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Conserved domains on  [gi|1034596566|ref|XP_016879357|]
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ubiquitin carboxyl-terminal hydrolase 10 isoform X2 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( 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
PubMed:  10603300
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 1034596566 219 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 298
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 299 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 378
Cdd:pfam00443  63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 379 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 453
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 454 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISkELLSPGvKNKN 529
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLS-RYLAEE-LKPK 247
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 219 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 298
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 299 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 378
Cdd:pfam00443  63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 379 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 453
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 454 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISkELLSPGvKNKN 529
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLS-RYLAEE-LKPK 247
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 324 RQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTIsngpknhsvneeeqeeqgegsedeweqvgprnktsvtrqadfvq 403
Cdd:cd02257    21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------------------------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 404 tpITGIFGGHIRSVVYQQS---SKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQG---YTTKTKQEVEISRRV 477
Cdd:cd02257    57 --IHDLFGGKLESTIVCLEcghESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 478 TLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTD 557
Cdd:cd02257   135 KIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034596566 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 1034596566  400 DFVQTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQEVEISR 475
Cdd:COG5077    294 TVVENALNGIFVGKMKSYIKcVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGdnrYNAEKHGLQDAKK 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566  476 RVTLEKLPPVLVLHLKRFVYE-KTGGCQKLIKNIEYPVDLEIsKELLSPGVKNKNFKCHrTYRLFAVVYHHGNSATGGHY 554
Cdd:COG5077    372 GVIFESLPPVLHLQLKRFEYDfERDMMVKINDRYEFPLEIDL-LPFLDRDADKSENSDA-VYVLYGVLVHSGDLHEGHYY 449
                          170       180
                   ....*....|....*....|.
gi 1034596566  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 1034596566 219 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 298
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 299 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 378
Cdd:pfam00443  63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 379 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 453
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 454 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISkELLSPGvKNKN 529
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLS-RYLAEE-LKPK 247
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 324 RQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTIsngpknhsvneeeqeeqgegsedeweqvgprnktsvtrqadfvq 403
Cdd:cd02257    21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------------------------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 404 tpITGIFGGHIRSVVYQQS---SKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQG---YTTKTKQEVEISRRV 477
Cdd:cd02257    57 --IHDLFGGKLESTIVCLEcghESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 478 TLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTD 557
Cdd:cd02257   135 KIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034596566 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 1034596566 218 PRGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRPCTSTpMIDSFVRLMNEFTNMPVPPKPRQALGDKIVR 295
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLanYLLSREHSKDCCNEGFCMMC-ALEAHVERALASSGPGSAPRIFSSNLKQISK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 296 DIRpgaafeptyiyrlltvnksslseKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEkltisngpknhsvneeeqee 375
Cdd:cd02661    80 HFR-----------------------IGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDP-------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 376 qgegsedeweqvgPRNKTSVTRQadfvqtpitgIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKirTVQDALESL 454
Cdd:cd02661   117 -------------SSQETTLVQQ----------IFGGYLRSqVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQF 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 455 VARESVQG----YTTKTKQEVEISRRVTLEKLPPVLVLHLKRFvYEKTGGcqKLIKNIEYPVDLEiskelLSPGVKNKNf 530
Cdd:cd02661   172 TKPEQLDGenkyKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-SNFRGG--KINKQISFPETLD-----LSPYMSQPN- 242
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 219 RGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRP--CTSTPMidsfvrlmneftnmpvppkprqalgDKIV 294
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLrnYFLSDRHSCTCLSCSPnsCLSCAM-------------------------DEIF 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 295 RDIRPGAAFEPTYIYRLLT-VNKSSLSEKG-RQEDAEEYLGFILNGLHEEMLNLKKLLSpsnekltisngpKNHSVNeee 372
Cdd:cd02660    56 QEFYYSGDRSPYGPINLLYlSWKHSRNLAGySQQDAHEFFQFLLDQLHTHYGGDKNEAN------------DESHCN--- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 373 qeeqgegsedeweqvgprnktsvtrqadfvqTPITGIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKIR------ 445
Cdd:cd02660   121 -------------------------------CIIHQTFSGSLQSsVTCQRCGGVSTTVDPFLDLSLDIPNKSTPswalge 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 446 -------TVQDALESLVARESVQGYTTKT---KQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLE 515
Cdd:cd02660   170 sgvsgtpTLSDCLDRFTRPEKLGDFAYKCsgcGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELN 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 516 ISKeLLSPGVKNKNFKCHR----TYRLFAVVYHHGNSATgGHYTTDVfQIGLNGWLRIDDQTVKVINQYQVVKPtaerTA 591
Cdd:cd02660   250 MTP-YTSSSIGDTQDSNSLdpdyTYDLFAVVVHKGTLDT-GHYTAYC-RQGDGQWFKFDDAMITRVSEEEVLKS----QA 322

                  ....*
gi 1034596566 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 1034596566 406 ITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDI-----QSDKIrTVQDALESLVARESVQG----YTTKTKQEVEISR 475
Cdd:cd02674    40 IVDLFQGQLKSRLTcLTCGKTSTTFEPFTYLSLPIpsgsgDAPKV-TLEDCLRLFTKEETLDGdnawKCPKCKKKRKATK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 476 RVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPvdleISKELLSPGVKNKNFKCHRTYRLFAVVYHHGnSATGGHYT 555
Cdd:cd02674   119 KLTISRLPKVLIIHLKRFSFSRGST-RKLTTPVTFP----LNDLDLTPYVDTRSFTGPFKYDLYAVVNHYG-SLNGGHYT 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034596566 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 1034596566 422 SSKEsatlQPFFTLQLDIQSDKirTVQDALESLVARESVQGY------TTKTKQEVEisRRVTLEKLPPVLVLHLKRFVY 495
Cdd:cd02663   130 SSRD----ETFLDLSIDVEQNT--SITSCLRQFSATETLCGRnkfycdECCSLQEAE--KRMKIKKLPKILALHLKRFKY 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 496 -EKTGGCQKLIKNIEYPVDLEiskellspgVKNKNFKCH---RTYRLFAVVYHHGNSATGGHYTTdVFQIGlNGWLRIDD 571
Cdd:cd02663   202 dEQLNRYIKLFYRVVFPLELR---------LFNTTDDAEnpdRLYELVAVVVHIGGGPNHGHYVS-IVKSH-GGWLLFDD 270
                         170       180
                  ....*....|....*....|....*....
gi 1034596566 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 1034596566 406 ITGIFGGHIrsvVYQQSSKE----SATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG----YTTKTKQEVEISRRV 477
Cdd:cd02659   113 IKNLFGGKL---VNYIICKEcpheSEREEYFLDLQVAVKGKK--NLEESLDAYVQGETLEGdnkyFCEKCGKKVDAEKGV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 478 TLEKLPPVLVLHLKRFVYEKTGGC-QKLIKNIEYP--VDLE--ISKELLSPGVKNKNFKCHR-TYRLFAVVYHHGnSATG 551
Cdd:cd02659   188 CFKKLPPVLTLQLKRFEFDFETMMrIKINDRFEFPleLDMEpyTEKGLAKKEGDSEKKDSESyIYELHGVLVHSG-DAHG 266
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 220 GLINKGNWCYINATLQALVACPPMyhlmKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMpvppkprqalgDKIVRDIRP 299
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPEL----RDALKNYNPARRGANQSSDNLTNALRDLFDTM-----------DKKQEPVPP 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 300 GAAfeptyiyrLLTVNKS--SLSEKGR-----QEDAEEYLGFILNGLHEEMlnlkKLLSPSNEKltisngpknhsvneee 372
Cdd:cd02657    66 IEF--------LQLLRMAfpQFAEKQNqggyaQQDAEECWSQLLSVLSQKL----PGAGSKGSF---------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 373 qeeqgegsedeweqvgprnktsvtrqadfvqtpITGIFGGHIRSVVY--QQSSKESATLQPFFTLQLDI-QSDKIRTVQD 449
Cdd:cd02657   118 ---------------------------------IDQLFGIELETKMKctESPDEEEVSTESEYKLQCHIsITTEVNYLQD 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 450 AL-----ESLVARESVQGYTTKTKQEVEISRrvtlekLPPVLVLHLKRFVY-EKTGGCQKLIKNIEYPVDLEISkELLSP 523
Cdd:cd02657   165 GLkkgleEEIEKHSPTLGRDAIYTKTSRISR------LPKYLTVQFVRFFWkRDIQKKAKILRKVKFPFELDLY-ELCTP 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 524 -GVknknfkchrtYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINqyqvvKPTAERT--------AYLL 594
Cdd:cd02657   238 sGY----------YELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVT-----EEDILKLsgggdwhiAYIL 302

                  ...
gi 1034596566 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 1034596566 220 GLINKGNWCYINATLQALVACPPMYHLMKFipLYSKVQrpcTSTPMIDSFVRLMNEFTNMPVPPKPRQALgdKIVRDIrp 299
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKH--LVSLIS---SVEQLQSSFLLNPEKYNDELANQAPRRLL--NALREV-- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 300 gaafEPTYiyrlltvnksslsEKGRQEDAEEYLGFILNglheemlNLKKLLSPSNEKLTISngpknhsvneeeqeeqgeg 379
Cdd:cd02671    97 ----NPMY-------------EGYLQHDAQEVLQCILG-------NIQELVEKDFQGQLVL------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 380 sedeweqvgpRNKT----SVTRQ-ADF----VQTPITGIFGGHIRSVVYQQSSKESATLQpfFTLQLDIQSDKIRTvqda 450
Cdd:cd02671   134 ----------RTRCleceTFTERrEDFqdisVPVQESELSKSEESSEISPDPKTEMKTLK--WAISQFASVERIVG---- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 451 lESLVARESVQGYTtktkqevEISRRVTLEKLPPVLVLHLKRF-----VYEKTGGCQKLikNIEYPVDLEISKELLSPGV 525
Cdd:cd02671   198 -EDKYFCENCHHYT-------EAERSLLFDKLPEVITIHLKCFaangsEFDCYGGLSKV--NTPLLTPLKLSLEEWSTKP 267
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 425 ESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQ-EVEISRRVTLEKLPPVLVLHLKRFVYE-KTG 499
Cdd:cd02668   138 ESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGdnqYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDrKTG 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 500 GCQKLIKNIEYPVDLEISKELLSpgvKNKNFkchRTYRLFAVVYHHGNSATGGHYTTDV--FQIGLngWLRIDDQTV--K 575
Cdd:cd02668   216 AKKKLNASISFPEILDMGEYLAE---SDEGS---YVYELSGVLIHQGVSAYSGHYIAHIkdEQTGE--WYKFNDEDVeeM 287
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 400 DFVQTPITGIFGGHIRSVVYQQSSKE-SATLQPFFTLQLDI--QSDKIRTVQDALESLVARESVQG---YTTKTKQEVEI 473
Cdd:cd02667    63 DGLRTFIDSIFGGELTSTIMCESCGTvSLVYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGnnkFACENCTKAKK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 474 SRRVTleKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISkELLSPGVKNKNFKCHRTYRLFAVVYHHGnSATGGH 553
Cdd:cd02667   143 QYLIS--KLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLA-PFCDPKCNSSEDKSSVLYRLYGVVEHSG-TMRSGH 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596566 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 1034596566 220 GLINKGNWCYINATLQAL-VACPPMYHLMKFIPLYSKvqrpCTSTPMidsfVRLMNEFTNMPVPPKPRQALGDKIVRDIR 298
Cdd:cd02664     1 GLINLGNTCYMNSVLQALfMAKDFRRQVLSLNLPRLG----DSQSVM----KKLQLLQAHLMHTQRRAEAPPDYFLEASR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 299 PgAAFEPtyiyrlltvnksslsekGRQEDAEEYLGFILNGLHeemlnlkkllspsnekltisngpknhsvneeeqeeqge 378
Cdd:cd02664    73 P-PWFTP-----------------GSQQDCSEYLRYLLDRLH-------------------------------------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 379 gsedeweqvgprnktsvtrqadfvqTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSdkirtVQDALESLVAR 457
Cdd:cd02664    97 -------------------------TLIEKMFGGKLSTTIRcLNCNSTSARTERFRDLDLSFPS-----VQDLLNYFLSP 146
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 458 ESVQG----YTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYE-KTGGCQKLIKNIEYPVDLEI-----SKELLSPGVKN 527
Cdd:cd02664   147 EKLTGdnqyYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDqKTHVREKIMDNVSINEVLSLpvrveSKSSESPLEKK 226
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566  400 DFVQTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQEVEISR 475
Cdd:COG5077    294 TVVENALNGIFVGKMKSYIKcVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGdnrYNAEKHGLQDAKK 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566  476 RVTLEKLPPVLVLHLKRFVYE-KTGGCQKLIKNIEYPVDLEIsKELLSPGVKNKNFKCHrTYRLFAVVYHHGNSATGGHY 554
Cdd:COG5077    372 GVIFESLPPVLHLQLKRFEYDfERDMMVKINDRYEFPLEIDL-LPFLDRDADKSENSDA-VYVLYGVLVHSGDLHEGHYY 449
                          170       180
                   ....*....|....*....|.
gi 1034596566  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 1034596566 220 GLINKGNWCYINATLQALVACPpmyhlmKFIPLYSK---VQRPCTSTPMIDsfvrLMNEFTnmpvppKPRQAL--GDKIV 294
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIP------SFQWRYDDlenKFPSDVVDPAND----LNCQLI------KLADGLlsGRYSK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 295 RDIRPGAAFE------PTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEmlNLKKLLSPSNE--KLTISN---GP 363
Cdd:cd02658    65 PASLKSENDPyqvgikPSMFKALIGKGHPEFS-TMRQQDALEFLLHLIDKLDRE--SFKNLGLNPNDlfKFMIEDrleCL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 364 KNHSVNeeeqeeqgegsedeweqvgprnktSVTRQADFVQTPItgifgghirsvvyqqsSKESATLQPFFTLQLDIQsdk 443
Cdd:cd02658   142 SCKKVK------------------------YTSELSEILSLPV----------------PKDEATEKEEGELVYEPV--- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 444 irTVQDALESLVARESVQGYTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPvdleiskELLSP 523
Cdd:cd02658   179 --PLEDCLKAYFAPETIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVP-------EELGP 249
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596566 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 1034596566 220 GLINKGNWCYINATLQALVACPpmyhlmkfiplyskvqrpctstpmidSFVRLMNEFTNmpvppkprqalgdkivrdirp 299
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLP--------------------------SLIEYLEEFLE--------------------- 33
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 300 gaafeptyiyrlltvnksslsekgrQEDAEEYLGFILNGLHEEMLNlkkllspsnekltisngpknhsvneeeqeeqgeg 379
Cdd:cd02662    34 -------------------------QQDAHELFQVLLETLEQLLKF---------------------------------- 54
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 380 sedeweqvgprnktsvtrqadfvqtPITGIFgghIRSVVYQQSSKESATLQPFFT-LQLDIQSDKIR---TVQDALESLV 455
Cdd:cd02662    55 -------------------------PFDGLL---ASRIVCLQCGESSKVRYESFTmLSLPVPNQSSGsgtTLEHCLDDFL 106
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 456 ARESVQGYTTKTKQEVeisrrvtLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPvdleiskELLSpgvknknfkcHRT 535
Cdd:cd02662   107 STEIIDDYKCDRCQTV-------IVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFP-------ERLP----------KVL 162
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 536 YRLFAVVYHHGnSATGGHYTT-----------DVFQIGL---------NGWLRIDDQTVKVINQYQVVkptAERTAYLLY 595
Cdd:cd02662   163 YRLRAVVVHYG-SHSSGHYVCyrrkplfskdkEPGSFVRmregpsstsHPWWRISDTTVKEVSESEVL---EQKSAYMLF 238

                  .
gi 1034596566 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 1034596566 474 SRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDleiskELLSPGVKNKNFKCHRTYRLFAVVYHHGNSAtGGH 553
Cdd:COG5560   708 SKQMELWRLPMILIIHLKRFSSVRSFR-DKIDDLVEYPID-----DLDLSGVEYMVDDPRLIYDLYAVDNHYGGLS-GGH 780
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034596566 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 1034596566 383 EWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSsKESATLQPFFtlQLDIQSDKIRTVQDALESLVARESVQG 462
Cdd:cd02665    34 DWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG-KPFCNCETFG--QYPLQVNGYGNLHECLEAAMFEGEVEL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 463 ytTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCqKLIKNIEYPVDLEISKellspgvknknfkchrtYRLFAVV 542
Cdd:cd02665   111 --LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE-KIHDKLEFPQIIQQVP-----------------YELHAVL 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596566 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 1034596566 220 GLINKGNWCYINATLQALVACPPM--YHLMKfiPLYSKVQRPCTstPMIDSFVRLMNEFTNmpvppkPRQalgdkIVRDI 297
Cdd:cd02669   121 GLNNIKNNDYANVIIQALSHVKPIrnFFLLY--ENYENIKDRKS--ELVKRLSELIRKIWN------PRN-----FKGHV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 298 RPgaafeptyiYRLLtvNKSSLSEKGR-----QEDAEEYLGFILNGLHeemlnlkkllspsneKLTISNGPKNHSVneeE 372
Cdd:cd02669   186 SP---------HELL--QAVSKVSKKKfsiteQSDPVEFLSWLLNTLH---------------KDLGGSKKPNSSI---I 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 373 QEEQGEGSEDEWEQVGPRNKTSVTRQADFVQTpitgifgghirsvvYQQSSKESatlqPFFTLQLDI---------QSDK 443
Cdd:cd02669   237 HDCFQGKVQIETQKIKPHAEEEGSKDKFFKDS--------------RVKKTSVS----PFLLLTLDLpppplfkdgNEEN 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 444 IrTVQDALESLVAResvqgYTTKTKQEVEISR-RVTLEKLPPVLVLHLKRFvyEKTGGCQKliKN---IEYPVDLEISKE 519
Cdd:cd02669   299 I-IPQVPLKQLLKK-----YDGKTETELKDSLkRYLISRLPKYLIFHIKRF--SKNNFFKE--KNptiVNFPIKNLDLSD 368
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596566 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 1034596566 435 LQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEISR-RVTleKLPPVLVLHLKRFvYEKTGGCQKLIKNIEYPVD 513
Cdd:cd02673   100 LDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSeRIM--TFPECLSINLKRY-KLRIATSDYLKKNEEIMKK 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 514 LEISkellspgvknknfkcHRTYRLFAVVYHHGNSATGGHYTTDVFQI-GLNGWLRIDDQTVKVINQYQVVKpTAERTAY 592
Cdd:cd02673   177 YCGT---------------DAKYSLVAVICHLGESPYDGHYIAYTKELyNGSSWLYCSDDEIRPVSKNDVST-NARSSGY 240

                  ....
gi 1034596566 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 1034596566 429 LQPFFTLQLDIQS------DKIRTVQDALESLVARESVQGYTTKTKQEVEIS-RRVTLEKLPPVLVLHLKRFVYEKtGGC 501
Cdd:cd02670    38 LMPLLEPKVDIIHggkkdqDDDKLVNERLLQIPVPDDDDGGGITLEQCLEQYfNNSVFAKAPSCLIICLKRYGKTE-GKA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596566 502 QKLIKNIEYPVDLEI-----------SKELLSPGVKNKNF-----KCHRTYRLFAVVYHHGNSATGGHY------TTDVF 559
Cdd:cd02670   117 QKMFKKILIPDEIDIpdfvaddpracSKCQLECRVCYDDKdfsptCGKFKLSLCSAVCHRGTSLETGHYvafvryGSYSL 196
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034596566 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 1034596566 448 QDALESLVARESVQGYTTKTKQEVEIS-RRVTLEKLPPVlVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELlspgvk 526
Cdd:cd02666   201 YDSLTKLPQRSQVQAQLAQPLQRELISmDRYELPSSIDD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQF------ 273
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596566 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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