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Conserved domains on  [gi|27371223|gb|AAH41366|]
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USP2 protein [Homo sapiens]

Protein Classification

similar to ubl carboxyl-terminal hydrolase (domain architecture ID 11995783)

protein similar to ubl carboxyl-terminal hydrolase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
24-353 3.71e-112

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 306860  Cd Length: 308  Bit Score: 333.20  E-value: 3.71e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223    24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpNDVVSPSEFKTQIQRY 103
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRISPLSEDSRYNKDIGQLLCALADLFKALQSSK-SSSVSPKEFKNTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   104 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKSSLTCT 183
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGVNLT--------------------------ENESLITDLFRGQLKSRLKCL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   184 DCGYCSTVFDPFWDLSLPIAKRGYPevtLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS 263
Cdd:pfam00443 134 NCGKESVTYEPFLDLSLPIPSAKNY---LQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFS 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   264 ESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPM 338
Cdd:pfam00443 211 YNRSTPEKLNTEVEFPE-ELDLSEYLAEGLkpktnNLQKYRLVAVVVHSGSLSSGHYIAYIKKYENGRWYKFDDEKVTEV 289
                         330
                  ....*....|....*....
gi 27371223   339 SSSQV----RTSDAYLLFY 353
Cdd:pfam00443 290 DEEEVlnvkVSSSAYILFY 308
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
24-353 3.71e-112

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 306860  Cd Length: 308  Bit Score: 333.20  E-value: 3.71e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223    24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpNDVVSPSEFKTQIQRY 103
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRISPLSEDSRYNKDIGQLLCALADLFKALQSSK-SSSVSPKEFKNTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   104 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKSSLTCT 183
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGVNLT--------------------------ENESLITDLFRGQLKSRLKCL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   184 DCGYCSTVFDPFWDLSLPIAKRGYPevtLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS 263
Cdd:pfam00443 134 NCGKESVTYEPFLDLSLPIPSAKNY---LQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFS 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   264 ESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPM 338
Cdd:pfam00443 211 YNRSTPEKLNTEVEFPE-ELDLSEYLAEGLkpktnNLQKYRLVAVVVHSGSLSSGHYIAYIKKYENGRWYKFDDEKVTEV 289
                         330
                  ....*....|....*....
gi 27371223   339 SSSQV----RTSDAYLLFY 353
Cdd:pfam00443 290 DEEEVlnvkVSSSAYILFY 308
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 7.40e-107

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  Cd Length: 230  Bit Score: 316.54  E-value: 7.40e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 prfvgyNQQDAQEFLRFLLDGLHnevnrvtlrpksnpenldhlpddekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 184
Cdd:cd02674  21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 185 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02674  57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 263 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSS 340
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
                       330
                ....*....|....
gi 27371223 341 SQVRTSDAYLLFYE 354
Cdd:cd02674 217 SSVVSSSAYILFYE 230
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
1-357 5.76e-58

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


Pssm-ID: 227820  Cd Length: 415  Bit Score: 196.40  E-value: 5.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   1 MLVPGSTRPSSKKRQNSKSAQGL--AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTA---LVEEF 75
Cdd:COG5533  47 LDPHFMELANPKKMVVSKRKDNLppNGLRNKGNTCYMNCALQCLLSIGDLNTMLQGRFYLQNINTDFPRGKPgsnAFKQF 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  76 AKLIQTIWTSSPNDVvSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVN----RVTLRPKSNPEN--LDHLPD 149
Cdd:COG5533 127 IALYETPGCHGPKSI-SPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHEDLNgnksRSPILELKDEFEevREELPL 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 150 DEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKrgYPEVTLMDCMRLFTKEDVLDGDE 229
Cdd:COG5533 206 SHFSHHEWNLHLRSNKSLVAKTFFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYE--VVQLGLQECIDRFYEEEKLEGKD 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 230 KPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTT----FVNFPLRDLDLREFASENTNHAV-YNLYAVS 304
Cdd:COG5533 284 AWRCPKCGRKESSRKRMEILVLPDVLIIHISRFHISVMGRKKIDTpqgwKNTASVEVNVTLLFNNGIGYIPRkYSLLGVV 363
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 27371223 305 NHSGTTMGGHYTAYCRSpgTGEWHTFNDSSVTPMS-SSQVRTSDAYLLFYELAS 357
Cdd:COG5533 364 CHNGTLNGGHYFSEVKR--SGTWNVYDDSQVRKGSrTTSGSHPSSYILFYTRSS 415
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
24-353 3.71e-112

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 306860  Cd Length: 308  Bit Score: 333.20  E-value: 3.71e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223    24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpNDVVSPSEFKTQIQRY 103
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRISPLSEDSRYNKDIGQLLCALADLFKALQSSK-SSSVSPKEFKNTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   104 APRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKSSLTCT 183
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGVNLT--------------------------ENESLITDLFRGQLKSRLKCL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   184 DCGYCSTVFDPFWDLSLPIAKRGYPevtLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS 263
Cdd:pfam00443 134 NCGKESVTYEPFLDLSLPIPSAKNY---LQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFS 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   264 ESRIRTSKLTTFVNFPLrDLDLREFASENT-----NHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPM 338
Cdd:pfam00443 211 YNRSTPEKLNTEVEFPE-ELDLSEYLAEGLkpktnNLQKYRLVAVVVHSGSLSSGHYIAYIKKYENGRWYKFDDEKVTEV 289
                         330
                  ....*....|....*....
gi 27371223   339 SSSQV----RTSDAYLLFY 353
Cdd:pfam00443 290 DEEEVlnvkVSSSAYILFY 308
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 7.40e-107

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  Cd Length: 230  Bit Score: 316.54  E-value: 7.40e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 prfvgyNQQDAQEFLRFLLDGLHnevnrvtlrpksnpenldhlpddekgrqmwrkyleredSRIGDLFVGQLKSSLTCTD 184
Cdd:cd02674  21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 185 CGYCSTVFDPFWDLSLPIAK--RGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02674  57 CGKTSTTFEPFTYLSLPIPSgsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF 136
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 263 SESRIRTSKLTTFVNFPLRDLDLREF--ASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSS 340
Cdd:cd02674 137 SFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
                       330
                ....*....|....
gi 27371223 341 SQVRTSDAYLLFYE 354
Cdd:cd02674 217 SSVVSSSAYILFYE 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
25-354 3.56e-74

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  Cd Length: 255  Bit Score: 233.91  E-value: 3.56e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNtrelrdyclqrlymrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 prfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRpksnpenldhlpddekgrqmwRKYLEREDSRIGDLFVGQLKSSLTCTD 184
Cdd:cd02257  21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 185 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKpTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS- 263
Cdd:cd02257  74 CGHESVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNC-YKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSf 152
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 264 ESRIRTSKLTTFVNFPLRdLDLREFASENT-------NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDSSV 335
Cdd:cd02257 153 NEDGTKEKLNTKVSFPLE-LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKV 231
                       330       340
                ....*....|....*....|....
gi 27371223 336 TPMSSSQV-----RTSDAYLLFYE 354
Cdd:cd02257 232 TEVSEEEVlefgsLSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-353 6.81e-74

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  Cd Length: 304  Bit Score: 234.48  E-value: 6.81e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKliQTIWTSSPNDVvsPSEFKTQIQRY 103
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVE--RALASSGPGSA--PRIFSSNLKQI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 104 APRFVGYNQQDAQEFLRFLLDGLHnevnRVTLRPKSNPENLDHLpddekgrqmwrkylEREDSRIGDLFVGQLKSSLTCT 183
Cdd:cd02661  78 SKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS--------------SQETTLVQQIFGGYLRSQVKCL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 184 DCGYCSTVFDPFWDLSLPIAKRGypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFS 263
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 264 EsrIRTSKLTTFVNFPLRdLDLREFASENT-NHAVYNLYAVSNHSGTTM-GGHYTAYCRSPgTGEWHTFNDSSVTPMSSS 341
Cdd:cd02661 216 N--FRGGKINKQISFPET-LDLSPYMSQPNdGPLKYKLYAVLVHSGFSPhSGHYYCYVKSS-NGKWYNMDDSKVSPVSIE 291
                       330
                ....*....|..
gi 27371223 342 QVRTSDAYLLFY 353
Cdd:cd02661 292 TVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-353 2.07e-63

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  Cd Length: 328  Bit Score: 208.38  E-value: 2.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELRDYclqrlYMRDLHH----GSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQI 100
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNY-----FLSDRHSctclSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 101 QRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpKSNPENLDHLPddekgrqmwrkyleredSRIGDLFVGQLKSSL 180
Cdd:cd02660  77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD----KNEANDESHCN-----------------CIIHQTFSGSLQSSV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 181 TCTDCGYCSTVFDPFWDLSLPI-----------AKRGYPEVTLMDCMRLFTKEDVLdGDEKPTCCRCRGRKRCIKKFSIQ 249
Cdd:cd02660 136 TCQRCGGVSTTVDPFLDLSLDIpnkstpswalgESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIK 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 250 RFPKILVLHLKRFSESRIRTS-KLTTFVNFPLRdLDLREFAS----------ENTNHAVYNLYAVSNHSGTTMGGHYTAY 318
Cdd:cd02660 215 KLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTSssigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTAY 293
                       330       340       350
                ....*....|....*....|....*....|....*
gi 27371223 319 CRSpGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFY 353
Cdd:cd02660 294 CRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 1.58e-59

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  Cd Length: 279  Bit Score: 196.45  E-value: 1.58e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELRDYCLQRlymrdlhhgsnahtalveefakliqtiwtsspndvvsPSEFKTQIQRYA 104
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------------------------------PKELFSQVCRKA 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 184
Cdd:cd02667  44 PQFKGYQQQDSHELLRYLLDGLRTFIDSI--------------------------------------FGGELTSTIMCES 85
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 185 CGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKptcCRCRGRKRCIKKFSIQRFPKILVLHLKRFS- 263
Cdd:cd02667  86 CGTVSLVYEPFLDLSLPRSDEIKSECSIESCLKQFTEVEILEGNNK---FACENCTKAKKQYLISKLPPVLVIHLKRFQq 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 264 ESRIRTSKLTTFVNFPLRdLDLREFASENTNHA------VYNLYAVSNHSGTTMGGHYTAYCRS---------------- 321
Cdd:cd02667 163 PRSANLRKVSRHVSFPEI-LDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpa 241
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 27371223 322 -----PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:cd02667 242 adeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
1-357 5.76e-58

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


Pssm-ID: 227820  Cd Length: 415  Bit Score: 196.40  E-value: 5.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   1 MLVPGSTRPSSKKRQNSKSAQGL--AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTA---LVEEF 75
Cdd:COG5533  47 LDPHFMELANPKKMVVSKRKDNLppNGLRNKGNTCYMNCALQCLLSIGDLNTMLQGRFYLQNINTDFPRGKPgsnAFKQF 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  76 AKLIQTIWTSSPNDVvSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVN----RVTLRPKSNPEN--LDHLPD 149
Cdd:COG5533 127 IALYETPGCHGPKSI-SPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHEDLNgnksRSPILELKDEFEevREELPL 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 150 DEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKrgYPEVTLMDCMRLFTKEDVLDGDE 229
Cdd:COG5533 206 SHFSHHEWNLHLRSNKSLVAKTFFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYE--VVQLGLQECIDRFYEEEKLEGKD 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 230 KPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTT----FVNFPLRDLDLREFASENTNHAV-YNLYAVS 304
Cdd:COG5533 284 AWRCPKCGRKESSRKRMEILVLPDVLIIHISRFHISVMGRKKIDTpqgwKNTASVEVNVTLLFNNGIGYIPRkYSLLGVV 363
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 27371223 305 NHSGTTMGGHYTAYCRSpgTGEWHTFNDSSVTPMS-SSQVRTSDAYLLFYELAS 357
Cdd:COG5533 364 CHNGTLNGGHYFSEVKR--SGTWNVYDDSQVRKGSrTTSGSHPSSYILFYTRSS 415
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
10-202 3.18e-49

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


Pssm-ID: 227847  Cd Length: 823  Bit Score: 177.77  E-value: 3.18e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  10 SSKKRQNSKSAQ--GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGS--NAHTALVEEFAKLIQTIWTS 85
Cdd:COG5560 250 SIVDDHNRSINKeaGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENplGMHGSVASAYADLIKQLYDG 329
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  86 SpNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENL---DHLPDDEKGRQMWRKYLE 162
Cdd:COG5560 330 N-LHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLspgDDVVVKKKAKECWWEHLK 408
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27371223 163 REDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPI 202
Cdd:COG5560 409 RNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
22-358 6.79e-43

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  Cd Length: 334  Bit Score: 153.95  E-value: 6.79e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  22 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlyMRDLHHGSNAH---TALVEEFAKLiQTiwtsSPNDVVSPSEFKT 98
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYS---IPPTEDDDDNKsvpLALQRLFLFL-QL----SESPVKTTELTDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  99 QiqryapRFVG------YNQQDAQEFLRFLLDglhnevnrvtlrpksnpeNLDHlpddekgrqMWrKYLEREDSrIGDLF 172
Cdd:cd02659  73 T------RSFGwdslntFEQHDVQEFFRVLFD------------------KLEE---------KL-KGTGQEGL-IKNLF 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 173 VGQLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYpeVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFP 252
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAV--KGK--KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLP 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 253 KILVLHLKRF-----SESRIrtsKLTTFVNFPLRdLDLREFASENTNH------------AVYNLYAVSNHSGTTMGGHY 315
Cdd:cd02659 194 PVLTLQLKRFefdfeTMMRI---KINDRFEFPLE-LDMEPYTEKGLAKkegdsekkdsesYIYELHGVLVHSGDAHGGHY 269
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27371223 316 TAYCRSPGTGEWHTFNDSSVTPMSSSQV----------------------RTSDAYLLFYELASP 358
Cdd:cd02659 270 YSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFYERKSP 334
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 2.73e-37

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  Cd Length: 300  Bit Score: 138.21  E-value: 2.73e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELrdYCLqrlymRDLHHGSNAHTALVeefakliqtiwtsspnDVVSPSEFKTQIQRYA 104
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYFENLL--TCL-----KDLFESISEQKKRT----------------GVISPKKFITRLKREN 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLR-PKSNPENLDHLPDDEKGrqmWrkyleredsrIGDLFVGQLKSSLTCT 183
Cdd:cd02663  58 ELFDNYMHQDAHEFLNFLLNEIAEILDAERKAeKANRKLNNNNNAEPQPT---W----------VHEIFQGILTNETRCL 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 184 DCGYCSTVFDPFWDLSLPIakrgYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF- 262
Cdd:cd02663 125 TCETVSSRDETFLDLSIDV----EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFk 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 263 -SESRIRTSKLTTFVNFPlrdLDLREFASENTNHAV---YNLYAVSNHSGTT-MGGHYTAYCRSpgTGEWHTFNDSSVTP 337
Cdd:cd02663 201 yDEQLNRYIKLFYRVVFP---LELRLFNTTDDAENPdrlYELVAVVVHIGGGpNHGHYVSIVKS--HGGWLLFDDETVEK 275
                       330       340
                ....*....|....*....|....*
gi 27371223 338 MSSSQVR--------TSDAYLLFYE 354
Cdd:cd02663 276 IDENAVEeffgdspnQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 8.12e-37

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  Cd Length: 324  Bit Score: 137.55  E-value: 8.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELRDY-----CLQRLYMRDLHHGSNAH-TALVEEFAKLIQTIWTSSPNdVVSPSEFKT 98
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAvyecnSTEDAELKNMPPDKPHEpQTIIDQLQLIFAQLQFGNRS-VVDPSGFVK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  99 qiqryAPRFVGYNQQDAQEFLRFLLDGLHNevnrvTLRPKSNPenldhlpddeKGRQMwrkyleredsrIGDLFVGQLKS 178
Cdd:cd02668  80 -----ALGLDTGQQQDAQEFSKLFLSLLEA-----KLSKSKNP----------DLKNI-----------VQDLFRGEYSY 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 179 SLTCTDCGYCSTVFDPFWDLSLPIAKrgypEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLH 258
Cdd:cd02668 129 VTQCSKCGRESSLPSKFYELELQLKG----HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 259 LKRFSESRIRTS--KLTTFVNFPLrDLDLREF-ASENTNHAVYNLYAVSNHSGT-TMGGHYTAYCRSPGTGEWHTFNDSS 334
Cdd:cd02668 205 LLRFVFDRKTGAkkKLNASISFPE-ILDMGEYlAESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDED 283
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 27371223 335 VTPMSSSQVR---------------------TSDAYLLFYE 354
Cdd:cd02668 284 VEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 5.52e-36

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  Cd Length: 305  Bit Score: 134.77  E-value: 5.52e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELRDYCLQrlYMRDLHHGSNAHTALVEEFAKLIQTIWTSSpnDVVSPSEFKTQIQRYA 104
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKN--YNPARRGANQSSDNLTNALRDLFDTMDKKQ--EPVPPIEFLQLLRMAF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 PRFV------GYNQQDAQEFLRFLLDGLHNEvnrvtLRPKSnpenldhlpddekgrqmwrkyleREDSRIGDLFVGQLKS 178
Cdd:cd02657  77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQK-----LPGAG-----------------------SKGSFIDQLFGIELET 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 179 SLTCTDCGYCSTV-FDPFWDLSLPIAkrgypevTLMDCMRLFTK-EDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILV 256
Cdd:cd02657 129 KMKCTESPDEEEVsTESEYKLQCHIS-------ITTEVNYLQDGlKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLT 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 257 LHLKRFS--ESRIRTSKLTTFVNFPLrDLDLREFAsenTNHAVYNLYAVSNHSGTTM-GGHYTAYCRSPGTGEWHTFNDS 333
Cdd:cd02657 202 VQFVRFFwkRDIQKKAKILRKVKFPF-ELDLYELC---TPSGYYELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDD 277
                       330       340
                ....*....|....*....|....*...
gi 27371223 334 SVTPMSSSQVRTSD-------AYLLFYE 354
Cdd:cd02657 278 KVSEVTEEDILKLSgggdwhiAYILLYK 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
208-354 1.39e-31

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


Pssm-ID: 227847  Cd Length: 823  Bit Score: 126.92  E-value: 1.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 208 PEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLRE 287
Cdd:COG5560 673 RTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSG 752
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27371223 288 FASENTNHAV-YNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:COG5560 753 VEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
4-353 8.45e-31

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  Cd Length: 332  Bit Score: 120.77  E-value: 8.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   4 PGSTRPSSKKRQNSKSaqgLAGLRNLGNTCFMNSILQCLSntrelrdYCLQrlYMRDLHHGSNAHTALVEefaklIQTIW 83
Cdd:cd02671   8 QPSSATSCEKRENLLP---FVGLNNLGNTCYLNSVLQVLY-------FCPG--FKHGLKHLVSLISSVEQ-----LQSSF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  84 TSSPNDVVS------PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlrpksnpenldhlpddekgrqmw 157
Cdd:cd02671  71 LLNPEKYNDelanqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK------------------------- 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 158 rkyleredsrigdLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEV---------------TLMDCMRLFTKE 222
Cdd:cd02671 126 -------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSeesseispdpktemkTLKWAISQFASV 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 223 DVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRT------SKLTTFVNFPLrDLDLREFASENTNHa 296
Cdd:cd02671 193 ERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPL-KLSLEEWSTKPKND- 270
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27371223 297 VYNLYAVSNHSGTTMG-GHYTAYCRspgtgeWHTFNDSSVTPM---------SSSQVRTSDAYLLFY 353
Cdd:cd02671 271 VYRLFAVVMHSGATISsGHYTAYVR------WLLFDDSEVKVTeekdflealSPNTSSTSTPYLLFY 331
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
22-354 1.12e-30

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  Cd Length: 440  Bit Score: 121.66  E-value: 1.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  22 GLAGLRNLGNTCFMNSILQCLSNTRELRDYCLqrLYMRDLHHGSNAhTALVEEFAKLIQTIWtsSPND---VVSPSEFKT 98
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--LYENYENIKDRK-SELVKRLSELIRKIW--NPRNfkgHVSPHELLQ 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  99 QIQRYAPRFVGYNQQ-DAQEFLRFLLDGLHNEVNRVTlrpKSNPENLDHLPDDEKgRQMWRKYLEREDSrigdlfvgqLK 177
Cdd:cd02669 193 AVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSK---KPNSSIIHDCFQGKV-QIETQKIKPHAEE---------EG 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 178 SSLTCTDCGYCSTVFD-PFWDLSL-----PIAKRGY-----PEVTLMDcmrLFTKedvLDGDEKPTCCRCrgrkrcIKKF 246
Cdd:cd02669 260 SKDKFFKDSRVKKTSVsPFLLLTLdlpppPLFKDGNeeniiPQVPLKQ---LLKK---YDGKTETELKDS------LKRY 327
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 247 SIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTN----HAVYNLYAVSNHSGTTMG-GHYTAYCRS 321
Cdd:cd02669 328 LISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPslnlSTKYNLVANIVHEGTPQEdGTWRVQLRH 407
                       330       340       350
                ....*....|....*....|....*....|...
gi 27371223 322 PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:cd02669 408 KSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 2.66e-29

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  Cd Length: 311  Bit Score: 115.88  E-value: 2.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELrdyclQRLYMRDLHHGSNA----HTALVEEFAKLIQTIWT---SSPNDVVS----- 92
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSF-----QWRYDDLENKFPSDvvdpANDLNCQLIKLADGLLSgrySKPASLKSendpy 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  93 -----PSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRvtlRPKSNPENLdhlpddekgrqmwRKYLEREdsr 167
Cdd:cd02658  76 qvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFK---NLGLNPNDL-------------FKFMIED--- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 168 igdlfvgqlksSLTCTDCGYCSTVFDPFWDLSLPI----------AKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR 237
Cdd:cd02658 137 -----------RLECLSCKKVKYTSELSEILSLPVpkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTT 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 238 GrkrcIKKFSIQRFPKILVLHLKRFsesrirtsklTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT-TMGGHYT 316
Cdd:cd02658 206 A----TKTTGFKTFPDYLVINMKRF----------QLLENWVPKKLDVPIDVPEELGPGKYELIAFISHKGTsVHSGHYV 271
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 27371223 317 AYCRSP--GTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYE 354
Cdd:cd02658 272 AHIKKEidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 1.36e-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: 239127  Cd Length: 240  Bit Score: 109.76  E-value: 1.36e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRELRDYcLQRLYmrdlhhgsnahtalveefakliqtiwtsspndvvspsefktqiqrya 104
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEY-LEEFL----------------------------------------------- 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 prfvgyNQQDAQEFLRFLLDGLHNEVnrvtlrpkSNPenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 184
Cdd:cd02662  33 ------EQQDAHELFQVLLETLEQLL--------KFP------------------------------FDGLLASRIVCLQ 68
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 185 CGYCSTV-FDPFWDLSLPI-AKRGYPEVTLMDCMRLFTKEDVLDGdekptccrcrgRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02662  69 CGESSKVrYESFTMLSLPVpNQSSGSGTTLEHCLDDFLSTEIIDD-----------YKCDRCQTVIVRLPQILCIHLSRS 137
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 263 SESRIRTS-KLTTFVNFPLRdldlrefasenTNHAVYNLYAVSNHSGTTMGGHYTAYCRSP------------------- 322
Cdd:cd02662 138 VFDGRGTStKNSCKVSFPER-----------LPKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkepgsfvrmregps 206
                       330       340       350
                ....*....|....*....|....*....|....
gi 27371223 323 -GTGEWHTFNDSSVTPMSSSQVR-TSDAYLLFYE 354
Cdd:cd02662 207 sTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-354 6.27e-26

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  Cd Length: 327  Bit Score: 106.42  E-value: 6.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  25 GLRNLGNTCFMNSILQCLSNTRelrDYCLQRLyMRDLHHGSNAHTALVEEfaKLIQTIWTSSPNDVVSPSEFKTQIQRyA 104
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAK---DFRRQVL-SLNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEAPPDYFLEASR-P 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 105 PRFVGYNQQDAQEFLRFLLDGLHNEVNRVtlrpksnpenldhlpddekgrqmwrkyleredsrigdlFVGQLKSSLTCTD 184
Cdd:cd02664  74 PWFTPGSQQDCSEYLRYLLDRLHTLIEKM--------------------------------------FGGKLSTTIRCLN 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 185 CGYCSTVFD--PFWDLSLPiakrgypevTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRF 262
Cdd:cd02664 116 CNSTSARTErfRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRF 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 263 S---ESRIRTsKLTTFVNFPL-------------------RDLDLREFASENTNHAVYNLYAVSNHSGTTM-GGHYTAYC 319
Cdd:cd02664 187 SydqKTHVRE-KIMDNVSINEvlslpvrveskssesplekKEEESGDDGELVTRQVHYRLYAVVVHSGYSSeSGHYFTYA 265
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371223 320 RSPGTGE--------------------WHTFNDSSVTPMSSSQV-------RTSDAYLLFYE 354
Cdd:cd02664 266 RDQTDADstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
16-343 6.31e-24

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


Pssm-ID: 227409  Cd Length: 1089  Bit Score: 103.80  E-value: 6.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   16 NSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRD-----------------YCLQRLY--MRDLHHGSNAhTALVEEFa 76
Cdd:COG5077  186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKdvygiptdhprgrdsvaLALQRLFynLQTGEEPVDT-TELTRSF- 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   77 kliqtIWTSspndvvspsefktqiqryaprFVGYNQQDAQEFLRFLLDGLHNEVNrvtlrpKSNPENLdhlpddekgrqm 156
Cdd:COG5077  264 -----GWDS---------------------DDSFMQHDIQEFNRVLQDNLEKSMR------GTVVENA------------ 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  157 wrkyleredsrIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIakRGYPevTLMDCMRLFTKEDVLDGDEKptCCRC 236
Cdd:COG5077  300 -----------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK--NLQESFRRYIQVETLDGDNR--YNAE 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  237 RGRKRCIKKFSI-QRFPKILVLHLKRFSESRIRTS--KLTTFVNFPLrDLDLREF------ASENTNHaVYNLYAVSNHS 307
Cdd:COG5077  363 KHGLQDAKKGVIfESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPL-EIDLLPFldrdadKSENSDA-VYVLYGVLVHS 440
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 27371223  308 GTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV 343
Cdd:COG5077  441 GDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-353 1.58e-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: 239131  Cd Length: 343  Bit Score: 67.90  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  24 AGLRNLGNTCFMNSILQCLSNTRELRDYCLQrlymrdlHHGSNAHTALVEEFAKLIqtiwtssPNDVVSPSEFKTQIQ-- 101
Cdd:cd02666   2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLN-------FDESKAELASDYPTERRI-------GGREVSRSELQRSNQfv 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 102 ---------------RYA-PR----FVGYNQQDAQEFLRFLLDGLhnevnRVTLRPKSNpENLDHLPDDEKgrqmwrkyl 161
Cdd:cd02666  68 yelrslfndlihsntRSVtPSkelaYLALRQQDVTECIDNVLFQL-----EVALEPISN-AFAGPDTEDDK--------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 162 EREDsRIGDLFVGQLKSSLTCTDCGYCSTVFDP---FWDLSLPIAKRGYPEVT------LMDCM-RLFTKEDVLDGDEKP 231
Cdd:cd02666 133 EQSD-LIKRLFSGKTKQQLVPESMGNQPSVRTKterFLSLLVDVGKKGREIVVllepkdLYDALdRYFDYDSLTKLPQRS 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 232 TCCRCRGRKRCIKKFSIQRF-PKILVLHLKRFSESRIRT-SKLTTFVNFPLRDLD-LREFASENTNHAVYNLYAVSNHSG 308
Cdd:cd02666 212 QVQAQLAQPLQRELISMDRYeLPSSIDDIDELIREAIQSeSSLVRQAQNELAELKhEIEKQFDDLKSYGYRLHAVFIHRG 291
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 27371223 309 TTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV----RTSDA--YLLFY 353
Cdd:cd02666 292 EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftLGNTAtpYFLVY 342
UBP14 COG5207
Uncharacterized Zn-finger protein, UBP-type [General function prediction only];
10-273 1.60e-12

Uncharacterized Zn-finger protein, UBP-type [General function prediction only];


Pssm-ID: 227532  Cd Length: 749  Bit Score: 68.55  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  10 SSKKRQNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDY--CLQRLYMRDLhhgSNAHTALVEEFAKLIQTIWTSSP 87
Cdd:COG5207 290 RAPESKGESVPSPYVGLINLGNSCYLSSVIQSLVGYAVSKEEfdLLQHFEICYM---KNPLECLFCQLMKLLSKMKETPD 366
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  88 N---DVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDglhnevnrvtlrpksnpenldhlpddeKGRQMWRKYLEre 164
Cdd:COG5207 367 NeyvNGISPLDFKMLIGQDHPEFGKFAQQDAHEFLLFLLE---------------------------KIRKGERSYLI-- 417
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 165 dSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIaKRGYPEVTLMDCMRLFTKEDVLDGdekpTCCRCRGRKRCIK 244
Cdd:COG5207 418 -PPITSLFEFEVERRLSCSGCMDVSYSYESMLMICIFL-EGNDEPQDIRKSVEAFFLPDTIEW----SCENCKGKKKASR 491
                       250       260
                ....*....|....*....|....*....
gi 27371223 245 KFSIQRFPKILVLHLKRFSESRIRTSKLT 273
Cdd:COG5207 492 KPFIKSLPKYLILQVGRYSLQNYKVEKLS 520
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
26-354 1.83e-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: 239138  Cd Length: 245  Bit Score: 66.40  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223  26 LRNLGNTCFMNSILQCLSNTRELRdyclqrlymrdlhhgsnahtalvEEFAkliqtiwtsspNDvvspsefktqiqryap 105
Cdd:cd02673   2 LVNTGNSCYFNSTMQALSSIGKIN-----------------------TEFD-----------ND---------------- 31
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 106 rfvgyNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKgrqmwrkyleredsrigdlFVGQLKSSLTCTDC 185
Cdd:cd02673  32 -----DQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLEA-------------------FKYTIESSYVCIGC 87
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 186 GYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDvldgdEKPTCCRCRGRKRCIKKFSiqRFPKILVLHLKRFsES 265
Cdd:cd02673  88 SFEENVSDVGNFLDVSMIDNKLDIDELLISNFKTWSPI-----EKDCSSCKCESAISSERIM--TFPECLSINLKRY-KL 159
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 266 RIRTSKLttfvnfpLRD--LDLREFASEntnHAVYNLYAVSNHSG-TTMGGHYTAYCRSPGTG-EWHTFNDSSVTPMSSS 341
Cdd:cd02673 160 RIATSDY-------LKKneEIMKKYCGT---DAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKN 229
                       330
                ....*....|....*.
gi 27371223 342 QVR---TSDAYLLFYE 354
Cdd:cd02673 230 DVStnaRSSGYLIFYD 245
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
24-335 5.38e-09

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 315986  Cd Length: 295  Bit Score: 56.65  E-value: 5.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223    24 AGLRNLGNTCFMNSILQCLSNTRELR--------DYCLQR----------LYMRDLHHGSNAHTAlveefaKLIQTIWTS 85
Cdd:pfam13423   1 SGLENHLDNSYLNALLQLYFFIPDLFeailghsfDECPPEncllcelgflFDMLDKSNGQNCQAT------NFLRTFSTI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223    86 SpndvvspsEFKTQIQryaprfvgynQQDAQEFLRFLLDGLHNEVNrvTLRPKSNPENLDHLPDDEkgrqmwrkylered 165
Cdd:pfam13423  75 P--------EAAALGL----------QQDIQEANRFILEQLSLPLL--TLKPSIENRRDSSEAESQ-------------- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   166 srIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPiakrgYPE----VTLMDCMRL-FTKEDVLDGDEKPTCCRCRGRK 240
Cdd:pfam13423 121 --LSELFGTGLINSIRCISCNNESVKEESTLTVELP-----YPPsekgQNFSNILKSsIRREKIVTIWCSSCNKYQPVLI 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223   241 RciKKFSiqRFPKILVLHLKRFSES-RIRTSKLTTFVNFPLrDLDLREFASE-------NTNHAVYNLYAVSNHSGTTMG 312
Cdd:pfam13423 194 R--KTFV--SLPPILGICLKRYSEKdNFWAVRLNLFVDIPL-EINMPHFIQDdeqnerpLSGLFKYELQGVVCHIGDSLT 268
                         330       340
                  ....*....|....*....|....*..
gi 27371223   313 -GHYTAYCR---SPGTGEWHTFNDSSV 335
Cdd:pfam13423 269 sGHLVSFIRvapSSENSQWYLFNDFLV 295
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-353 1.98e-08

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


Pssm-ID: 239130  Cd Length: 228  Bit Score: 54.10  E-value: 1.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 112 QQDAQEFLRFLLDGLHNEVNRV--TLRPKSNPENldHLPDDEKGRQMWRKYLERedsrigdlfvgqlKSSLTCTDCGycs 189
Cdd:cd02665  22 QQDVSEFTHLLLDWLEDAFQAAaeAISPGEKSKN--PMVQLFYGTFLTEGVLEG-------------KPFCNCETFG--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 190 tvfdpfwdlSLPIAKRGYPEvtLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKkfsiqrFPKILVLHLKRFSESRIRT 269
Cdd:cd02665  84 ---------QYPLQVNGYGN--LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 270 SKLTTFVNFPlrdldlREFASENtnhavYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQV------ 343
Cdd:cd02665 147 EKIHDKLEFP------QIIQQVP-----YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVerdsfg 215
                       250
                ....*....|..
gi 27371223 344 --RTSDAYLLFY 353
Cdd:cd02665 216 ggRNPSAYCLMY 227
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
245-354 1.19e-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  Cd Length: 268  Bit Score: 45.97  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371223 245 KFSIQRFPKI----LVLHLKRFSESR-------IRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYA-VSNHSGTTMG 312
Cdd:cd02672 149 TTSIRHLPDIlllvLVINLSVTNGEFddinvvlPSGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGyVCEINDSSRG 228
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 27371223 313 GHYTA----YCRSPGTGEWHTFNDSSVTPMSssqvrtSDAYLLFYE 354
Cdd:cd02672 229 QHNVVfvikVNEESTHGRWYLFNDFLVTPVS------ELAYILLYQ 268
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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