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Conserved domains on  [gi|578829354|ref|XP_006721395|]
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ubiquitin carboxyl-terminal hydrolase 10 isoform X2 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 11995783)

ubiquitin carboxyl-terminal hydrolase family protein may remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
SCOP:  4003158

Graphical summary

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List of domain hits

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
 
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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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