|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
219-596 |
8.05e-51 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 177.63 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 219 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 298
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 299 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 378
Cdd:pfam00443 63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 379 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 453
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 454 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISkELLSPGvKNKN 529
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLS-RYLAEE-LKPK 247
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829354 530 FKCHRTYRLFAVVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKptaERTAYLLYY 596
Cdd:pfam00443 248 TNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL---SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
324-597 |
4.79e-50 |
|
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: 4.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 324 RQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTIsngpknhsvneeeqeeqgegsedeweqvgprnktsvtrqadfvq 403
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 404 tpITGIFGGHIRSVVYQQS---SKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQG---YTTKTKQEVEISRRV 477
Cdd:cd02257 57 --IHDLFGGKLESTIVCLEcghESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 478 TLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTD 557
Cdd:cd02257 135 KIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578829354 558 VFQIGLNGWLRIDDQTVKVINQYQVVKPTAER-TAYLLYYR 597
Cdd:cd02257 215 VKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSsSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
218-596 |
2.16e-39 |
|
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: 146.27 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 218 PRGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRPCTSTpMIDSFVRLMNEFTNMPVPPKPRQALGDKIVR 295
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLanYLLSREHSKDCCNEGFCMMC-ALEAHVERALASSGPGSAPRIFSSNLKQISK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 296 DIRpgaafeptyiyrlltvnksslseKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEkltisngpknhsvneeeqee 375
Cdd:cd02661 80 HFR-----------------------IGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDP-------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 376 qgegsedeweqvgPRNKTSVTRQadfvqtpitgIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKirTVQDALESL 454
Cdd:cd02661 117 -------------SSQETTLVQQ----------IFGGYLRSqVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQF 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 455 VARESVQG----YTTKTKQEVEISRRVTLEKLPPVLVLHLKRFvYEKTGGcqKLIKNIEYPVDLEiskelLSPGVKNKNf 530
Cdd:cd02661 172 TKPEQLDGenkyKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-SNFRGG--KINKQISFPETLD-----LSPYMSQPN- 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829354 531 KCHRTYRLFAVVYHHGNSATGGHYTTDVfqIGLNG-WLRIDDQTVKVINQYQVVKptaeRTAYLLYY 596
Cdd:cd02661 243 DGPLKYKLYAVLVHSGFSPHSGHYYCYV--KSSNGkWYNMDDSKVSPVSIETVLS----QKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
219-596 |
1.11e-32 |
|
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: 128.26 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 219 RGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRP--CTSTPMidsfvrlmneftnmpvppkprqalgDKIV 294
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLrnYFLSDRHSCTCLSCSPnsCLSCAM-------------------------DEIF 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 295 RDIRPGAAFEPTYIYRLLT-VNKSSLSEKG-RQEDAEEYLGFILNGLHEEMLNLKKLLSpsnekltisngpKNHSVNeee 372
Cdd:cd02660 56 QEFYYSGDRSPYGPINLLYlSWKHSRNLAGySQQDAHEFFQFLLDQLHTHYGGDKNEAN------------DESHCN--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 373 qeeqgegsedeweqvgprnktsvtrqadfvqTPITGIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKIR------ 445
Cdd:cd02660 121 -------------------------------CIIHQTFSGSLQSsVTCQRCGGVSTTVDPFLDLSLDIPNKSTPswalge 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 446 -------TVQDALESLVARESVQGYTTKT---KQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLE 515
Cdd:cd02660 170 sgvsgtpTLSDCLDRFTRPEKLGDFAYKCsgcGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 516 ISKeLLSPGVKNKNFKCHR----TYRLFAVVYHHGNSATgGHYTTDVfQIGLNGWLRIDDQTVKVINQYQVVKPtaerTA 591
Cdd:cd02660 250 MTP-YTSSSIGDTQDSNSLdpdyTYDLFAVVVHKGTLDT-GHYTAYC-RQGDGQWFKFDDAMITRVSEEEVLKS----QA 322
|
....*
gi 578829354 592 YLLYY 596
Cdd:cd02660 323 YLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
406-597 |
5.04e-28 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 112.38 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 406 ITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDI-----QSDKIrTVQDALESLVARESVQG----YTTKTKQEVEISR 475
Cdd:cd02674 40 IVDLFQGQLKSRLTcLTCGKTSTTFEPFTYLSLPIpsgsgDAPKV-TLEDCLRLFTKEETLDGdnawKCPKCKKKRKATK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 476 RVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPvdleISKELLSPGVKNKNFKCHRTYRLFAVVYHHGnSATGGHYT 555
Cdd:cd02674 119 KLTISRLPKVLIIHLKRFSFSRGST-RKLTTPVTFP----LNDLDLTPYVDTRSFTGPFKYDLYAVVNHYG-SLNGGHYT 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578829354 556 TDVFQIGLNGWLRIDDQTVKVINQYQVVKptaeRTAYLLYYR 597
Cdd:cd02674 193 AYCKNNETNDWYKFDDSRVTKVSESSVVS----SSAYILFYE 230
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
422-596 |
2.70e-21 |
|
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: 94.68 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 422 SSKEsatlQPFFTLQLDIQSDKirTVQDALESLVARESVQGY------TTKTKQEVEisRRVTLEKLPPVLVLHLKRFVY 495
Cdd:cd02663 130 SSRD----ETFLDLSIDVEQNT--SITSCLRQFSATETLCGRnkfycdECCSLQEAE--KRMKIKKLPKILALHLKRFKY 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 496 -EKTGGCQKLIKNIEYPVDLEiskellspgVKNKNFKCH---RTYRLFAVVYHHGNSATGGHYTTdVFQIGlNGWLRIDD 571
Cdd:cd02663 202 dEQLNRYIKLFYRVVFPLELR---------LFNTTDDAEnpdRLYELVAVVVHIGGGPNHGHYVS-IVKSH-GGWLLFDD 270
|
170 180
....*....|....*....|....*....
gi 578829354 572 QTVKVINQYQVVKPTAER----TAYLLYY 596
Cdd:cd02663 271 ETVEKIDENAVEEFFGDSpnqaTAYVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
406-600 |
2.96e-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: 89.24 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 406 ITGIFGGHIrsvVYQQSSKE----SATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG----YTTKTKQEVEISRRV 477
Cdd:cd02659 113 IKNLFGGKL---VNYIICKEcpheSEREEYFLDLQVAVKGKK--NLEESLDAYVQGETLEGdnkyFCEKCGKKVDAEKGV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 478 TLEKLPPVLVLHLKRFVYEKTGGC-QKLIKNIEYP--VDLE--ISKELLSPGVKNKNFKCHR-TYRLFAVVYHHGnSATG 551
Cdd:cd02659 188 CFKKLPPVLTLQLKRFEFDFETMMrIKINDRFEFPleLDMEpyTEKGLAKKEGDSEKKDSESyIYELHGVLVHSG-DAHG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829354 552 GHYTTDVFQIGLNGWLRIDDQTVKVINQ----------------YQVVKPTAERT--AYLLYYRRVD 600
Cdd:cd02659 267 GHYYSYIKDRDDGKWYKFNDDVVTPFDPndaeeecfggeetqktYDSGPRAFKRTtnAYMLFYERKS 333
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
220-597 |
2.18e-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 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: 83.15 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 220 GLINKGNWCYINATLQALVACPPMyhlmKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMpvppkprqalgDKIVRDIRP 299
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPEL----RDALKNYNPARRGANQSSDNLTNALRDLFDTM-----------DKKQEPVPP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 300 GAAfeptyiyrLLTVNKS--SLSEKGR-----QEDAEEYLGFILNGLHEEMlnlkKLLSPSNEKltisngpknhsvneee 372
Cdd:cd02657 66 IEF--------LQLLRMAfpQFAEKQNqggyaQQDAEECWSQLLSVLSQKL----PGAGSKGSF---------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 373 qeeqgegsedeweqvgprnktsvtrqadfvqtpITGIFGGHIRSVVY--QQSSKESATLQPFFTLQLDI-QSDKIRTVQD 449
Cdd:cd02657 118 ---------------------------------IDQLFGIELETKMKctESPDEEEVSTESEYKLQCHIsITTEVNYLQD 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 450 AL-----ESLVARESVQGYTTKTKQEVEISRrvtlekLPPVLVLHLKRFVY-EKTGGCQKLIKNIEYPVDLEISkELLSP 523
Cdd:cd02657 165 GLkkgleEEIEKHSPTLGRDAIYTKTSRISR------LPKYLTVQFVRFFWkRDIQKKAKILRKVKFPFELDLY-ELCTP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 524 -GVknknfkchrtYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINqyqvvKPTAERT--------AYLL 594
Cdd:cd02657 238 sGY----------YELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVT-----EEDILKLsgggdwhiAYIL 302
|
...
gi 578829354 595 YYR 597
Cdd:cd02657 303 LYK 305
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
220-597 |
9.94e-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: 81.86 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 220 GLINKGNWCYINATLQALVACPPMYHLMKFipLYSKVQrpcTSTPMIDSFVRLMNEFTNMPVPPKPRQALgdKIVRDIrp 299
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKH--LVSLIS---SVEQLQSSFLLNPEKYNDELANQAPRRLL--NALREV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 300 gaafEPTYiyrlltvnksslsEKGRQEDAEEYLGFILNglheemlNLKKLLSPSNEKLTISngpknhsvneeeqeeqgeg 379
Cdd:cd02671 97 ----NPMY-------------EGYLQHDAQEVLQCILG-------NIQELVEKDFQGQLVL------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 380 sedeweqvgpRNKT----SVTRQ-ADF----VQTPITGIFGGHIRSVVYQQSSKESATLQpfFTLQLDIQSDKIRTvqda 450
Cdd:cd02671 134 ----------RTRCleceTFTERrEDFqdisVPVQESELSKSEESSEISPDPKTEMKTLK--WAISQFASVERIVG---- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 451 lESLVARESVQGYTtktkqevEISRRVTLEKLPPVLVLHLKRF-----VYEKTGGCQKLikNIEYPVDLEISKELLSPGV 525
Cdd:cd02671 198 -EDKYFCENCHHYT-------EAERSLLFDKLPEVITIHLKCFaangsEFDCYGGLSKV--NTPLLTPLKLSLEEWSTKP 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829354 526 KNKnfkchrTYRLFAVVYHHGNSATGGHYTTDVfqiglnGWLRIDDQTVKVINQ---YQVVKPTAERTA--YLLYYR 597
Cdd:cd02671 268 KND------VYRLFAVVMHSGATISSGHYTAYV------RWLLFDDSEVKVTEEkdfLEALSPNTSSTStpYLLFYK 332
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
425-597 |
4.05e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 79.77 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 425 ESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQ-EVEISRRVTLEKLPPVLVLHLKRFVYE-KTG 499
Cdd:cd02668 138 ESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGdnqYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDrKTG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 500 GCQKLIKNIEYPVDLEISKELLSpgvKNKNFkchRTYRLFAVVYHHGNSATGGHYTTDV--FQIGLngWLRIDDQTV--K 575
Cdd:cd02668 216 AKKKLNASISFPEILDMGEYLAE---SDEGS---YVYELSGVLIHQGVSAYSGHYIAHIkdEQTGE--WYKFNDEDVeeM 287
|
170 180 190
....*....|....*....|....*....|....*..
gi 578829354 576 VINQYQ--VVKPTAE-------------RTAYLLYYR 597
Cdd:cd02668 288 PGKPLKlgNSEDPAKprkseikkgthssRTAYMLVYK 324
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
400-597 |
1.47e-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: 77.43 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 400 DFVQTPITGIFGGHIRSVVYQQSSKE-SATLQPFFTLQLDI--QSDKIRTVQDALESLVARESVQG---YTTKTKQEVEI 473
Cdd:cd02667 63 DGLRTFIDSIFGGELTSTIMCESCGTvSLVYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGnnkFACENCTKAKK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 474 SRRVTleKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISkELLSPGVKNKNFKCHRTYRLFAVVYHHGnSATGGH 553
Cdd:cd02667 143 QYLIS--KLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLA-PFCDPKCNSSEDKSSVLYRLYGVVEHSG-TMRSGH 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829354 554 YTTDVF-----QIGLNGWLRIDDQTVKVINQYQ-------VVKPTAERT-----AYLLYYR 597
Cdd:cd02667 219 YVAYVKvrppqQRLSDLTKSKPAADEAGPGSGQwyyisdsDVREVSLEEvlkseAYLLFYE 279
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
220-556 |
7.56e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 72.91 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 220 GLINKGNWCYINATLQAL-VACPPMYHLMKFIPLYSKvqrpCTSTPMidsfVRLMNEFTNMPVPPKPRQALGDKIVRDIR 298
Cdd:cd02664 1 GLINLGNTCYMNSVLQALfMAKDFRRQVLSLNLPRLG----DSQSVM----KKLQLLQAHLMHTQRRAEAPPDYFLEASR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 299 PgAAFEPtyiyrlltvnksslsekGRQEDAEEYLGFILNGLHeemlnlkkllspsnekltisngpknhsvneeeqeeqge 378
Cdd:cd02664 73 P-PWFTP-----------------GSQQDCSEYLRYLLDRLH-------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 379 gsedeweqvgprnktsvtrqadfvqTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSdkirtVQDALESLVAR 457
Cdd:cd02664 97 -------------------------TLIEKMFGGKLSTTIRcLNCNSTSARTERFRDLDLSFPS-----VQDLLNYFLSP 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 458 ESVQG----YTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYE-KTGGCQKLIKNIEYPVDLEI-----SKELLSPGVKN 527
Cdd:cd02664 147 EKLTGdnqyYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDqKTHVREKIMDNVSINEVLSLpvrveSKSSESPLEKK 226
|
330 340 350
....*....|....*....|....*....|....*..
gi 578829354 528 KNFK------CHRT--YRLFAVVYHHGNSATGGHYTT 556
Cdd:cd02664 227 EEESgddgelVTRQvhYRLYAVVVHSGYSSESGHYFT 263
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
400-574 |
1.58e-13 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 74.14 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 400 DFVQTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQEVEISR 475
Cdd:COG5077 294 TVVENALNGIFVGKMKSYIKcVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGdnrYNAEKHGLQDAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 476 RVTLEKLPPVLVLHLKRFVYE-KTGGCQKLIKNIEYPVDLEIsKELLSPGVKNKNFKCHrTYRLFAVVYHHGNSATGGHY 554
Cdd:COG5077 372 GVIFESLPPVLHLQLKRFEYDfERDMMVKINDRYEFPLEIDL-LPFLDRDADKSENSDA-VYVLYGVLVHSGDLHEGHYY 449
|
170 180
....*....|....*....|.
gi 578829354 555 TtdVFQIGLNG-WLRIDDQTV 574
Cdd:COG5077 450 A--LLKPEKDGrWYKFDDTRV 468
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
220-597 |
8.21e-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: 69.66 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 220 GLINKGNWCYINATLQALVACPpmyhlmKFIPLYSK---VQRPCTSTPMIDsfvrLMNEFTnmpvppKPRQAL--GDKIV 294
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIP------SFQWRYDDlenKFPSDVVDPAND----LNCQLI------KLADGLlsGRYSK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 295 RDIRPGAAFE------PTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEmlNLKKLLSPSNE--KLTISN---GP 363
Cdd:cd02658 65 PASLKSENDPyqvgikPSMFKALIGKGHPEFS-TMRQQDALEFLLHLIDKLDRE--SFKNLGLNPNDlfKFMIEDrleCL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 364 KNHSVNeeeqeeqgegsedeweqvgprnktSVTRQADFVQTPItgifgghirsvvyqqsSKESATLQPFFTLQLDIQsdk 443
Cdd:cd02658 142 SCKKVK------------------------YTSELSEILSLPV----------------PKDEATEKEEGELVYEPV--- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 444 irTVQDALESLVARESVQGYTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPvdleiskELLSP 523
Cdd:cd02658 179 --PLEDCLKAYFAPETIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVP-------EELGP 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829354 524 GvknknfkchrTYRLFAVVYHHGNSATGGHYTTDVFQ--IGLNGWLRIDDQTVkvinqYQVVK-PTAERTAYLLYYR 597
Cdd:cd02658 250 G----------KYELIAFISHKGTSVHSGHYVAHIKKeiDGEGKWVLFNDEKV-----VASQDpPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
220-596 |
2.39e-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: 67.01 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 220 GLINKGNWCYINATLQALVACPpmyhlmkfiplyskvqrpctstpmidSFVRLMNEFTNmpvppkprqalgdkivrdirp 299
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP--------------------------SLIEYLEEFLE--------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 300 gaafeptyiyrlltvnksslsekgrQEDAEEYLGFILNGLHEEMLNlkkllspsnekltisngpknhsvneeeqeeqgeg 379
Cdd:cd02662 34 -------------------------QQDAHELFQVLLETLEQLLKF---------------------------------- 54
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 380 sedeweqvgprnktsvtrqadfvqtPITGIFgghIRSVVYQQSSKESATLQPFFT-LQLDIQSDKIR---TVQDALESLV 455
Cdd:cd02662 55 -------------------------PFDGLL---ASRIVCLQCGESSKVRYESFTmLSLPVPNQSSGsgtTLEHCLDDFL 106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 456 ARESVQGYTTKTKQEVeisrrvtLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPvdleiskELLSpgvknknfkcHRT 535
Cdd:cd02662 107 STEIIDDYKCDRCQTV-------IVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFP-------ERLP----------KVL 162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 536 YRLFAVVYHHGnSATGGHYTT-----------DVFQIGL---------NGWLRIDDQTVKVINQYQVVkptAERTAYLLY 595
Cdd:cd02662 163 YRLRAVVVHYG-SHSSGHYVCyrrkplfskdkEPGSFVRmregpsstsHPWWRISDTTVKEVSESEVL---EQKSAYMLF 238
|
.
gi 578829354 596 Y 596
Cdd:cd02662 239 Y 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
474-598 |
3.74e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 66.06 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 474 SRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDleiskELLSPGVKNKNFKCHRTYRLFAVVYHHGNSAtGGH 553
Cdd:COG5560 708 SKQMELWRLPMILIIHLKRFSSVRSFR-DKIDDLVEYPID-----DLDLSGVEYMVDDPRLIYDLYAVDNHYGGLS-GGH 780
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578829354 554 YTTDVFQIGLNGWLRIDDQTVKVINQYQVVKptaeRTAYLLYYRR 598
Cdd:COG5560 781 YTAYARNFANNGWYLFDDSRITEVDPEDSVT----SSAYVLFYRR 821
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
383-596 |
5.91e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 59.88 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 383 EWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSsKESATLQPFFtlQLDIQSDKIRTVQDALESLVARESVQG 462
Cdd:cd02665 34 DWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG-KPFCNCETFG--QYPLQVNGYGNLHECLEAAMFEGEVEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 463 ytTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCqKLIKNIEYPVDLEISKellspgvknknfkchrtYRLFAVV 542
Cdd:cd02665 111 --LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE-KIHDKLEFPQIIQQVP-----------------YELHAVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578829354 543 YHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKPT----AERTAYLLYY 596
Cdd:cd02665 171 VHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggRNPSAYCLMY 227
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
220-578 |
8.76e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 61.18 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 220 GLINKGNWCYINATLQALVACPPM--YHLMKfiPLYSKVQRPCTstPMIDSFVRLMNEFTNmpvppkPRQalgdkIVRDI 297
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIrnFFLLY--ENYENIKDRKS--ELVKRLSELIRKIWN------PRN-----FKGHV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 298 RPgaafeptyiYRLLtvNKSSLSEKGR-----QEDAEEYLGFILNGLHeemlnlkkllspsneKLTISNGPKNHSVneeE 372
Cdd:cd02669 186 SP---------HELL--QAVSKVSKKKfsiteQSDPVEFLSWLLNTLH---------------KDLGGSKKPNSSI---I 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 373 QEEQGEGSEDEWEQVGPRNKTSVTRQADFVQTpitgifgghirsvvYQQSSKESatlqPFFTLQLDI---------QSDK 443
Cdd:cd02669 237 HDCFQGKVQIETQKIKPHAEEEGSKDKFFKDS--------------RVKKTSVS----PFLLLTLDLpppplfkdgNEEN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 444 IrTVQDALESLVAResvqgYTTKTKQEVEISR-RVTLEKLPPVLVLHLKRFvyEKTGGCQKliKN---IEYPVDLEISKE 519
Cdd:cd02669 299 I-IPQVPLKQLLKK-----YDGKTETELKDSLkRYLISRLPKYLIFHIKRF--SKNNFFKE--KNptiVNFPIKNLDLSD 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578829354 520 LLSPGVKNKNFkcHRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVIN 578
Cdd:cd02669 369 YVHFDKPSLNL--STKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVL 425
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
435-596 |
8.96e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 53.30 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 435 LQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEISR-RVTleKLPPVLVLHLKRFvYEKTGGCQKLIKNIEYPVD 513
Cdd:cd02673 100 LDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSeRIM--TFPECLSINLKRY-KLRIATSDYLKKNEEIMKK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 514 LEISkellspgvknknfkcHRTYRLFAVVYHHGNSATGGHYTTDVFQI-GLNGWLRIDDQTVKVINQYQVVKpTAERTAY 592
Cdd:cd02673 177 YCGT---------------DAKYSLVAVICHLGESPYDGHYIAYTKELyNGSSWLYCSDDEIRPVSKNDVST-NARSSGY 240
|
....
gi 578829354 593 LLYY 596
Cdd:cd02673 241 LIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
429-597 |
1.49e-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: 43.67 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 429 LQPFFTLQLDIQS------DKIRTVQDALESLVARESVQGYTTKTKQEVEIS-RRVTLEKLPPVLVLHLKRFVYEKtGGC 501
Cdd:cd02670 38 LMPLLEPKVDIIHggkkdqDDDKLVNERLLQIPVPDDDDGGGITLEQCLEQYfNNSVFAKAPSCLIICLKRYGKTE-GKA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 502 QKLIKNIEYPVDLEI-----------SKELLSPGVKNKNF-----KCHRTYRLFAVVYHHGNSATGGHY------TTDVF 559
Cdd:cd02670 117 QKMFKKILIPDEIDIpdfvaddpracSKCQLECRVCYDDKdfsptCGKFKLSLCSAVCHRGTSLETGHYvafvryGSYSL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578829354 560 QIGLNG-----WLRIDDQTVKVINQYQVVKPTAERT--AYLLYYR 597
Cdd:cd02670 197 TETDNEaynaqWVFFDDMADRDGVSNGFNIPAARLLedPYMLFYQ 241
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
448-596 |
1.59e-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: 44.02 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829354 448 QDALESLVARESVQGYTTKTKQEVEIS-RRVTLEKLPPVlVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELlspgvk 526
Cdd:cd02666 201 YDSLTKLPQRSQVQAQLAQPLQRELISmDRYELPSSIDD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQF------ 273
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829354 527 nKNFKCHrTYRLFAVVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKPTAERTA--YLLYY 596
Cdd:cd02666 274 -DDLKSY-GYRLHAVFIHRG-EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVFLFTLGNTAtpYFLVY 342
|
|
| |
