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Conserved domains on  [gi|2217308113|ref|XP_047290832|]
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ubiquitin carboxyl-terminal hydrolase 10 isoform X1 [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;
420-775 1.98e-41

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 153.75  E-value: 1.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 420 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 499
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 500 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 579
Cdd:pfam00443  63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 580 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 654
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 655 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISK----------- 719
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLSRylaeelkpktn 249
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217308113 720 ---------VVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKptaERTAYLLYY 775
Cdd:pfam00443 250 nlqdyrlvaVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL---SSSAYILFY 310
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
420-775 1.98e-41

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 153.75  E-value: 1.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 420 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 499
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 500 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 579
Cdd:pfam00443  63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 580 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 654
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 655 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISK----------- 719
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLSRylaeelkpktn 249
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217308113 720 ---------VVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKptaERTAYLLYY 775
Cdd:pfam00443 250 nlqdyrlvaVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL---SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
525-776 4.98e-41

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: 151.10  E-value: 4.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 525 RQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTIsngpknhsvneeeqeeqgegsedeweqvgprnktsvtrqadfvq 604
Cdd:cd02257    21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------------------------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 605 tpITGIFGGHIRSVVYQQS---SKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQG---YTTKTKQEVEISRRV 678
Cdd:cd02257    57 --IHDLFGGKLESTIVCLEcghESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 679 TLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISK----------------------VVYHHGNSATGGHYTTD 736
Cdd:cd02257   135 KIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPylsegekdsdsdngsykyelvaVVVHSGTSADSGHYVAY 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217308113 737 VFQIGLNGWLRIDDQTVKVINQYQVVKPTAER-TAYLLYYR 776
Cdd:cd02257   215 VKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSsSAYILFYE 255
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
675-777 5.10e-10

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 62.98  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 675 SRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVD-LEISKVVY----------------HHGNSAtGGHYTTDV 737
Cdd:COG5560   708 SKQMELWRLPMILIIHLKRFSSVRSFR-DKIDDLVEYPIDdLDLSGVEYmvddprliydlyavdnHYGGLS-GGHYTAYA 785
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217308113 738 FQIGLNGWLRIDDQTVKVINQYQVVKptaeRTAYLLYYRR 777
Cdd:COG5560   786 RNFANNGWYLFDDSRITEVDPEDSVT----SSAYVLFYRR 821
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
420-775 1.98e-41

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 153.75  E-value: 1.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 420 RGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPvppkprqalgdkivrdir 499
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNS------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 500 PGAAFEPTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEMlnlkkllspsnekltisngpknhsvneeeqeeqge 579
Cdd:pfam00443  63 KSSSVSPKMFKKSLGKLNPDFS-GYKQQDAQEFLLFLLDGLHEDL----------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 580 gsedewEQVGPRNKTSvtrqadfvqtPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKIRTV----QDALES 654
Cdd:pfam00443 107 ------NGNHSTENES----------LITDLFRGQLKSRLKcLSCGEVSETFEPFSDLSLPIPGDSAELKtaslQICFLQ 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 655 LVARESVQGYTT----KTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVDLEISK----------- 719
Cdd:pfam00443 171 FSKLEELDDEEKyycdKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW-EKLNTEVEFPLELDLSRylaeelkpktn 249
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217308113 720 ---------VVYHHGnSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKptaERTAYLLYY 775
Cdd:pfam00443 250 nlqdyrlvaVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL---SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
525-776 4.98e-41

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: 151.10  E-value: 4.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 525 RQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTIsngpknhsvneeeqeeqgegsedeweqvgprnktsvtrqadfvq 604
Cdd:cd02257    21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSL-------------------------------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 605 tpITGIFGGHIRSVVYQQS---SKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQG---YTTKTKQEVEISRRV 678
Cdd:cd02257    57 --IHDLFGGKLESTIVCLEcghESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGdncYKCEKKKKQEATKRL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 679 TLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISK----------------------VVYHHGNSATGGHYTTD 736
Cdd:cd02257   135 KIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPylsegekdsdsdngsykyelvaVVVHSGTSADSGHYVAY 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217308113 737 VFQIGLNGWLRIDDQTVKVINQYQVVKPTAER-TAYLLYYR 776
Cdd:cd02257   215 VKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSsSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
419-775 5.73e-34

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 132.40  E-value: 5.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 419 PRGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRPCTSTpMIDSFVRLMNEFTNMPVPPKPRQALGDKIVR 496
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLanYLLSREHSKDCCNEGFCMMC-ALEAHVERALASSGPGSAPRIFSSNLKQISK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 497 DIRpgaafeptyiyrlltvnksslseKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEkltisngpknhsvneeeqee 576
Cdd:cd02661    80 HFR-----------------------IGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDP-------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 577 qgegsedeweqvgPRNKTSVTRQadfvqtpitgIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKirTVQDALESL 655
Cdd:cd02661   117 -------------SSQETTLVQQ----------IFGGYLRSqVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQF 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 656 VARESVQG----YTTKTKQEVEISRRVTLEKLPPVLVLHLKRFvYEKTGGcqKLIKNIEYPVDLEISK------------ 719
Cdd:cd02661   172 TKPEQLDGenkyKCERCKKKVKASKQLTIHRAPNVLTIHLKRF-SNFRGG--KINKQISFPETLDLSPymsqpndgplky 248
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217308113 720 ----VVYHHGNSATGGHYTTDVfqIGLNG-WLRIDDQTVKVINQYQVVKptaeRTAYLLYY 775
Cdd:cd02661   249 klyaVLVHSGFSPHSGHYYCYV--KSSNGkWYNMDDSKVSPVSIETVLS----QKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
420-775 4.98e-27

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 112.85  E-value: 4.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 420 RGLINKGNWCYINATLQALVACPPM--YHLMKFIPLYSKVQRP--CTSTPMidsfvrlmneftnmpvppkprqalgDKIV 495
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLrnYFLSDRHSCTCLSCSPnsCLSCAM-------------------------DEIF 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 496 RDIRPGAAFEPTYIYRLLT-VNKSSLSEKG-RQEDAEEYLGFILNGLHEEMLNLKKLLSpsnekltisngpKNHSVNeee 573
Cdd:cd02660    56 QEFYYSGDRSPYGPINLLYlSWKHSRNLAGySQQDAHEFFQFLLDQLHTHYGGDKNEAN------------DESHCN--- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 574 qeeqgegsedeweqvgprnktsvtrqadfvqTPITGIFGGHIRS-VVYQQSSKESATLQPFFTLQLDIQSDKIR------ 646
Cdd:cd02660   121 -------------------------------CIIHQTFSGSLQSsVTCQRCGGVSTTVDPFLDLSLDIPNKSTPswalge 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 647 -------TVQDALESLVARESVQGYTTKT---KQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDL- 715
Cdd:cd02660   170 sgvsgtpTLSDCLDRFTRPEKLGDFAYKCsgcGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELn 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 716 ------------------------EISKVVYHHGNSATgGHYTTDVfQIGLNGWLRIDDQTVKVINQYQVVKPtaerTAY 771
Cdd:cd02660   250 mtpytsssigdtqdsnsldpdytyDLFAVVVHKGTLDT-GHYTAYC-RQGDGQWFKFDDAMITRVSEEEVLKS----QAY 323

                  ....
gi 2217308113 772 LLYY 775
Cdd:cd02660   324 LLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
607-776 4.99e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 92.74  E-value: 4.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 607 ITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDI-----QSDKIrTVQDALESLVARESVQG----YTTKTKQEVEISR 676
Cdd:cd02674    40 IVDLFQGQLKSRLTcLTCGKTSTTFEPFTYLSLPIpsgsgDAPKV-TLEDCLRLFTKEETLDGdnawKCPKCKKKRKATK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 677 RVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPV-DLEISK-----------------VVYHHGnSATGGHYTTDVF 738
Cdd:cd02674   119 KLTISRLPKVLIIHLKRFSFSRGST-RKLTTPVTFPLnDLDLTPyvdtrsftgpfkydlyaVVNHYG-SLNGGHYTAYCK 196
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217308113 739 QIGLNGWLRIDDQTVKVINQYQVVKptaeRTAYLLYYR 776
Cdd:cd02674   197 NNETNDWYKFDDSRVTKVSESSVVS----SSAYILFYE 230
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
623-775 1.77e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 83.90  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 623 SSKEsatlQPFFTLQLDIQSDKirTVQDALESLVARESVQGY------TTKTKQEVEisRRVTLEKLPPVLVLHLKRFVY 696
Cdd:cd02663   130 SSRD----ETFLDLSIDVEQNT--SITSCLRQFSATETLCGRnkfycdECCSLQEAE--KRMKIKKLPKILALHLKRFKY 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 697 -EKTGGCQKLIKNIEYPVDL----------------EISKVVYHHGNSATGGHYTTdVFQIGlNGWLRIDDQTVKVINQY 759
Cdd:cd02663   202 dEQLNRYIKLFYRVVFPLELrlfnttddaenpdrlyELVAVVVHIGGGPNHGHYVS-IVKSH-GGWLLFDDETVEKIDEN 279
                         170       180
                  ....*....|....*....|
gi 2217308113 760 QVVKPTAER----TAYLLYY 775
Cdd:cd02663   280 AVEEFFGDSpnqaTAYVLFY 299
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
607-779 1.18e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 75.76  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 607 ITGIFGGHIrsvVYQQSSKE----SATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG----YTTKTKQEVEISRRV 678
Cdd:cd02659   113 IKNLFGGKL---VNYIICKEcpheSEREEYFLDLQVAVKGKK--NLEESLDAYVQGETLEGdnkyFCEKCGKKVDAEKGV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 679 TLEKLPPVLVLHLKRFVY------------------------------EKTGGCQKLIKNIEYPVDLeiSKVVYHHGnSA 728
Cdd:cd02659   188 CFKKLPPVLTLQLKRFEFdfetmmrikindrfefpleldmepytekglAKKEGDSEKKDSESYIYEL--HGVLVHSG-DA 264
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217308113 729 TGGHYTTDVFQIGLNGWLRIDDQTVKVINQ----------------YQVVKPTAERT--AYLLYYRRVD 779
Cdd:cd02659   265 HGGHYYSYIKDRDDGKWYKFNDDVVTPFDPndaeeecfggeetqktYDSGPRAFKRTtnAYMLFYERKS 333
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
421-776 1.57e-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 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: 75.06  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 421 GLINKGNWCYINATLQALVACPPMyhlmKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMpvppkprqalgDKIVRDIRP 500
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPEL----RDALKNYNPARRGANQSSDNLTNALRDLFDTM-----------DKKQEPVPP 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 501 GAAfeptyiyrLLTVNKS--SLSEKGR-----QEDAEEYLGFILNGLHEEMlnlkKLLSPSNEKltisngpknhsvneee 573
Cdd:cd02657    66 IEF--------LQLLRMAfpQFAEKQNqggyaQQDAEECWSQLLSVLSQKL----PGAGSKGSF---------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 574 qeeqgegsedeweqvgprnktsvtrqadfvqtpITGIFGGHIRSVVY--QQSSKESATLQPFFTLQLDI-QSDKIRTVQD 650
Cdd:cd02657   118 ---------------------------------IDQLFGIELETKMKctESPDEEEVSTESEYKLQCHIsITTEVNYLQD 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 651 AL-----ESLVARESVQGYTTKTKQEVEISRrvtlekLPPVLVLHLKRFVY-EKTGGCQKLIKNIEYPVDL--------- 715
Cdd:cd02657   165 GLkkgleEEIEKHSPTLGRDAIYTKTSRISR------LPKYLTVQFVRFFWkRDIQKKAKILRKVKFPFELdlyelctps 238
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217308113 716 ---EISKVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINqyqvvKPTAERT--------AYLLYYR 776
Cdd:cd02657   239 gyyELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVT-----EEDILKLsgggdwhiAYILLYK 305
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
626-776 3.66e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 71.30  E-value: 3.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 626 ESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQ-EVEISRRVTLEKLPPVLVLHLKRFVYE-KTG 700
Cdd:cd02668   138 ESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGdnqYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFDrKTG 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 701 GCQKLIKNIEYPVDL----------------EISKVVYHHGNSATGGHYTTDV--FQIGLngWLRIDDQTV--KVINQYQ 760
Cdd:cd02668   216 AKKKLNASISFPEILdmgeylaesdegsyvyELSGVLIHQGVSAYSGHYIAHIkdEQTGE--WYKFNDEDVeeMPGKPLK 293
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217308113 761 --VVKPTAE-------------RTAYLLYYR 776
Cdd:cd02668   294 lgNSEDPAKprkseikkgthssRTAYMLVYK 324
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
421-776 5.94e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 67.61  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 421 GLINKGNWCYINATLQALVACPPMYHLMKFipLYSKVQrpcTSTPMIDSFVRLMNEFTNMPVPPKPRQALgdKIVRDIrp 500
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKH--LVSLIS---SVEQLQSSFLLNPEKYNDELANQAPRRLL--NALREV-- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 501 gaafEPTYiyrlltvnksslsEKGRQEDAEEYLGFILNglheemlNLKKLLSPSNEKLTISngpknhsvneeeqeeqgeg 580
Cdd:cd02671    97 ----NPMY-------------EGYLQHDAQEVLQCILG-------NIQELVEKDFQGQLVL------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 581 sedeweqvgpRNKT----SVTRQ-ADF----VQTPITGIFGGHIRSVVYQQSSKESATLQpfFTLQLDIQSDKIRTvqda 651
Cdd:cd02671   134 ----------RTRCleceTFTERrEDFqdisVPVQESELSKSEESSEISPDPKTEMKTLK--WAISQFASVERIVG---- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 652 lESLVARESVQGYTtktkqevEISRRVTLEKLPPVLVLHLKRF-----VYEKTGGCQKLIKNIEYPVDL----------- 715
Cdd:cd02671   198 -EDKYFCENCHHYT-------EAERSLLFDKLPEVITIHLKCFaangsEFDCYGGLSKVNTPLLTPLKLsleewstkpkn 269
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217308113 716 ---EISKVVYHHGNSATGGHYTTDVfqiglnGWLRIDDQTVKVINQ---YQVVKPTAERTA--YLLYYR 776
Cdd:cd02671   270 dvyRLFAVVMHSGATISSGHYTAYV------RWLLFDDSEVKVTEEkdfLEALSPNTSSTStpYLLFYK 332
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
601-776 1.06e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 63.17  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 601 DFVQTPITGIFGGHIRSVVYQQSSKE-SATLQPFFTLQLDI--QSDKIRTVQDALESLVARESVQG---YTTKTKQEVEI 674
Cdd:cd02667    63 DGLRTFIDSIFGGELTSTIMCESCGTvSLVYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGnnkFACENCTKAKK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 675 SRRVTleKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISK---------------------VVYHHGnSATGGHY 733
Cdd:cd02667   143 QYLIS--KLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPfcdpkcnssedkssvlyrlygVVEHSG-TMRSGHY 219
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 734 TTDVF-----QIGLNGWLRIDDQTVKVINQYQ-------VVKPTAERT-----AYLLYYR 776
Cdd:cd02667   220 VAYVKvrppqQRLSDLTKSKPAADEAGPGSGQwyyisdsDVREVSLEEvlkseAYLLFYE 279
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
421-776 1.07e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 63.50  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 421 GLINKGNWCYINATLQALVACPpmyhlmKFIPLYSK---VQRPCTSTPMIDsfvrLMNEFTnmpvppKPRQAL--GDKIV 495
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIP------SFQWRYDDlenKFPSDVVDPAND----LNCQLI------KLADGLlsGRYSK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 496 RDIRPGAAFE------PTYIYRLLTVNKSSLSeKGRQEDAEEYLGFILNGLHEEmlNLKKLLSPSNE--KLTISN---GP 564
Cdd:cd02658    65 PASLKSENDPyqvgikPSMFKALIGKGHPEFS-TMRQQDALEFLLHLIDKLDRE--SFKNLGLNPNDlfKFMIEDrleCL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 565 KNHSVNeeeqeeqgegsedeweqvgprnktSVTRQADFVQTPItgifgghirsvvyqqsSKESATLQPFFTLQLDIQsdk 644
Cdd:cd02658   142 SCKKVK------------------------YTSELSEILSLPV----------------PKDEATEKEEGELVYEPV--- 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 645 irTVQDALESLVARESVQGYTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDL-----EISK 719
Cdd:cd02658   179 --PLEDCLKAYFAPETIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEELgpgkyELIA 256
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 720 VVYHHGNSATGGHYTTDVFQ--IGLNGWLRIDDQTVkvinqYQVVK-PTAERTAYLLYYR 776
Cdd:cd02658   257 FISHKGTSVHSGHYVAHIKKeiDGEGKWVLFNDEKV-----VASQDpPEMKKLGYIYFYQ 311
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
675-777 5.10e-10

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 62.98  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 675 SRRVTLEKLPPVLVLHLKRFVYEKTGGcQKLIKNIEYPVD-LEISKVVY----------------HHGNSAtGGHYTTDV 737
Cdd:COG5560   708 SKQMELWRLPMILIIHLKRFSSVRSFR-DKIDDLVEYPIDdLDLSGVEYmvddprliydlyavdnHYGGLS-GGHYTAYA 785
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217308113 738 FQIGLNGWLRIDDQTVKVINQYQVVKptaeRTAYLLYYRR 777
Cdd:COG5560   786 RNFANNGWYLFDDSRITEVDPEDSVT----SSAYVLFYRR 821
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
421-775 1.17e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 59.30  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 421 GLINKGNWCYINATLQALVACPpmyhlmkfiplyskvqrpctstpmidSFVRLMNEFTNmpvppkprqalgdkivrdirp 500
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLP--------------------------SLIEYLEEFLE--------------------- 33
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 501 gaafeptyiyrlltvnksslsekgrQEDAEEYLGFILNGLHEEMLNlkkllspsnekltisngpknhsvneeeqeeqgeg 580
Cdd:cd02662    34 -------------------------QQDAHELFQVLLETLEQLLKF---------------------------------- 54
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 581 sedeweqvgprnktsvtrqadfvqtPITGIFgghIRSVVYQQSSKESATLQPFFT-LQLDIQSDKIR---TVQDALESLV 656
Cdd:cd02662    55 -------------------------PFDGLL---ASRIVCLQCGESSKVRYESFTmLSLPVPNQSSGsgtTLEHCLDDFL 106
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 657 ARESVQGYTTKTKQEVeisrrvtLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPvdLEISKVVY-------HHGnSAT 729
Cdd:cd02662   107 STEIIDDYKCDRCQTV-------IVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFP--ERLPKVLYrlravvvHYG-SHS 176
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217308113 730 GGHYTT-----------DVFQIGL---------NGWLRIDDQTVKVINQYQVVkptAERTAYLLYY 775
Cdd:cd02662   177 SGHYVCyrrkplfskdkEPGSFVRmregpsstsHPWWRISDTTVKEVSESEVL---EQKSAYMLFY 239
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
584-775 1.80e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 58.72  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 584 EWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSsKESATLQPFFtlQLDIQSDKIRTVQDALESLVARESVQG 663
Cdd:cd02665    34 DWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG-KPFCNCETFG--QYPLQVNGYGNLHECLEAAMFEGEVEL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 664 ytTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCqKLIKNIEYPVdlEISKVVYH------HGNSATGGHYTTDV 737
Cdd:cd02665   111 --LPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE-KIHDKLEFPQ--IIQQVPYElhavlvHEGQANAGHYWAYI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217308113 738 FQIGLNGWLRIDDQTVKVINQYQVVKPT----AERTAYLLYY 775
Cdd:cd02665   186 YKQSRQEWEKYNDISVTESSWEEVERDSfgggRNPSAYCLMY 227
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
601-753 6.05e-09

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 59.88  E-value: 6.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113  601 DFVQTPITGIFGGHIRSVVY-QQSSKESATLQPFFTLQLDIQSDKirTVQDALESLVARESVQG---YTTKTKQEVEISR 676
Cdd:COG5077    294 TVVENALNGIFVGKMKSYIKcVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGdnrYNAEKHGLQDAKK 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113  677 RVTLEKLPPVLVLHLKRFVYE-KTGGCQKLIKNIEYP--VDL-----------EISKVVYH------HGNSATGGHYTTd 736
Cdd:COG5077    372 GVIFESLPPVLHLQLKRFEYDfERDMMVKINDRYEFPleIDLlpfldrdadksENSDAVYVlygvlvHSGDLHEGHYYA- 450
                          170
                   ....*....|....*...
gi 2217308113  737 VFQIGLNG-WLRIDDQTV 753
Cdd:COG5077    451 LLKPEKDGrWYKFDDTRV 468
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
421-757 1.16e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 48.47  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 421 GLINKGNWCYINATLQALVACPPM--YHLMKfiPLYSKVQRPCTstPMIDSFVRLMNEFTNmpvppkPRQalgdkIVRDI 498
Cdd:cd02669   121 GLNNIKNNDYANVIIQALSHVKPIrnFFLLY--ENYENIKDRKS--ELVKRLSELIRKIWN------PRN-----FKGHV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 499 RPgaafeptyiYRLLtvNKSSLSEKGR-----QEDAEEYLGFILNGLHeemlnlkkllspsneKLTISNGPKNHSVneeE 573
Cdd:cd02669   186 SP---------HELL--QAVSKVSKKKfsiteQSDPVEFLSWLLNTLH---------------KDLGGSKKPNSSI---I 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 574 QEEQGEGSEDEWEQVGPRNKTSVTRQADFVQTpitgifgghirsvvYQQSSKESatlqPFFTLQLDI---------QSDK 644
Cdd:cd02669   237 HDCFQGKVQIETQKIKPHAEEEGSKDKFFKDS--------------RVKKTSVS----PFLLLTLDLpppplfkdgNEEN 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 645 IrTVQDALESLVAResvqgYTTKTKQEVEISR-RVTLEKLPPVLVLHLKRF-----VYEKTGGCQKL-IKN------IEY 711
Cdd:cd02669   299 I-IPQVPLKQLLKK-----YDGKTETELKDSLkRYLISRLPKYLIFHIKRFsknnfFKEKNPTIVNFpIKNldlsdyVHF 372
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217308113 712 PVDLEISKVVY-------HHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVIN 757
Cdd:cd02669   373 DKPSLNLSTKYnlvanivHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVL 425
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
636-775 5.04e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 45.60  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217308113 636 LQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEISR-RVTleKLPPVLVLHLKRFvYEKTGGCQKLIKNIEY--P 712
Cdd:cd02673   100 LDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSeRIM--TFPECLSINLKRY-KLRIATSDYLKKNEEImkK 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217308113 713 VDLEISK-----VVYHHGNSATGGHYTTDVFQI-GLNGWLRIDDQTVKVINQYQVVKpTAERTAYLLYY 775
Cdd:cd02673   177 YCGTDAKyslvaVICHLGESPYDGHYIAYTKELyNGSSWLYCSDDEIRPVSKNDVST-NARSSGYLIFY 244
 
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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