|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
541-918 |
5.21e-49 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 176.09 E-value: 5.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 541 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 620
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 621 PGAAFEPTYIYRLLTVIKSSLSeKGRQEDAEEYLGFILNGLHEEMlslkkllspthekhsvsngpgshliedeeledtge 700
Cdd:pfam00443 63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 701 gsedewEQVGPKNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 775
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 776 LVARESVQGYTT----KTKQEVEVSRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLVKNIEYPVDLEISReLLSPGvKNKN 851
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLSR-YLAEE-LKPK 247
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672085227 852 FKCHRTYRLFAVVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVRPSadrTAYLLYY 918
Cdd:pfam00443 248 TNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS---SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
646-919 |
7.72e-49 |
|
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: 173.82 E-value: 7.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 646 RQEDAEEYLGFILNGLHEEMLSLKKLLSPTHEKHSVsngpgshliedeeledtgegsedeweqvgpknktsvtrqadfvq 725
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 726 tpITGIFGGHIRSVVYQQS---SKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQG---YTTKTKQEVEVSRRV 799
Cdd:cd02257 57 --IHDLFGGKLESTIVCLEcghESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 800 TLEKLPPVLVLHLKRFVYEKTGGCQKLVKNIEYPVDLEISRELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTD 879
Cdd:cd02257 135 KIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672085227 880 VFQIGLNGWLRIDDQTVKVINQYQVVRPSADR-TAYLLYYR 919
Cdd:cd02257 215 VKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSsSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
540-918 |
2.28e-40 |
|
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: 151.27 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 540 PRGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRPCtstpmidsFVRLMNEFTNmpvppkprQALgdkivR 617
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLanYLLSREHSKDCCNEGFC--------MMCALEAHVE--------RAL-----A 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 618 DIRPGAAfePTYIYRLLTVIKSSLSeKGRQEDAEEYLGFILNGLHEEMLSLKKLLSPTHEkhsvsngpgshliedeeled 697
Cdd:cd02661 60 SSGPGSA--PRIFSSNLKQISKHFR-IGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDP-------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 698 tgegsedeweqvgPKNKTSVTRQadfvqtpitgIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKirTVQDALESL 776
Cdd:cd02661 117 -------------SSQETTLVQQ----------IFGGYLRSqVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQF 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 777 VARESVQG----YTTKTKQEVEVSRRVTLEKLPPVLVLHLKRFvYEKTGGcqKLVKNIEYPVDLEisrelLSPGVKNKNf 852
Cdd:cd02661 172 TKPEQLDGenkyKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-SNFRGG--KINKQISFPETLD-----LSPYMSQPN- 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672085227 853 KCHRTYRLFAVVYHHGNSATGGHYTTDVfqIGLNG-WLRIDDQTVKVINQYQVVRpsadRTAYLLYY 918
Cdd:cd02661 243 DGPLKYKLYAVLVHSGFSPHSGHYYCYV--KSSNGkWYNMDDSKVSPVSIETVLS----QKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
541-918 |
1.12e-33 |
|
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: 132.50 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 541 RGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRP--CTSTPMidsfvrlmneftnmpvppkprqalgDKIV 616
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLrnYFLSDRHSCTCLSCSPnsCLSCAM-------------------------DEIF 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 617 RDIRPGAAFEPTYIYRLLT---VIKSSLSEKGrQEDAEEYLGFILNGLHEEMLSLKKLLSPTHEkhsvsngpgshliede 693
Cdd:cd02660 56 QEFYYSGDRSPYGPINLLYlswKHSRNLAGYS-QQDAHEFFQFLLDQLHTHYGGDKNEANDESH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 694 eledtgegsedeweqvgpknktsvtrqadfVQTPITGIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKIR----- 767
Cdd:cd02660 119 ------------------------------CNCIIHQTFSGSLQSsVTCQRCGGVSTTVDPFLDLSLDIPNKSTPswalg 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 768 --------TVQDALESLVARESVQGYTTKT---KQEVEVSRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLVKNIEYPVDL 836
Cdd:cd02660 169 esgvsgtpTLSDCLDRFTRPEKLGDFAYKCsgcGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLEL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 837 EIsRELLSPGVKNKNFKCHR----TYRLFAVVYHHGNSATgGHYTTDVfQIGLNGWLRIDDQTVKVINQYQVVRPSadrt 912
Cdd:cd02660 249 NM-TPYTSSSIGDTQDSNSLdpdyTYDLFAVVVHKGTLDT-GHYTAYC-RQGDGQWFKFDDAMITRVSEEEVLKSQ---- 321
|
....*.
gi 672085227 913 AYLLYY 918
Cdd:cd02660 322 AYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
728-919 |
3.53e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 110.84 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 728 ITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDI-----QSDKIrTVQDALESLVARESVQG----YTTKTKQEVEVSR 797
Cdd:cd02674 40 IVDLFQGQLKSRLTcLTCGKTSTTFEPFTYLSLPIpsgsgDAPKV-TLEDCLRLFTKEETLDGdnawKCPKCKKKRKATK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 798 RVTLEKLPPVLVLHLKRFVYEKTGGcQKLVKNIEYPV-DLeisreLLSPGVKNKNFKCHRTYRLFAVVYHHGnSATGGHY 876
Cdd:cd02674 119 KLTISRLPKVLIIHLKRFSFSRGST-RKLTTPVTFPLnDL-----DLTPYVDTRSFTGPFKYDLYAVVNHYG-SLNGGHY 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 672085227 877 TTDVFQIGLNGWLRIDDQTVKVINqyqvVRPSADRTAYLLYYR 919
Cdd:cd02674 192 TAYCKNNETNDWYKFDDSRVTKVS----ESSVVSSSAYILFYE 230
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-918 |
6.46e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 97.38 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQALVacppmyhlmkFIPLYSkvqrpCTSTpmidsfvrLMNEFTNmpvppkprqalGDKIVRDIRP 621
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----------FENLLT-----CLKD--------LFESISE-----------QKKRTGVISP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 622 gaafeptyiYRLLTVIKSS--LSEKGRQEDAEEYLGFILNGLHEemlslkkllspthekhsvsngpgshLIEDEeledtg 699
Cdd:cd02663 47 ---------KKFITRLKREneLFDNYMHQDAHEFLNFLLNEIAE-------------------------ILDAE------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 700 egSEDEWEQVGPKNKTSVTRQADFVQTPITGIFGGHIR-----SVvyqqSSKEsatlQPFFTLQLDIQSDKirTVQDALE 774
Cdd:cd02663 87 --RKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRcltceTV----SSRD----ETFLDLSIDVEQNT--SITSCLR 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 775 SLVARESVQGY------TTKTKQEVEvsRRVTLEKLPPVLVLHLKRFVY-EKTGGCQKLVKNIEYPVDLEisrellspgV 847
Cdd:cd02663 155 QFSATETLCGRnkfycdECCSLQEAE--KRMKIKKLPKILALHLKRFKYdEQLNRYIKLFYRVVFPLELR---------L 223
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672085227 848 KNKNFKCH---RTYRLFAVVYHHGNSATGGHYTTdVFQIGlNGWLRIDDQTVKVINQYQVVRPSADR----TAYLLYY 918
Cdd:cd02663 224 FNTTDDAEnpdRLYELVAVVVHIGGGPNHGHYVS-IVKSH-GGWLLFDDETVEKIDENAVEEFFGDSpnqaTAYVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
728-922 |
7.74e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 88.85 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 728 ITGIFGGHIrsvVYQQSSKE----SATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG----YTTKTKQEVEVSRRV 799
Cdd:cd02659 113 IKNLFGGKL---VNYIICKEcpheSEREEYFLDLQVAVKGKK--NLEESLDAYVQGETLEGdnkyFCEKCGKKVDAEKGV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 800 TLEKLPPVLVLHLKRFVYEKTGGC-QKLVKNIEYPVDLEISRElLSPGVKNKNFKCHR------TYRLFAVVYHHGnSAT 872
Cdd:cd02659 188 CFKKLPPVLTLQLKRFEFDFETMMrIKINDRFEFPLELDMEPY-TEKGLAKKEGDSEKkdsesyIYELHGVLVHSG-DAH 265
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672085227 873 GGHYTTDVFQIGLNGWLRIDDQTVKVINQ----------------YQVVRPSADRT--AYLLYYRRVD 922
Cdd:cd02659 266 GGHYYSYIKDRDDGKWYKFNDDVVTPFDPndaeeecfggeetqktYDSGPRAFKRTtnAYMLFYERKS 333
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-919 |
1.42e-18 |
|
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: 87.39 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQALVACPPMyhlmKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNM-----PVPPKP-RQALGDKI 615
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPEL----RDALKNYNPARRGANQSSDNLTNALRDLFDTMdkkqePVPPIEfLQLLRMAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 616 vrdirpgaafePTYIYRlltviksslSEKG--RQEDAEEYLGFILNGLHEEmLSLKKLLSPTHEKHSVsngpgshlIEDE 693
Cdd:cd02657 77 -----------PQFAEK---------QNQGgyAQQDAEECWSQLLSVLSQK-LPGAGSKGSFIDQLFG--------IELE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 694 ELEDTGEGSEDEWEQVGPKNKTSVtrqADFVQTPITGIFGGhIRSVVYQQSSKESATLQpfftlqldiqsdkirtvQDAL 773
Cdd:cd02657 128 TKMKCTESPDEEEVSTESEYKLQC---HISITTEVNYLQDG-LKKGLEEEIEKHSPTLG-----------------RDAI 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 774 eslvaresvqgYTTKTKqeveVSRrvtlekLPPVLVLHLKRFVY-EKTGGCQKLVKNIEYPVDLEISrELLSP-GVknkn 851
Cdd:cd02657 187 -----------YTKTSR----ISR------LPKYLTVQFVRFFWkRDIQKKAKILRKVKFPFELDLY-ELCTPsGY---- 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672085227 852 fkchrtYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVRPSA---DRTAYLLYYR 919
Cdd:cd02657 241 ------YELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGggdWHIAYILLYK 305
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-919 |
7.66e-17 |
|
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: 83.02 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQALVACPPMYHLMKFipLYSKVQrpcTSTPMIDSFVRLMNEFTNMPVPPKPRQALgdKIVRDIrp 621
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKH--LVSLIS---SVEQLQSSFLLNPEKYNDELANQAPRRLL--NALREV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 622 gaafEPTYiyrlltviksslsEKGRQEDAEEYLGFILNglheemlSLKKLLSPTHEKHSVSNgpgSHLIEDEELEDTGEG 701
Cdd:cd02671 97 ----NPMY-------------EGYLQHDAQEVLQCILG-------NIQELVEKDFQGQLVLR---TRCLECETFTERRED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 702 SEDeweqvgpknkTSVTrqadfvqTPITGIFGGHIRSVVYQQSSKESATLQpfFTLQLDIQSDKIRTvqdalESLVARES 781
Cdd:cd02671 150 FQD----------ISVP-------VQESELSKSEESSEISPDPKTEMKTLK--WAISQFASVERIVG-----EDKYFCEN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 782 VQGYTtktkqevEVSRRVTLEKLPPVLVLHLKRF-----VYEKTGGCQKLvkNIEYPVDLEISRELLSPGVKNKnfkchr 856
Cdd:cd02671 206 CHHYT-------EAERSLLFDKLPEVITIHLKCFaangsEFDCYGGLSKV--NTPLLTPLKLSLEEWSTKPKND------ 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672085227 857 TYRLFAVVYHHGNSATGGHYTTDVfqiglnGWLRIDDQTVKVINQYQVVRP-SADR----TAYLLYYR 919
Cdd:cd02671 271 VYRLFAVVMHSGATISSGHYTAYV------RWLLFDDSEVKVTEEKDFLEAlSPNTsstsTPYLLFYK 332
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
747-919 |
7.75e-17 |
|
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: 82.85 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 747 ESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQ-EVEVSRRVTLEKLPPVLVLHLKRFVYE-KTG 821
Cdd:cd02668 138 ESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGdnqYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDrKTG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 822 GCQKLVKNIEYPVDLEISRELLSpgvKNKNFkchRTYRLFAVVYHHGNSATGGHYTTDV--FQIGLngWLRIDDQTVK-- 897
Cdd:cd02668 216 AKKKLNASISFPEILDMGEYLAE---SDEGS---YVYELSGVLIHQGVSAYSGHYIAHIkdEQTGE--WYKFNDEDVEem 287
|
170 180 190
....*....|....*....|....*....|....*..
gi 672085227 898 --------VINQYQVVRPSAD-------RTAYLLYYR 919
Cdd:cd02668 288 pgkplklgNSEDPAKPRKSEIkkgthssRTAYMLVYK 324
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
722-919 |
1.45e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 78.20 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 722 DFVQTPITGIFGGHIRSVVYQQSSKE-SATLQPFFTLQLDI--QSDKIRTVQDALESLVARESVQG---YTTKTKQEVEV 795
Cdd:cd02667 63 DGLRTFIDSIFGGELTSTIMCESCGTvSLVYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGnnkFACENCTKAKK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 796 SRRVTleKLPPVLVLHLKRFVYEKTGGCQKLVKNIEYPVDLEISrELLSPGVKNKNFKCHRTYRLFAVVYHHGnSATGGH 875
Cdd:cd02667 143 QYLIS--KLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLA-PFCDPKCNSSEDKSSVLYRLYGVVEHSG-TMRSGH 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672085227 876 YTTDVF-----QIGLNGWLRIDDQTVKVINQYQ-------VVRPSADRT-----AYLLYYR 919
Cdd:cd02667 219 YVAYVKvrppqQRLSDLTKSKPAADEAGPGSGQwyyisdsDVREVSLEEvlkseAYLLFYE 279
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-878 |
8.62e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 73.68 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQAL-VACPPMYHLMKFIPLYSKvqrpCTSTPMidsfVRLMNEFTNMPVPPKPRQALGDKIVRDIR 620
Cdd:cd02664 1 GLINLGNTCYMNSVLQALfMAKDFRRQVLSLNLPRLG----DSQSVM----KKLQLLQAHLMHTQRRAEAPPDYFLEASR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 621 PgAAFEPtyiyrlltviksslsekGRQEDAEEYLGFILNGLHeemlslkkllspthekhsvsngpgshliedeeledtge 700
Cdd:cd02664 73 P-PWFTP-----------------GSQQDCSEYLRYLLDRLH-------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 701 gsedeweqvgpknktsvtrqadfvqTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSdkirtVQDALESLVAR 779
Cdd:cd02664 97 -------------------------TLIEKMFGGKLSTTIRcLNCNSTSARTERFRDLDLSFPS-----VQDLLNYFLSP 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 780 ESVQG----YTTKTKQEVEVSRRVTLEKLPPVLVLHLKRFVYE-KTGGCQKLVKNIEYPVDLEI-----SRELLSPGVKN 849
Cdd:cd02664 147 EKLTGdnqyYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDqKTHVREKIMDNVSINEVLSLpvrveSKSSESPLEKK 226
|
330 340 350
....*....|....*....|....*....|....*..
gi 672085227 850 KNFK------CHRT--YRLFAVVYHHGNSATGGHYTT 878
Cdd:cd02664 227 EEESgddgelVTRQvhYRLYAVVVHSGYSSESGHYFT 263
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
722-924 |
1.26e-13 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 75.29 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 722 DFVQTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQEVEVSR 797
Cdd:COG5077 294 TVVENALNGIFVGKMKSYIKcVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGdnrYNAEKHGLQDAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 798 RVTLEKLPPVLVLHLKRFVYE-KTGGCQKLVKNIEYPVDLEISrELLSPGVKNKNFKCHrTYRLFAVVYHHGNSATGGHY 876
Cdd:COG5077 372 GVIFESLPPVLHLQLKRFEYDfERDMMVKINDRYEFPLEIDLL-PFLDRDADKSENSDA-VYVLYGVLVHSGDLHEGHYY 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672085227 877 TtdVFQIGLNG-WLRIDDQTVKVINQYQVV-------RPSADR-----------TAYLLYYRRVDLL 924
Cdd:COG5077 450 A--LLKPEKDGrWYKFDDTRVTRATEKEVLeenfggdHPYKDKirdhsgikrfmSAYMLVYLRKSML 514
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-919 |
2.15e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 71.97 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQALVACPPM---YHLMKFIPlYSKVQRPCTS--TPMIDSFVRLMNEFTNMPVPPKPRQalgDKIV 616
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwrYDDLENKF-PSDVVDPANDlnCQLIKLADGLLSGRYSKPASLKSEN---DPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 617 RDIRPgAAFEptyiyrllTVIKSSLSE--KGRQEDAEEYLGFILNGLHEEmlSLKKLLSPTHEKHSVsngpgshLIEDEe 694
Cdd:cd02658 77 VGIKP-SMFK--------ALIGKGHPEfsTMRQQDALEFLLHLIDKLDRE--SFKNLGLNPNDLFKF-------MIEDR- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 695 LEDTGegsedeweqvgpKNKTSVTRQAD-FVQTPItgifgghirsvvyqqsSKESATLQPFFTLQLDIQsdkirTVQDAL 773
Cdd:cd02658 138 LECLS------------CKKVKYTSELSeILSLPV----------------PKDEATEKEEGELVYEPV-----PLEDCL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 774 ESLVARESVQGYTTKTKQEVEVSRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLVKNIEYPvdleisrELLSPGvknknfk 853
Cdd:cd02658 185 KAYFAPETIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVP-------EELGPG------- 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672085227 854 chrTYRLFAVVYHHGNSATGGHYTTDVFQ--IGLNGWLRIDDQTVkvinqYQVVRPSADR-TAYLLYYR 919
Cdd:cd02658 251 ---KYELIAFISHKGTSVHSGHYVAHIKKeiDGEGKWVLFNDEKV-----VASQDPPEMKkLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-918 |
2.02e-12 |
|
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: 67.78 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQALVACPpmyhlmkfiplyskvqrpctstpmidSFVRLMNEFTNmpvppkprqalgdkivrdirp 621
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP--------------------------SLIEYLEEFLE--------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 622 gaafeptyiyrlltviksslsekgrQEDAEEYLgfilnglheemlslkkllspthekhsvsngpgSHLIEdeeledtgeg 701
Cdd:cd02662 34 -------------------------QQDAHELF--------------------------------QVLLE---------- 46
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 702 sedEWEQVgpknktsvtrqadfVQTPITGIFgghIRSVVYQQSSKESATLQPFFT-LQLDIQSDKIR---TVQDALESLV 777
Cdd:cd02662 47 ---TLEQL--------------LKFPFDGLL---ASRIVCLQCGESSKVRYESFTmLSLPVPNQSSGsgtTLEHCLDDFL 106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 778 ARESVQGYTTKTKQEVEVsrrvtleKLPPVLVLHLKRFVYEKTGGCQKLVKNIEYPvdleisrELLSpgvknknfkcHRT 857
Cdd:cd02662 107 STEIIDDYKCDRCQTVIV-------RLPQILCIHLSRSVFDGRGTSTKNSCKVSFP-------ERLP----------KVL 162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 858 YRLFAVVYHHGnSATGGHYTT-----------DVFQIGL---------NGWLRIDDQTVKVINQYQVVrpsADRTAYLLY 917
Cdd:cd02662 163 YRLRAVVVHYG-SHSSGHYVCyrrkplfskdkEPGSFVRmregpsstsHPWWRISDTTVKEVSESEVL---EQKSAYMLF 238
|
.
gi 672085227 918 Y 918
Cdd:cd02662 239 Y 239
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
542-900 |
2.03e-12 |
|
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: 70.43 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 542 GLINKGNWCYINATLQALVACPPM--YHLMKfiPLYSKVQRPCTstPMIDSFVRLMNEFTNmpvppkPRQalgdkIVRDI 619
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIrnFFLLY--ENYENIKDRKS--ELVKRLSELIRKIWN------PRN-----FKGHV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 620 RPgaafeptyiYRLLTVIkSSLSEK----GRQEDAEEYLGFILNGLHeemLSLKKllspthekhsvSNGPGSHLIEDEEL 695
Cdd:cd02669 186 SP---------HELLQAV-SKVSKKkfsiTEQSDPVEFLSWLLNTLH---KDLGG-----------SKKPNSSIIHDCFQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 696 edtGEgSEDEWEQVGPKNKTSVTRQADFVQTpitgifgghirsvvYQQSSKESatlqPFFTLQLDI---------QSDKI 766
Cdd:cd02669 242 ---GK-VQIETQKIKPHAEEEGSKDKFFKDS--------------RVKKTSVS----PFLLLTLDLpppplfkdgNEENI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 767 rTVQDALESLVAResvqgYTTKTKQEV-EVSRRVTLEKLPPVLVLHLKRF-----VYEKTggcQKLVkniEYPVDLEISR 840
Cdd:cd02669 300 -IPQVPLKQLLKK-----YDGKTETELkDSLKRYLISRLPKYLIFHIKRFsknnfFKEKN---PTIV---NFPIKNLDLS 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 841 ELLSPGVKNKNFkcHRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVIN 900
Cdd:cd02669 368 DYVHFDKPSLNL--STKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVL 425
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
705-918 |
1.74e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 64.89 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 705 EWEQVGPKNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSsKESATLQPFFtlQLDIQSDKIRTVQDALESLVARESVQG 784
Cdd:cd02665 34 DWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG-KPFCNCETFG--QYPLQVNGYGNLHECLEAAMFEGEVEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 785 ytTKTKQEVEVSRRVTLEKLPPVLVLHLKRFVYEKTGGCqKLVKNIEYPVDLEisrellspgvknknfkcHRTYRLFAVV 864
Cdd:cd02665 111 --LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE-KIHDKLEFPQIIQ-----------------QVPYELHAVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 672085227 865 YHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVRPS----ADRTAYLLYY 918
Cdd:cd02665 171 VHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggRNPSAYCLMY 227
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
655-920 |
2.44e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 67.60 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 655 GFILNGLHEEMLSLKKLLS--PT-----HEKHSVSN---GPGSHLIEDEELEDTGEGSEDEWEQVGPKNKTSVTRQADfv 724
Cdd:COG5560 572 ASIYDKLVKEFEELLVLVEmkKTdvdlvSEQVRLLReesSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEWE-- 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 725 qtpitgifgghirsvvyQQSSKESATLQPFFTL-QLDIQSDKIrTVQDALESLVARE----SVQGYTTKTKQEVEVSRRV 799
Cdd:COG5560 650 -----------------EKRYLSLFSYDPLWTIrEIGAAERTI-TLQDCLNEFSKPEqlglSDSWYCPGCKEFRQASKQM 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 800 TLEKLPPVLVLHLKRFVYEKTGGcQKLVKNIEYPVDleisrELLSPGVKNKNFKCHRTYRLFAVVYHHGNSAtGGHYTTD 879
Cdd:COG5560 712 ELWRLPMILIIHLKRFSSVRSFR-DKIDDLVEYPID-----DLDLSGVEYMVDDPRLIYDLYAVDNHYGGLS-GGHYTAY 784
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672085227 880 VFQIGLNGWLRIDDQTVKVINQYQVVRPSadrtAYLLYYRR 920
Cdd:COG5560 785 ARNFANNGWYLFDDSRITEVDPEDSVTSS----AYVLFYRR 821
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
757-918 |
2.80e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 52.53 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 757 LQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEVSR-RVTleKLPPVLVLHLKRFvYEKTGGCQKLVKNIEYPVD 835
Cdd:cd02673 100 LDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSeRIM--TFPECLSINLKRY-KLRIATSDYLKKNEEIMKK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 836 LEISrellspgvknknfkcHRTYRLFAVVYHHGNSATGGHYTTDVFQI-GLNGWLRIDDQTVKVINQYQVVRpSADRTAY 914
Cdd:cd02673 177 YCGT---------------DAKYSLVAVICHLGESPYDGHYIAYTKELyNGSSWLYCSDDEIRPVSKNDVST-NARSSGY 240
|
....
gi 672085227 915 LLYY 918
Cdd:cd02673 241 LIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
858-918 |
2.62e-04 |
|
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: 44.40 E-value: 2.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672085227 858 YRLFAVVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVV--RPSADRTAYLLYY 918
Cdd:cd02666 281 YRLHAVFIHRG-EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVFlfTLGNTATPYFLVY 342
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
751-919 |
4.12e-04 |
|
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: 42.90 E-value: 4.12e-04
10 20 30 40 50 60 70 80
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gi 672085227 751 LQPFFTLQLDIQS------DKIRTVQDALESLVARESVQGYTTKTKQEVEVS-RRVTLEKLPPVLVLHLKRFVYEKtGGC 823
Cdd:cd02670 38 LMPLLEPKVDIIHggkkdqDDDKLVNERLLQIPVPDDDDGGGITLEQCLEQYfNNSVFAKAPSCLIICLKRYGKTE-GKA 116
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672085227 824 QKLVKNIEYPVDLEISRELL-------------SPGVKNKNF---KCHRTYRLFAVVYHHGNSATGGHY------TTDVF 881
Cdd:cd02670 117 QKMFKKILIPDEIDIPDFVAddpracskcqlecRVCYDDKDFsptCGKFKLSLCSAVCHRGTSLETGHYvafvryGSYSL 196
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170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 672085227 882 QIGLNG-----WLRIDDQTVKVINQYQVVRPSADRT--AYLLYYR 919
Cdd:cd02670 197 TETDNEaynaqWVFFDDMADRDGVSNGFNIPAARLLedPYMLFYQ 241
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