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Conserved domains on  [gi|2739433|gb|AAB94636|]
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hematopoietic-specific IL-2 deubiquitinating enzyme [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119183)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
PubMed:  7845226|11517925
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
50-346 5.61e-149

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: 429.39  E-value: 5.61e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   50 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKP----SQILTSA 125
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfssnLKQISKH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  126 FHKHQQEDAHEFLMFTLETMHESCLQVHRQSE---PTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  203 AQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2739433  283 PTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYV 346
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
50-346 5.61e-149

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: 429.39  E-value: 5.61e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   50 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKP----SQILTSA 125
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfssnLKQISKH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  126 FHKHQQEDAHEFLMFTLETMHESCLQVHRQSE---PTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  203 AQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2739433  283 PTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYV 346
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
51-345 9.22e-96

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 293.96  E-value: 9.22e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433     51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCK--MCAMEAHVtQSLLHSHSGDVMKPSQILTSA--- 125
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInlLCALRDLF-KALQKNSKSSSVSPKMFKKSLgkl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    126 ---FHKHQQEDAHEFLMFTLETMHESCLQVHrqsepTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:pfam00443  80 npdFSGYKQQDAQEFLLFLLDGLHEDLNGNH-----STENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    203 AQSV------NQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFS--AFMGNKLDRKVSYPEFL 274
Cdd:pfam00443 155 DSAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLEL 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2739433    275 DLKPYLSQPTGGPLP----YALYAVLVHEGaTCHSGHYFSYVKA-RHGAWYKMDDTKVTSCDV-TSVLNENAYVLFY 345
Cdd:pfam00443 235 DLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEeTAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
52-373 5.34e-26

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 113.04  E-value: 5.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    52 GLQNTGNSCYLNAALQCLTHTpplaDYMLSQEYSQTCCSPEGCKMCAMEA----HVTQSLLHSHSGDVMKPSQILTSAFH 127
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHPRGRDSVALALqrlfYNLQTGEEPVDTTELTRSFGWDSDDS 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   128 KHQQeDAHEF---LMFTLEtmhesclqvhrQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQ 204
Cdd:COG5077  271 FMQH-DIQEFnrvLQDNLE-----------KSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   205 SVNQALWDTEKSEELRGENAYYCgrcrQK---MPASKTLHIHSAPKVLLLVLKRFSA-F---MGNKLDRKVSYPEFLDLK 277
Cdd:COG5077  339 NLQESFRRYIQVETLDGDNRYNA----EKhglQDAKKGVIFESLPPVLHLQLKRFEYdFerdMMVKINDRYEFPLEIDLL 414
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   278 PYLS----QPTGGPLPYALYAVLVHEGaTCHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNEN------------- 339
Cdd:COG5077  415 PFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEENfggdhpykdkird 493
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 2739433   340 ---------AYVLFYVQQTDLKQV-----SIDMPEgRVHEVLDPEYQL 373
Cdd:COG5077  494 hsgikrfmsAYMLVYLRKSMLDDLlnpvaAVDIPP-HVEEVLSEEIDK 540
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
50-346 5.61e-149

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: 429.39  E-value: 5.61e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   50 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKP----SQILTSA 125
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfssnLKQISKH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  126 FHKHQQEDAHEFLMFTLETMHESCLQVHRQSE---PTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  203 AQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2739433  283 PTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYV 346
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
51-345 9.22e-96

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 293.96  E-value: 9.22e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433     51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCK--MCAMEAHVtQSLLHSHSGDVMKPSQILTSA--- 125
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInlLCALRDLF-KALQKNSKSSSVSPKMFKKSLgkl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    126 ---FHKHQQEDAHEFLMFTLETMHESCLQVHrqsepTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISS 202
Cdd:pfam00443  80 npdFSGYKQQDAQEFLLFLLDGLHEDLNGNH-----STENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    203 AQSV------NQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFS--AFMGNKLDRKVSYPEFL 274
Cdd:pfam00443 155 DSAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLEL 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2739433    275 DLKPYLSQPTGGPLP----YALYAVLVHEGaTCHSGHYFSYVKA-RHGAWYKMDDTKVTSCDV-TSVLNENAYVLFY 345
Cdd:pfam00443 235 DLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEeTAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
52-346 1.72e-69

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: 223.90  E-value: 1.72e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHtppladymlsqeysqtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhQQ 131
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS----------------------------------------------------------EQ 22
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  132 EDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRF----LDVPLDISSAQSVN 207
Cdd:cd02257  23 QDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPElflsLPLPVKGLPQVSLE 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  208 QALWDTEKSEELRGENAYYCGRCRqKMPASKTLHIHSAPKVLLLVLKRFS---AFMGNKLDRKVSYPEFLDLKPYLSQPT 284
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGE 181
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2739433  285 ------GGPLPYALYAVLVHEGATCHSGHYFSYVKAR-HGAWYKMDDTKVTSCDVTSVL-----NENAYVLFYV 346
Cdd:cd02257 182 kdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKDPsDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-346 9.51e-68

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: 221.86  E-value: 9.51e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTC--CSPEGCKMCAMeAHVTQSLLHSHSGDVMKPSQILTSAFHK- 128
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAM-DEIFQEFYYSGDRSPYGPINLLYLSWKHs 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  129 -----HQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDI--- 200
Cdd:cd02660  81 rnlagYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIpnk 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  201 --------SSAQSVNQALW---DTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRF---SAFMGNKLDR 266
Cdd:cd02660 161 stpswalgESGVSGTPTLSdclDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKIDT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  267 KVSYPEFLDLKPYLSQPTGGPLP---------YALYAVLVHEGaTCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLN 337
Cdd:cd02660 241 YVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLK 319

                ....*....
gi 2739433  338 ENAYVLFYV 346
Cdd:cd02660 320 SQAYLLFYH 328
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 3.36e-53

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: 180.18  E-value: 3.36e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHtppladymlsqeysqtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhQQ 131
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA----------------------------------------------------------DQ 22
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  132 EDAHEFLMFTLETMHesclqvhrqseptsedsSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQ------S 205
Cdd:cd02674  23 QDAQEFLLFLLDGLH-----------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvT 85
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  206 VNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSA--FMGNKLDRKVSYP-EFLDLKPYL-S 281
Cdd:cd02674  86 LEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFsrGSTRKLTTPVTFPlNDLDLTPYVdT 165
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2739433  282 QPTGGPLPYALYAVLVHEGaTCHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNENAYVLFY 345
Cdd:cd02674 166 RSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
51-350 6.98e-53

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: 182.84  E-value: 6.98e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   51 CGLQNTGNSCYLNAALQCLTHTPPL--ADYMLSQEYSQTCCSPEGCKM--CAMEAHVTQSLLHSHSGDVMKPS---QILT 123
Cdd:cd02659   3 VGLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDDDNKSVPLALqrLFLFLQLSESPVKTTELTDKTRSfgwDSLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  124 SafhkHQQEDAHEFLMFTLETMHESclqvhrqSEPTSEDSSpIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSA 203
Cdd:cd02659  83 T----FEQHDVQEFFRVLFDKLEEK-------LKGTGQEGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  204 QSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSaF-----MGNKLDRKVSYPEFLDLKP 278
Cdd:cd02659 151 KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE-FdfetmMRIKINDRFEFPLELDMEP 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  279 YLSQ----PTGGPLP-------YALYAVLVHEGaTCHSGHYFSYVKAR-HGAWYKMDDTKVTSCDVTSVLNE-------- 338
Cdd:cd02659 230 YTEKglakKEGDSEKkdsesyiYELHGVLVHSG-DAHGGHYYSYIKDRdDGKWYKFNDDVVTPFDPNDAEEEcfggeetq 308
                       330       340
                ....*....|....*....|....*.
gi 2739433  339 --------------NAYVLFYVQQTD 350
Cdd:cd02659 309 ktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 4.68e-47

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: 166.33  E-value: 4.68e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHT---PPLADYMlsqeYSQTCCSPegckmcameahvtqsllhshSGDVMKPSQILT----- 123
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYFEnllTCLKDLF----ESISEQKK--------------------RTGVISPKKFITrlkre 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  124 -SAFHKHQQEDAHEFLMFTLETMHEsCLQVHRQSEPTSEDSSP----------IHDIFGGLWRSQIKCLHCQGTSDTYDR 192
Cdd:cd02663  57 nELFDNYMHQDAHEFLNFLLNEIAE-ILDAERKAEKANRKLNNnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDET 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  193 FLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFsAFMGN-----KLDRK 267
Cdd:cd02663 136 FLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF-KYDEQlnryiKLFYR 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  268 VSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKArHGAWYKMDDTKVTSCDVTSVLN--------EN 339
Cdd:cd02663 215 VVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENAVEEffgdspnqAT 293

                ....*.
gi 2739433  340 AYVLFY 345
Cdd:cd02663 294 AYVLFY 299
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 2.41e-44

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: 158.32  E-value: 2.41e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqeysqtccspegckmcameahvtqsllhshsgdvmKPSQILTSAFHKH-- 129
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-----------------------------------TPKELFSQVCRKApq 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  130 ----QQEDAHEFLMFTLETMhesclqvhrqseptsedSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPL----DIS 201
Cdd:cd02667  46 fkgyQQQDSHELLRYLLDGL-----------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIK 108
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  202 SAQSVNQALWDTEKSEELRGENAYYCGRCRQkmpASKTLHIHSAPKVLLLVLKRFSA-FMGN--KLDRKVSYPEFLDLKP 278
Cdd:cd02667 109 SECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQpRSANlrKVSRHVSFPEILDLAP 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  279 YLSQPTGGP-----LPYALYAVLVHEGaTCHSGHYFSYVKARH----------------------GAWYKMDDTKVTSCD 331
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
                       330
                ....*....|....
gi 2739433  332 VTSVLNENAYVLFY 345
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 1.26e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 146.87  E-value: 1.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQT-CCSPEGCKMCAMEAHvtqsLLHSHSGDVMKPSQILTSA----F 126
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLgDSQSVMKKLQLLQAH----LMHTQRRAEAPPDYFLEASrppwF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  127 HKHQQEDAHEFLMFTLETMHesclqvhrqseptsedsSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSV 206
Cdd:cd02664  77 TPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  207 nqaLWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFS----AFMGNKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02664 140 ---LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkTHVREKIMDNVSINEVLSLPVRVES 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  283 PTGGP-------------------LPYALYAVLVHEGATCHSGHYFSYvkARHGA-----------------------WY 320
Cdd:cd02664 217 KSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTY--ARDQTdadstgqecpepkdaeendesknWY 294
                       330       340       350
                ....*....|....*....|....*....|..
gi 2739433  321 KMDDTKVTSCDVTSVLN-------ENAYVLFY 345
Cdd:cd02664 295 LFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-327 2.14e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 132.54  E-value: 2.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSqtcCSPEGCKMCAMEAHVTQS----------LLHSHSGDVMKPSQ- 120
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNST---EDAELKNMPPDKPHEPQTiidqlqlifaQLQFGNRSVVDPSGf 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  121 ILTSAFHKHQQEDAHEFLMFTLETMhESCLQVHRQSEPtsedSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDI 200
Cdd:cd02668  78 VKALGLDTGQQQDAQEFSKLFLSLL-EAKLSKSKNPDL----KNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  201 SSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSaFMGNKLDRK-----VSYPEFLD 275
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FDRKTGAKKklnasISFPEILD 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 2739433  276 LKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVK-ARHGAWYKMDDTKV 327
Cdd:cd02668 232 MGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 1.61e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 126.67  E-value: 1.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCC--SPEGCKMCAMeAHVTQSLLhshSGDVMKPSQ--------- 120
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLL---SGRYSKPASlksendpyq 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  121 --ILTSAF-----HKHQ------QEDAHEFLMFTLETMHESCLQVHrQSEPTsedsspihDIFGGLWRSQIKCLHCQ--G 185
Cdd:cd02658  77 vgIKPSMFkaligKGHPefstmrQQDALEFLLHLIDKLDRESFKNL-GLNPN--------DLFKFMIEDRLECLSCKkvK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  186 TSDTYDRFLDVPLDISSAQSVNQalwDTEKSEELRGE-----------NAYYCGRCRQKMPASKTLHIHSAPKVLLLVLK 254
Cdd:cd02658 148 YTSELSEILSLPVPKDEATEKEE---GELVYEPVPLEdclkayfapetIEDFCSTCKEKTTATKTTGFKTFPDYLVINMK 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  255 RFSAFMG---NKLDRKVSYPEFLdlkpylsqptgGPLPYALYAVLVHEGATCHSGHYFSYVK---ARHGAWYKMDDTKVT 328
Cdd:cd02658 225 RFQLLENwvpKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
                       330
                ....*....|....*..
gi 2739433  329 SCDVTSVLNENAYVLFY 345
Cdd:cd02658 294 ASQDPPEMKKLGYIYFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
52-373 5.34e-26

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 113.04  E-value: 5.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    52 GLQNTGNSCYLNAALQCLTHTpplaDYMLSQEYSQTCCSPEGCKMCAMEA----HVTQSLLHSHSGDVMKPSQILTSAFH 127
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHPRGRDSVALALqrlfYNLQTGEEPVDTTELTRSFGWDSDDS 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   128 KHQQeDAHEF---LMFTLEtmhesclqvhrQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQ 204
Cdd:COG5077  271 FMQH-DIQEFnrvLQDNLE-----------KSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   205 SVNQALWDTEKSEELRGENAYYCgrcrQK---MPASKTLHIHSAPKVLLLVLKRFSA-F---MGNKLDRKVSYPEFLDLK 277
Cdd:COG5077  339 NLQESFRRYIQVETLDGDNRYNA----EKhglQDAKKGVIFESLPPVLHLQLKRFEYdFerdMMVKINDRYEFPLEIDLL 414
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   278 PYLS----QPTGGPLPYALYAVLVHEGaTCHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNEN------------- 339
Cdd:COG5077  415 PFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEENfggdhpykdkird 493
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 2739433   340 ---------AYVLFYVQQTDLKQV-----SIDMPEgRVHEVLDPEYQL 373
Cdd:COG5077  494 hsgikrfmsAYMLVYLRKSMLDDLlnpvaAVDIPP-HVEEVLSEEIDK 540
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 1.42e-24

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: 103.95  E-value: 1.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQeysqtccSPEGCKMCAMEAHVTQSLLH-----SHSGDVMKPSqILTSAF 126
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNY-------NPARRGANQSSDNLTNALRDlfdtmDKKQEPVPPI-EFLQLL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  127 HKH-------------QQEDAHEFLMftletmheSCLQVHRQS-EPTSEDSSPIHDIFGGLWRSQIKC------------ 180
Cdd:cd02657  73 RMAfpqfaekqnqggyAQQDAEECWS--------QLLSVLSQKlPGAGSKGSFIDQLFGIELETKMKCtespdeeevste 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  181 ----LHCQGTSDTYDRFLDVPLDISSAQSVnqalwdtEKSEELRGENAYYcgrcrqkmpaSKTLHIHSAPKVLLLVLKRF 256
Cdd:cd02657 145 seykLQCHISITTEVNYLQDGLKKGLEEEI-------EKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRF 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  257 ----SAFMGNKLDRKVSYPEFLDLKPYLSqPTGgplPYALYAVLVHEGATCHSGHYFSYVKARH-GAWYKMDDTKVTSCD 331
Cdd:cd02657 208 fwkrDIQKKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVT 283
                       330       340
                ....*....|....*....|.
gi 2739433  332 VTSVLN-------ENAYVLFY 345
Cdd:cd02657 284 EEDILKlsgggdwHIAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
49-345 1.81e-24

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: 104.20  E-value: 1.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   49 PGCGLQNTGNSCYLNAALQCLTHTP-------PLADYMLSQEYSQTCC--SPEgckmcameaHVTQSLLHSHSGDVMKPS 119
Cdd:cd02671  23 PFVGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSSFllNPE---------KYNDELANQAPRRLLNAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  120 QILTSAFHKHQQEDAHEFLMFTLETMHESclqvhrqseptsedsspIHDIFGGLWRSQIKCLHCQGTSDTYDRFLD--VP 197
Cdd:cd02671  94 REVNPMYEGYLQHDAQEVLQCILGNIQEL-----------------VEKDFQGQLVLRTRCLECETFTERREDFQDisVP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  198 LDISSAQSVNQ--------------ALWDTEK---SEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAfM 260
Cdd:cd02671 157 VQESELSKSEEsseispdpktemktLKWAISQfasVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAA-N 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  261 GNKLD-----RKVSYPEFLDLKPYLSQPTGGPLP--YALYAVLVHEGATCHSGHYFSYVKarhgaWYKMDDTKV------ 327
Cdd:cd02671 236 GSEFDcygglSKVNTPLLTPLKLSLEEWSTKPKNdvYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvteek 310
                       330       340
                ....*....|....*....|.
gi 2739433  328 ---TSCDVTSVLNENAYVLFY 345
Cdd:cd02671 311 dflEALSPNTSSTSTPYLLFY 331
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
214-349 8.48e-23

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 102.65  E-value: 8.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  214 EKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMG--NKLDRKVSYPEF-LDLKPYLSQPTGGPLPY 290
Cdd:COG5560 685 SKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPIDdLDLSGVEYMVDDPRLIY 764
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  291 ALYAVLVHEGATcHSGHYFSYVK-ARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYVQQT 349
Cdd:COG5560 765 DLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
51-200 2.44e-21

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 98.03  E-value: 2.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHS-HSGDV--MKPSQI------ 121
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQlYDGNLhaFTPSGFkktigs 345
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  122 LTSAFHKHQQEDAHEFLMFTLETMHE--SCLQVHRQSE-PTSEDSSPIH---------------------DIFGGLWRSQ 177
Cdd:COG5560 346 FNEEFSGYDQQDSQEFIAFLLDGLHEdlNRIIKKPYTSkPDLSPGDDVVvkkkakecwwehlkrndsiitDLFQGMYKST 425
                       170       180
                ....*....|....*....|...
gi 2739433  178 IKCLHCQGTSDTYDRFLDVPLDI 200
Cdd:COG5560 426 LTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-345 1.26e-18

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 85.11  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMlsQEYSQtccspegckmcameahvtqsllhshsgdvmkpsqiltsafhkhqQ 131
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYL--EEFLE--------------------------------------------Q 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  132 EDAHEFLMFTLETMHESClqvhrqseptsedSSPIHdifgGLWRSQIKCLHCQGTSD-----TYDRFLDVPLDIS-SAQS 205
Cdd:cd02662  35 QDAHELFQVLLETLEQLL-------------KFPFD----GLLASRIVCLQCGESSKvryesFTMLSLPVPNQSSgSGTT 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  206 VNQALWDTEKSEELRGenaYYCGRCRQKmpasktlhIHSAPKVLLLVLKRFSaFMGN----KLDRKVSYPEFldLKPYLs 281
Cdd:cd02662  98 LEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSV-FDGRgtstKNSCKVSFPER--LPKVL- 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  282 qptggplpYALYAVLVHEGaTCHSGHYFSYVKAR---------------------HGAWYKMDDTKVTSCDVTSVLNE-N 339
Cdd:cd02662 163 --------YRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQkS 233

                ....*.
gi 2739433  340 AYVLFY 345
Cdd:cd02662 234 AYMLFY 239
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
52-347 1.76e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 86.01  E-value: 1.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLT-HTPPLADYM---------LSQEYSQtccSPEGCKMCAMEAHVTQSLlhshSGDVMKPSQI 121
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTALW----SSKEHKVGWI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  122 LTSAfhkhQQEDAHEFLMFTLETMHESCL-QVHRQSEPTSED--SSPIHDIFgglwrsQIKCLHCQGTSD----TYDRFL 194
Cdd:COG5533  74 PPMG----SQEDAHELLGKLLDELKLDLVnSFTIRIFKTTKDkkKTSTGDWF------DIIIELPDQTWVnnlkTLQEFI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  195 D-VPLDISSAQSVNqalWDTEKSEELRGENAYYcgrcrqkmpasktLHIHSAPKVLLLVLKRFSAFMGN-KLDRKVSYPE 272
Cdd:COG5533 144 DnMEELVDDETGVK---AKENEELEVQAKQEYE-------------VSFVKLPKILTIQLKRFANLGGNqKIDTEVDEKF 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  273 FLDLKPylsQPTGGPLP---YALYAVLVHEGaTCHSGHYFSYVKaRHGAWYKMDDTKVTSCDVTSVLN---ENAYVLFYV 346
Cdd:COG5533 208 ELPVKH---DQILNIVKetyYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYE 282

                .
gi 2739433  347 Q 347
Cdd:COG5533 283 R 283
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
20-330 7.27e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 76.97  E-value: 7.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   20 QQLHQDEAQVVVELTANDKPSLswecpqgPGC-GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQ---TCCSPEGCK 95
Cdd:cd02669  95 EQISDLDRDPKLSRDLDGKPYL-------PGFvGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYEnikDRKSELVKR 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   96 MC----------AMEAHVTQ----SLLHSHSGdvmKPSQILtsafhkhQQEDAHEFLMFTLETMHeSCLQVHRQSeptse 161
Cdd:cd02669 168 LSelirkiwnprNFKGHVSPhellQAVSKVSK---KKFSIT-------EQSDPVEFLSWLLNTLH-KDLGGSKKP----- 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  162 DSSPIHDIFGGLWR--------------SQIKCLHCQGTSDTYD-RFLDVPLDI------SSAQSVNQ----ALWD---- 212
Cdd:cd02669 232 NSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVsPFLLLTLDLpppplfKDGNEENIipqvPLKQllkk 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  213 -TEKSEELRGENayycgrcrqkmpaSKTLHIHSAPKVLLLVLKRFS--AFMGNKLDRKVSYP-EFLDLKPYLSQPTGGPL 288
Cdd:cd02669 312 yDGKTETELKDS-------------LKRYLISRLPKYLIFHIKRFSknNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSLN 378
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 2739433  289 P---YALYAVLVHEGATCHSGHYFSYVkaRHGA---WYKMDDTKVTSC 330
Cdd:cd02669 379 LstkYNLVANIVHEGTPQEDGTWRVQL--RHKStnkWFEIQDLNVKEV 424
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
53-345 1.96e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 70.25  E-value: 1.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   53 LQNTGNSCYLNAALQCLthtppladymlsqeysqtccspegckmcameahvtqsllhSHSGDVMKpsqiltsAFHKHQQE 132
Cdd:cd02673   2 LVNTGNSCYFNSTMQAL----------------------------------------SSIGKINT-------EFDNDDQQ 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  133 DAHEFLMFTLETMhESCLQVHRQSEPTSEDS----SPIHDIFGGLWRSQIkCLHCQGTSDTYDRFLDVPLDISSAQSVNQ 208
Cdd:cd02673  35 DAHEFLLTLLEAI-DDIMQVNRTNVPPSNIEikrlNPLEAFKYTIESSYV-CIGCSFEENVSDVGNFLDVSMIDNKLDID 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  209 ALWDTEKSEELRGENAyyCGRCRQKMPASKTlHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFldlKPYLSQPTGgpl 288
Cdd:cd02673 113 ELLISNFKTWSPIEKD--CSSCKCESAISSE-RIMTFPECLSINLKRYKLRIATSDYLKKNEEIM---KKYCGTDAK--- 183
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2739433  289 pYALYAVLVHEGATCHSGHYFSYVKARHG--AWYKMDDT---KVTSCDVTSVLNENAYVLFY 345
Cdd:cd02673 184 -YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDeirPVSKNDVSTNARSSGYLIFY 244
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
52-346 3.36e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 70.98  E-value: 3.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPE--------GCKMCAMEAHVTQS-----------LLHSHS 112
Cdd:cd02666   3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterrigGREVSRSELQRSNQfvyelrslfndLIHSNT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  113 GDVmKPSQILT-SAFhkhQQEDAHEFL---MFTLE--TMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQI---KCLHC 183
Cdd:cd02666  83 RSV-TPSKELAyLAL---RQQDVTECIdnvLFQLEvaLEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLvpeSMGNQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  184 QGTSDTYDRFLDVPLDI----------SSAQSVNQAL----------------WDTEKSEELRGENAYYCGRCRQKMPAS 237
Cdd:cd02666 159 PSVRTKTERFLSLLVDVgkkgreivvlLEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRELISMDRYELPSSID 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  238 KTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYpEFLDLKPYlsqptggplPYALYAVLVHEGATCHsGHYFSYVKARH- 316
Cdd:cd02666 239 DIDELIREAIQSESSLVRQAQNELAELKHEIEK-QFDDLKSY---------GYRLHAVFIHRGEASS-GHYWVYIKDFEe 307
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 2739433  317 GAWYKMDDTKVTSCDVTSVLNE------NAYVLFYV 346
Cdd:cd02666 308 NVWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
52-327 5.22e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 66.91  E-value: 5.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433     52 GLQNTGNSCYLNAALQCLTHTPPLadYMLSQEYSQTCCSPEGCKMCAM----------------------------EAHv 103
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPL--RNLALSHLATECLKEHCLLCELgflfdmlekakgkncqasnflralssipEAS- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    104 TQSLL--HSHSGDVMKPSQILTSaFHKhqqedaheFLmftLETMHESCLqvhRQSEPTSEDSSPIHDIFGGLWRSQIKCL 181
Cdd:pfam13423  79 ALGLLdeDRETNSAISLSSLIQS-FNR--------FL---LDQLSSEEN---STPPNPSPAESPLEQLFGIDAETTIRCS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    182 HCQGTSDTYDRFLDVPLDISS-AQSVNQALWDTEKSEELRG----ENAY--YCGRCRQKMPASKTLHIHSAPKVLLLVLK 254
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYPRkPSSNNKKPPNQTFSSILKSslerETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433    255 RFSAFMGNkLDRKVSY--PEFldlKPYLSQPTGGPLP---YALYAVLVHEGATCHSGHYFSYVK--------ARHGAWYK 321
Cdd:pfam13423 224 LTNEEWRQ-LWKTPGWlpPEI---GLTLSDDLQGDNEivkYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQWYL 299

                  ....*.
gi 2739433    322 MDDTKV 327
Cdd:pfam13423 300 FNDFLV 305
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
130-346 1.06e-06

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: 49.86  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  130 QQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGlwRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQA 209
Cdd:cd02665  21 QQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYG--TFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHEC 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  210 LWDTEKSEELRGENAYYCGRCRQKMPASKTlhihsaPKVLLLVLKRFS--AFMGNKLDRKVSYPEFLDlkpylsqptggP 287
Cdd:cd02665  99 LEAAMFEGEVELLPSDHSVKSGQERWFTEL------PPVLTFELSRFEfnQGRPEKIHDKLEFPQIIQ-----------Q 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2739433  288 LPYALYAVLVHEGATcHSGHYFSYVKARH-GAWYKMDDTKVTSCDVTSV--------LNENAYVLFYV 346
Cdd:cd02665 162 VPYELHAVLVHEGQA-NAGHYWAYIYKQSrQEWEKYNDISVTESSWEEVerdsfgggRNPSAYCLMYI 228
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
245-345 1.79e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 46.37  E-value: 1.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  245 APKVLLLVLKRFSAFMGN--KLDRKVSYPEFLDLKPYL----------------------SQPTGGPLPYALYAVLVHEG 300
Cdd:cd02670  98 APSCLIICLKRYGKTEGKaqKMFKKILIPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCHRG 177
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2739433  301 ATCHSGHYFSYVK------------ARHGAWYK---MDDTKVTSCDV---TSVLNENAYVLFY 345
Cdd:cd02670 178 TSLETGHYVAFVRygsysltetdneAYNAQWVFfddMADRDGVSNGFnipAARLLEDPYMLFY 240
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
51-345 4.93e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 45.20  E-value: 4.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433   51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQeysQTCCSPEGCKMCAMeahvtqsllhshsgdvmkpsQILTSAFHKhq 130
Cdd:cd02672  16 AGLENHITNSYCNSLLQLLYFIPPFRNFTAII---LVACPKESCLLCEL--------------------GYLFSTLIQ-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  131 qedahEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDifgglwrsqikclhcqgtsdtydrfLDVPLDISSAQSVNQAL 210
Cdd:cd02672  71 -----NFTRFLLETISQDQLGTPFSCGTSRNSVSLLYT-------------------------LSLPLGSTKTSKESTFL 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739433  211 WDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLK-RFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLP 289
Cdd:cd02672 121 QLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLViNLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDK 200
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2739433  290 ------------YALYAVLVHEGATCHSGHYFSYV-----KARHGAWYKMDDTKVTSCDvtsvlnENAYVLFY 345
Cdd:cd02672 201 lvknrgqesiykYELVGYVCEINDSSRGQHNVVFVikvneESTHGRWYLFNDFLVTPVS------ELAYILLY 267
 
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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