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528943998 450 PFLAKD---SPVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 508
Cdd:COG5077 415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
540-609 |
1.25e-15 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 72.39 E-value: 1.25e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528943998 540 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 609
Cdd:smart00695 3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
546-616 |
4.96e-12 |
|
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: 62.00 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 546 FYISRQWLNKFKTFAE-----PGPISNNDFLCihggvPPRKAGYIEDLVL-----MLPQNIWDNLYSRYGGGPAVNHLYI 615
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQEgvdyvIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 528943998 616 C 616
Cdd:pfam06337 80 N 80
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-120 |
7.63e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 45.40 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 1 MNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPTTLFQGIKTVNPTF------RGY 72
Cdd:cd02657 11 LNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQFaekqnqGGY 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 528943998 73 SQQDAQEFLRCLMDLLHEELKEQVME--VEEDPQTIMTEETMEEDKSQSD 120
Cdd:cd02657 89 AQQDAEECWSQLLSVLSQKLPGAGSKgsFIDQLFGIELETKMKCTESPDE 138
|
|
| SEEEED |
pfam14797 |
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ... |
108-215 |
3.07e-04 |
|
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.
Pssm-ID: 434218 [Multi-domain] Cd Length: 111 Bit Score: 41.07 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 108 TEETMEEDKSQSDVDFQScESCSSSDKAENENGSrsfSEDNNETTMLIQDDENNSEmSKDWQKEKMcNKINKVHSEGELD 187
Cdd:pfam14797 7 SESEEEEDSSDSSSDSES-ESGSESEEEGKEGSS---SEDSSEDSSSEQESESGSE-SEKKRTAKR-NSKAKGKSDSEDG 80
|
90 100
....*....|....*....|....*...
gi 528943998 188 KDRDSVSETADLNNQETVKVQIHSRASE 215
Cdd:pfam14797 81 EKKNEKSKTSDSSDTESSSSEESSSDSE 108
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-519 |
7.01e-65 |
|
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: 215.23 E-value: 7.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 279 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvkr 358
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 359 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTH 438
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 439 VSFPLEGLDLQPFLAKDSPVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 518
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 528943998 519 R 519
Cdd:cd02674 230 E 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1-518 |
1.48e-62 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 211.92 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 1 MNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDA 77
Cdd:pfam00443 12 MNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 78 QEFLRCLMDLLHEELKeqvmeveedpqtimteetmeedksqsdvdfqscescsssdkaenengsrsfsednnettmliqd 157
Cdd:pfam00443 92 QEFLLFLLDGLHEDLN---------------------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 158 dennsemskdwqkekmcnkinkvhsegeldkdrdsvsetadlnnqetvkvqihsraseyitdvhlndlstpqilpsnegv 237
Cdd:pfam00443 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 238 nprlsasppksgnlwpglppthkkvqsalspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPG 317
Cdd:pfam00443 108 ---------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 318 KEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDELKGDNMYSCE 397
Cdd:pfam00443 155 DSA------------------------------------------------ELKTASLQICFLQFSKLEELDDEEKYYCD 186
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 398 KCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKD---SPVQIVTYDLLSVICHHGT 474
Cdd:pfam00443 187 KCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEElkpKTNNLQDYRLVAVVVHSGS 265
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 528943998 475 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 518
Cdd:pfam00443 266 LSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
267-519 |
1.30e-55 |
|
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: 191.16 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 267 SPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapq 346
Cdd:cd02257 43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 347 gwiaffmeyvkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQKFPEILCIHLKRFR 426
Cdd:cd02257 97 ------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 427 H-ELMFSTKISTHVSFPLEgLDLQPFLAK-----DSPVQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQS 499
Cdd:cd02257 152 FnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDK 230
|
250 260
....*....|....*....|....*
gi 528943998 500 VTEVSESTVQ-----NAEAYVLFYR 519
Cdd:cd02257 231 VTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
263-518 |
6.13e-49 |
|
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: 175.25 E-value: 6.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 263 QSALSPKRKKQHKKYRSVISD-IFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshpTSIVKAGSCGE 341
Cdd:cd02660 104 THYGGDKNEANDESHCNCIIHqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKS-----------TPSWALGESGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 342 AYAPqgwiaffmeyvkrfvvscvpswfwgpvvTLQDCLAaFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIH 421
Cdd:cd02660 173 SGTP----------------------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 422 LKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPVQIVTYDLLSVICHHGTASSGHYIAYCRNNlNNLW 492
Cdd:cd02660 224 LKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQW 301
|
250 260
....*....|....*....|....*.
gi 528943998 493 YEFDDQSVTEVSESTVQNAEAYVLFY 518
Cdd:cd02660 302 FKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
258-518 |
4.01e-47 |
|
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: 169.38 E-value: 4.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 258 THKKVQSALSPKRKK-----QHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklhssshpts 332
Cdd:cd02661 96 LLDAMQKACLDRFKKlkavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 333 ivkagscgeayapqgwiaffmeyvkrfvvscvpswfwgpVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQ 412
Cdd:cd02661 161 ---------------------------------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIH 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 413 KFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPVQIVTYDLLSVICHHGT-ASSGHYIAYCRnNLNNL 491
Cdd:cd02661 202 RAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGK 276
|
250 260
....*....|....*....|....*..
gi 528943998 492 WYEFDDQSVTEVSESTVQNAEAYVLFY 518
Cdd:cd02661 277 WYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-522 |
5.78e-39 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 155.04 E-value: 5.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 1 MNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPTTLFQGIKTVNPTFRGYSQ 74
Cdd:COG5560 277 MNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGFKKTIGSFNEEFSGYDQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 75 QDAQEFLRCLMDLLHEELK--------EQVMEVEEDPQTI--MTEETMEEDKSQSD---VD-FQSCEScSSSDKAENENG 140
Cdd:COG5560 356 QDSQEFIAFLLDGLHEDLNriikkpytSKPDLSPGDDVVVkkKAKECWWEHLKRNDsiiTDlFQGMYK-STLTCPGCGSV 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 141 SRSFSEDNNETTMLiqddennsEMSKDWQKekmcnKINKVHSEG-------ELDKDrdsvSETADLNNQETVKVQIHSRA 213
Cdd:COG5560 435 SITFDPFMDLTLPL--------PVSMVWKH-----TIVVFPESGrrqplkiELDAS----STIRGLKKLVDAEYGKLGCF 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 214 SEYITDVHLN---DLSTPQILPSNEGVNPRLSA---SPPKSGNLWPGLpptHKKVQSALSPKRKKQHKKYRSVISD---I 284
Cdd:COG5560 498 EIKVMCIYYGgnyNMLEPADKVLLQDIPQTDFVylyETNDNGIEVPVV---HLRIEKGYKSKRLFGDPFLQLNVLIkasI 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 285 FDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssSHPTSIVKAGSCG----EAYAPQGWIAFFMEYV---- 356
Cdd:COG5560 575 YDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREE--------SSPSSWLKLETEIdtkrEEQVEEEGQMNFNDAVvisc 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 357 ----KR--FVVSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKR 424
Cdd:COG5560 647 eweeKRylSLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 425 FRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPVQIvtYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEV 503
Cdd:COG5560 727 FSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEV 804
|
570
....*....|....*....
gi 528943998 504 SESTVQNAEAYVLFYRKSS 522
Cdd:COG5560 805 DPEDSVTSSAYVLFYRRKS 823
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-522 |
1.83e-38 |
|
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: 145.86 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 281 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLaklhssshptsivkagscgeayapqgwiaffmeyvkrfv 360
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 361 vscvpswfwgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKISTH 438
Cdd:cd02659 154 ---------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 439 VSFPLEgLDLQPFLAKDSPVQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 508
Cdd:cd02659 219 FEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDA 297
|
250 260 270
....*....|....*....|....*....|....*.
gi 528943998 509 QNA----------------------EAYVLFYRKSS 522
Cdd:cd02659 298 EEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
278-519 |
2.71e-34 |
|
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: 132.51 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 278 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvk 357
Cdd:cd02667 66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 358 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST-KIS 436
Cdd:cd02667 109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 437 THVSFPlEGLDLQPFLakDSPVQI------VTYDLLSVICHHGTASSGHYIAYCR-NNLNNL------------------ 491
Cdd:cd02667 173 RHVSFP-EILDLAPFC--DPKCNSsedkssVLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagpgs 249
|
250 260 270
....*....|....*....|....*....|
gi 528943998 492 --WYEFDDQSVTEVSESTVQNAEAYVLFYR 519
Cdd:cd02667 250 gqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
281-518 |
1.24e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 125.11 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 281 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklHSSshptsivkagscgeayapqgwiaffmeyvkrfv 360
Cdd:cd02663 109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 361 vscvpswfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS--TKISTH 438
Cdd:cd02663 149 --------------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 439 VSFPLEgldLQPF-LAKDSPVQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTVQN------ 510
Cdd:cd02663 215 VVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAVEEffgdsp 289
|
250
....*....|
gi 528943998 511 --AEAYVLFY 518
Cdd:cd02663 290 nqATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
271-502 |
3.21e-29 |
|
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: 119.06 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 271 KKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshptsivkagscgeayapqgwia 350
Cdd:cd02668 108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 351 ffmeyvkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL- 429
Cdd:cd02668 157 -----------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRk 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528943998 430 -MFSTKISTHVSFPLEgLDLQPFLAkDSPVQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 502
Cdd:cd02668 214 tGAKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
646-730 |
3.63e-29 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 111.30 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 646 EEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVILRQGADSGQISEETWNFLQSIYGGGPEVI 722
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*...
gi 528943998 723 LRPPVVHV 730
Cdd:smart00695 81 PRKVVCQG 88
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
285-518 |
9.67e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 106.68 E-value: 9.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 285 FDGTIISSVQCLTCDRVS-VTLETFQDLSLPIPGKedlaklhSSSHPTsivkagscgeayapqgwiaffmeyvkrfvvsc 363
Cdd:cd02662 56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 364 vpswfwgpvvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKISTHVSFP 442
Cdd:cd02662 97 ----------TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 443 LEgldlqpflakdspVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTE 502
Cdd:cd02662 156 ER-------------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKE 222
|
250
....*....|....*..
gi 528943998 503 VSESTV-QNAEAYVLFY 518
Cdd:cd02662 223 VSESEVlEQKSAYMLFY 239
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-519 |
7.83e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 100.26 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 279 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLpipgkedlaklhssshptsivkagscgeayapqgwiaffmeyvkr 358
Cdd:cd02664 97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 359 fvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFSTKIS 436
Cdd:cd02664 132 ----SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 437 THVSFPL--------EGLDLQPFLAKD---------SPVQIVTYDLLSVICHHGTAS-SGHYIAYCRN------------ 486
Cdd:cd02664 200 DNVSINEvlslpvrvESKSSESPLEKKeeesgddgeLVTRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqecp 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 528943998 487 --------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 519
Cdd:cd02664 280 epkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
278-519 |
4.48e-22 |
|
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: 98.04 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 278 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdLAKLHSSSHPTSIVKAgscgeayapqgwiaffmeyvk 357
Cdd:cd02671 120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 358 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS----- 432
Cdd:cd02671 178 -------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygg 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 433 -TKISTHVSFPlegLDLQPFLAKDSPVQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------T 501
Cdd:cd02671 245 lSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflE 314
|
250
....*....|....*...
gi 528943998 502 EVSESTVQNAEAYVLFYR 519
Cdd:cd02671 315 ALSPNTSSTSTPYLLFYK 332
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
652-724 |
1.13e-20 |
|
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: 86.65 E-value: 1.13e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528943998 652 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVI---LRQGADSGQISEETWNFLQSIYGGGPEVILR 724
Cdd:pfam06337 3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
374-508 |
1.43e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 90.70 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 374 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 449
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528943998 450 PFLAKD---SPVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 508
Cdd:COG5077 415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
415-519 |
3.27e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 80.07 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 415 PEILCIHLKRF--RHELMFSTKISTHVSFPLEgLDLQPFLakdSPVQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 491
Cdd:cd02657 197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270
|
90 100 110
....*....|....*....|....*....|....*
gi 528943998 492 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 519
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
270-519 |
9.66e-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 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: 78.90 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 270 RKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSshptsivkagscgEAYAPqgwi 349
Cdd:cd02658 115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP---- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 350 affmeyvkrfvvscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL 429
Cdd:cd02658 178 -----------------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 430 MF-STKISTHVSFPLEGLDlqpflakdspvqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSE 505
Cdd:cd02658 231 NWvPKKLDVPIDVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQD 297
|
250
....*....|....
gi 528943998 506 STVQNAEAYVLFYR 519
Cdd:cd02658 298 PPEMKKLGYIYFYQ 311
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
540-609 |
1.25e-15 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 72.39 E-value: 1.25e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528943998 540 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 609
Cdd:smart00695 3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
413-520 |
1.65e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.54 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 413 KFPEILCIHLKRFRHELMFsTKISTHVSFPLEgldlQPFL--AKDSPVQIVTYDLLSVICHHGTASSGHYIAYCRNnlNN 490
Cdd:COG5533 178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVKhdQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GG 250
|
90 100 110
....*....|....*....|....*....|...
gi 528943998 491 LWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 520
Cdd:COG5533 251 KWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
371-519 |
1.56e-14 |
|
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: 76.59 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 371 PVVTLQDCLAAFFArdelkgdnmyscEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQP 450
Cdd:cd02669 301 PQVPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSD 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528943998 451 FLAKDSPVQI--VTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 519
Cdd:cd02669 369 YVHFDKPSLNlsTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
546-616 |
4.96e-12 |
|
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: 62.00 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 546 FYISRQWLNKFKTFAE-----PGPISNNDFLCihggvPPRKAGYIEDLVL-----MLPQNIWDNLYSRYGGGPAVNHLYI 615
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQEgvdyvIVPEEVWEFLVEWYGGGPEIKRNVV 79
|
.
gi 528943998 616 C 616
Cdd:pfam06337 80 N 80
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
463-518 |
3.41e-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: 62.12 E-value: 3.41e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528943998 463 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 518
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-518 |
5.53e-09 |
|
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: 57.54 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 396 CEKCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKISTHVSfpleglDLQPFLAKDSpVQIVTYDLLSVICHHG-T 474
Cdd:cd02673 129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDYLK------KNEEIMKKYC-GTDAKYSLVAVICHLGeS 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 528943998 475 ASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 518
Cdd:cd02673 197 PYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
413-518 |
1.36e-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: 56.03 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 413 KFPEILCIHLKRFRHELMFSTKISTHVSFPLEgldlqpflakdspVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 492
Cdd:cd02665 127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
|
90 100 110
....*....|....*....|....*....|....
gi 528943998 493 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 518
Cdd:cd02665 194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
358-519 |
1.35e-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: 53.30 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 358 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscekckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIST 437
Cdd:cd02670 65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 438 HVsFPLEGLDLQPFLAKDSP-------VQIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 487
Cdd:cd02670 122 KI-LIPDEIDIPDFVADDPRacskcqlECRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528943998 488 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 519
Cdd:cd02670 201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-518 |
1.99e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 52.90 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 396 CEKCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKISTHVSFPLEglDLQPFLAKDSPVQIVTYD 464
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528943998 465 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 518
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
396-500 |
5.10e-07 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 52.27 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 396 CEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKISTHVSFPLE-GLDLQPFLAKDSpvQIVTYDLLSVICH-HG 473
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPEiGLTLSDDLQGDN--EIVKYELRGVVVHiGD 271
|
90 100 110
....*....|....*....|....*....|....
gi 528943998 474 TASSGHYIAYCRNNLNNL-------WYEFDDQSV 500
Cdd:pfam13423 272 SGTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-120 |
7.63e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 45.40 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 1 MNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPTTLFQGIKTVNPTF------RGY 72
Cdd:cd02657 11 LNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQFaekqnqGGY 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 528943998 73 SQQDAQEFLRCLMDLLHEELKEQVME--VEEDPQTIMTEETMEEDKSQSD 120
Cdd:cd02657 89 AQQDAEECWSQLLSVLSQKLPGAGSKgsFIDQLFGIELETKMKCTESPDE 138
|
|
| SEEEED |
pfam14797 |
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ... |
108-215 |
3.07e-04 |
|
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.
Pssm-ID: 434218 [Multi-domain] Cd Length: 111 Bit Score: 41.07 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528943998 108 TEETMEEDKSQSDVDFQScESCSSSDKAENENGSrsfSEDNNETTMLIQDDENNSEmSKDWQKEKMcNKINKVHSEGELD 187
Cdd:pfam14797 7 SESEEEEDSSDSSSDSES-ESGSESEEEGKEGSS---SEDSSEDSSSEQESESGSE-SEKKRTAKR-NSKAKGKSDSEDG 80
|
90 100
....*....|....*....|....*...
gi 528943998 188 KDRDSVSETADLNNQETVKVQIHSRASE 215
Cdd:pfam14797 81 EKKNEKSKTSDSSDTESSSSEESSSDSE 108
|
|
| |
