NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|40795667|ref|NP_955475|]
View 

ubiquitin carboxyl-terminal hydrolase 4 isoform b [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 1000871)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0046872|GO:0003723

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-876 9.26e-150

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 462.82  E-value: 9.26e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560  48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560 115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 186 --KYMSNTYEQLSKLDNTVQDAGLyqGQVLV----IEPQNEDGTWPRQTLQSNGSGFSASYNCQEPPSSHIQPGLCGLGN 259
Cdd:COG5560 193 vpEIMGLRLGLDSFFRRYRVLASD--GRVLHpltrLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAGTCGLRN 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 260 LGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQF 339
Cdd:COG5560 271 LGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEF 350
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 340 SGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDANGRPDAVV---AKEAWENHRLRNDSVIVDTFHGLFKSTLVCPE 416
Cdd:COG5560 351 SGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPG 430
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 417 CAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPhcRPTQYRVTVPLMGAVSDLCEALSRLSGI-AAENMVVADVYNHR 495
Cdd:COG5560 431 CGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESG--RRQPLKIELDASSTIRGLKKLVDAEYGKlGCFEIKVMCIYYGG 508
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 496 FHKIF--QMDEGLNHIMPRDDIFVYEvcsTSVDGsecVTLPVYfrerksrpssTSSASALYGQPLLLSVPKHKLTLesly 573
Cdd:COG5560 509 NYNMLepADKVLLQDIPQTDFVYLYE---TNDNG---IEVPVV----------HLRIEKGYKSKRLFGDPFLQLNV---- 568
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 574 qavcdRISRYVKQPLPDEFgssplepgacngsrnscegedeeemehqeegkEQLSETEGSGEDEPGNDPSETTQKKIKGQ 653
Cdd:COG5560 569 -----LIKASIYDKLVKEF--------------------------------EELLVLVEMKKTDVDLVSEQVRLLREESS 611
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 654 PCpkrlFTFSLVNSYGTADINSLAADGkLLKLNSRSTLAMDWdSETRRLYYDEQESEAYEKHVSMLQPqkkkktTVALRD 733
Cdd:COG5560 612 PS----SWLKLETEIDTKREEQVEEEG-QMNFNDAVVISCEW-EEKRYLSLFSYDPLWTIREIGAAER------TITLQD 679
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 734 CIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSA 813
Cdd:COG5560 680 CLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDD 759
                       810       820       830       840       850       860
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40795667 814 RPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQRR 876
Cdd:COG5560 760 PRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-876 9.26e-150

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 462.82  E-value: 9.26e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560  48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560 115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 186 --KYMSNTYEQLSKLDNTVQDAGLyqGQVLV----IEPQNEDGTWPRQTLQSNGSGFSASYNCQEPPSSHIQPGLCGLGN 259
Cdd:COG5560 193 vpEIMGLRLGLDSFFRRYRVLASD--GRVLHpltrLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAGTCGLRN 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 260 LGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQF 339
Cdd:COG5560 271 LGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEF 350
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 340 SGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDANGRPDAVV---AKEAWENHRLRNDSVIVDTFHGLFKSTLVCPE 416
Cdd:COG5560 351 SGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPG 430
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 417 CAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPhcRPTQYRVTVPLMGAVSDLCEALSRLSGI-AAENMVVADVYNHR 495
Cdd:COG5560 431 CGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESG--RRQPLKIELDASSTIRGLKKLVDAEYGKlGCFEIKVMCIYYGG 508
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 496 FHKIF--QMDEGLNHIMPRDDIFVYEvcsTSVDGsecVTLPVYfrerksrpssTSSASALYGQPLLLSVPKHKLTLesly 573
Cdd:COG5560 509 NYNMLepADKVLLQDIPQTDFVYLYE---TNDNG---IEVPVV----------HLRIEKGYKSKRLFGDPFLQLNV---- 568
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 574 qavcdRISRYVKQPLPDEFgssplepgacngsrnscegedeeemehqeegkEQLSETEGSGEDEPGNDPSETTQKKIKGQ 653
Cdd:COG5560 569 -----LIKASIYDKLVKEF--------------------------------EELLVLVEMKKTDVDLVSEQVRLLREESS 611
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 654 PCpkrlFTFSLVNSYGTADINSLAADGkLLKLNSRSTLAMDWdSETRRLYYDEQESEAYEKHVSMLQPqkkkktTVALRD 733
Cdd:COG5560 612 PS----SWLKLETEIDTKREEQVEEEG-QMNFNDAVVISCEW-EEKRYLSLFSYDPLWTIREIGAAER------TITLQD 679
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 734 CIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSA 813
Cdd:COG5560 680 CLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDD 759
                       810       820       830       840       850       860
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40795667 814 RPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQRR 876
Cdd:COG5560 760 PRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
729-874 1.69e-60

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: 205.60  E-value: 1.69e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 729 VALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFV 808
Cdd:cd02674  84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40795667 809 CNLSAR-PYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 874
Cdd:cd02674 164 DTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
706-873 2.96e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.04  E-value: 2.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   706 EQESEAYEKHVS---MLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFS 782
Cdd:pfam00443 136 GEVSETFEPFSDlslPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   783 YNRYWRDKLDTVVEFPIRgLNMSEFVCN----LSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLA 858
Cdd:pfam00443 216 YNRSTWEKLNTEVEFPLE-LDLSRYLAEelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEV 294
                         170
                  ....*....|....*.
gi 40795667   859 SED-QIVTKAAYVLFY 873
Cdd:pfam00443 295 DEEtAVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 7.32e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 119.00  E-value: 7.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667     27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 40795667    107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-876 9.26e-150

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 462.82  E-value: 9.26e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560  48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560 115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 186 --KYMSNTYEQLSKLDNTVQDAGLyqGQVLV----IEPQNEDGTWPRQTLQSNGSGFSASYNCQEPPSSHIQPGLCGLGN 259
Cdd:COG5560 193 vpEIMGLRLGLDSFFRRYRVLASD--GRVLHpltrLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAGTCGLRN 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 260 LGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQF 339
Cdd:COG5560 271 LGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEF 350
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 340 SGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDANGRPDAVV---AKEAWENHRLRNDSVIVDTFHGLFKSTLVCPE 416
Cdd:COG5560 351 SGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPG 430
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 417 CAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPhcRPTQYRVTVPLMGAVSDLCEALSRLSGI-AAENMVVADVYNHR 495
Cdd:COG5560 431 CGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESG--RRQPLKIELDASSTIRGLKKLVDAEYGKlGCFEIKVMCIYYGG 508
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 496 FHKIF--QMDEGLNHIMPRDDIFVYEvcsTSVDGsecVTLPVYfrerksrpssTSSASALYGQPLLLSVPKHKLTLesly 573
Cdd:COG5560 509 NYNMLepADKVLLQDIPQTDFVYLYE---TNDNG---IEVPVV----------HLRIEKGYKSKRLFGDPFLQLNV---- 568
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 574 qavcdRISRYVKQPLPDEFgssplepgacngsrnscegedeeemehqeegkEQLSETEGSGEDEPGNDPSETTQKKIKGQ 653
Cdd:COG5560 569 -----LIKASIYDKLVKEF--------------------------------EELLVLVEMKKTDVDLVSEQVRLLREESS 611
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 654 PCpkrlFTFSLVNSYGTADINSLAADGkLLKLNSRSTLAMDWdSETRRLYYDEQESEAYEKHVSMLQPqkkkktTVALRD 733
Cdd:COG5560 612 PS----SWLKLETEIDTKREEQVEEEG-QMNFNDAVVISCEW-EEKRYLSLFSYDPLWTIREIGAAER------TITLQD 679
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 734 CIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSA 813
Cdd:COG5560 680 CLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDD 759
                       810       820       830       840       850       860
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40795667 814 RPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQRR 876
Cdd:COG5560 760 PRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
729-874 1.69e-60

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: 205.60  E-value: 1.69e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 729 VALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFV 808
Cdd:cd02674  84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40795667 809 CNLSAR-PYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 874
Cdd:cd02674 164 DTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
706-873 2.96e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.04  E-value: 2.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   706 EQESEAYEKHVS---MLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFS 782
Cdd:pfam00443 136 GEVSETFEPFSDlslPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   783 YNRYWRDKLDTVVEFPIRgLNMSEFVCN----LSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLA 858
Cdd:pfam00443 216 YNRSTWEKLNTEVEFPLE-LDLSRYLAEelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEV 294
                         170
                  ....*....|....*.
gi 40795667   859 SED-QIVTKAAYVLFY 873
Cdd:pfam00443 295 DEEtAVLSSSAYILFY 310
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
255-438 3.51e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 185.34  E-value: 3.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   255 CGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPlgmKGEIAEAYAELIKQMWSG-RDAHVAPRMFKTQVG 333
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   334 RFAPQFSGYQQQDSQELLAFLLDGLHEDLNRvkkkpylelkdangrpdavvakeaweNHRLRNDSVIVDTFHGLFKSTLV 413
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180
                  ....*....|....*....|....*
gi 40795667   414 CPECAKVSVTFDPFCYLTLPLPLKK 438
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDS 156
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
719-874 1.94e-40

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: 149.94  E-value: 1.94e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 719 LQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCpNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWR-DKLDTVVEF 797
Cdd:cd02257  89 LPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSF 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 798 PIRgLNMSEFV------CNLSARPYVYDLIAVSNHYG-AMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIV-----T 865
Cdd:cd02257 168 PLE-LDLSPYLsegekdSDSDNGSYKYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgslS 246

                ....*....
gi 40795667 866 KAAYVLFYQ 874
Cdd:cd02257 247 SSAYILFYE 255
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
139-226 1.63e-36

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 132.29  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 40795667   219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 7.32e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 119.00  E-value: 7.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667     27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 40795667    107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
726-873 3.91e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 125.18  E-value: 3.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 726 KTTVALRDCIELFTTMETLGEhDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRD-KLDTVVEFPIRgLNM 804
Cdd:cd02660 173 SGTPTLSDCLDRFTRPEKLGD-FAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNM 250
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40795667 805 SEFVC---------NLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKlNGKWYYFDDSNVSLASEDQIVTKAAYVLFY 873
Cdd:cd02660 251 TPYTSssigdtqdsNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
731-873 5.07e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 123.93  E-value: 5.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 731 LRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYwrDKLDTVVEFPIRgLNMSEFVCN 810
Cdd:cd02661 164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFPET-LDLSPYMSQ 240
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40795667 811 LSARPYVYDLIAVSNHYGA-MGVGHYTAYAKNkLNGKWYYFDDSNVSLASEDQIVTKAAYVLFY 873
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
31-123 1.70e-26

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 103.60  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667    31 GAQWYLIDSRWFKQWKKYVGfdswdmynvgEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGc 110
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG- 69
                          90
                  ....*....|...
gi 40795667   111 veGQQPIVRKVVE 123
Cdd:pfam06337  70 --GGPEIKRNVVN 80
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
255-439 6.78e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 103.12  E-value: 6.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 255 CGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKgeIAEAYAELIkqMWSGRDAhVAPRMFKTQVGR 334
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC--ALEAHVERA--LASSGPG-SAPRIFSSNLKQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 335 FAPQFSGYQQQDSQELLAFLLDGLHedlnrvkkKPYLELKdangrpdavvAKEAWENHRLRNDSVIVDTFHGLFKSTLVC 414
Cdd:cd02661  77 ISKHFRIGRQEDAHEFLRYLLDAMQ--------KACLDRF----------KKLKAVDPSSQETTLVQQIFGGYLRSQVKC 138
                       170       180
                ....*....|....*....|....*
gi 40795667 415 PECAKVSVTFDPFcyLTLPLPLKKD 439
Cdd:cd02661 139 LNCKHVSNTYDPF--LDLSLDIKGA 161
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
728-878 6.10e-23

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: 101.18  E-value: 6.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 728 TVALRDCIEL------FTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYN--RYWRDKLDTVVEFPI 799
Cdd:cd02659 144 QVAVKGKKNLeesldaYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPL 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 800 RgLNMSEFV-----------CNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIV---- 864
Cdd:cd02659 224 E-LDMEPYTekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEeecf 302
                       170       180       190
                ....*....|....*....|....*....|..
gi 40795667 865 ------------------TKAAYVLFYQRRDD 878
Cdd:cd02659 303 ggeetqktydsgprafkrTTNAYMLFYERKSP 334
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-444 5.03e-22

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: 95.82  E-value: 5.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNtapltdyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdahvaprmfktqvgrf 335
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 336 apqfsgyQQQDSQELLAFLLDGLHedlnrvkkkpylelkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTLVCP 415
Cdd:cd02674  21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                       170       180
                ....*....|....*....|....*....
gi 40795667 416 ECAKVSVTFDPFCYLTLPLPLKKDRVMEV 444
Cdd:cd02674  56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKV 84
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-438 1.15e-21

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 97.06  E-value: 1.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKG-EIAEAYAELikqMWSGRDAHVAPRMFKTQVGR 334
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLScAMDEIFQEF---YYSGDRSPYGPINLLYLSWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 335 FAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKkPYLELKDANgrpdavvakeawenhrlrndsVIVD-TFHGLFKSTLV 413
Cdd:cd02660  79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN-EANDESHCN---------------------CIIHqTFSGSLQSSVT 136
                       170       180
                ....*....|....*....|....*
gi 40795667 414 CPECAKVSVTFDPFCYLTLPLPLKK 438
Cdd:cd02660 137 CQRCGGVSTTVDPFLDLSLDIPNKS 161
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
709-874 2.62e-21

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 95.15  E-value: 2.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 709 SEAYEKHVSMLQPQKKK-KTTVALRDCIELFTTMETLGEHDPWYCPNCKKhqqATKKFDLWSLPKILVVHLKRFSYNRYW 787
Cdd:cd02667  90 SLVYEPFLDLSLPRSDEiKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSA 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 788 RD-KLDTVVEFPIRgLNMSEFV---CNLSA--RPYVYDLIAVSNHYGAMGVGHYTAYAK--------------------- 840
Cdd:cd02667 167 NLrKVSRHVSFPEI-LDLAPFCdpkCNSSEdkSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadea 245
                       170       180       190
                ....*....|....*....|....*....|....
gi 40795667 841 NKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 874
Cdd:cd02667 246 GPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
733-874 3.92e-21

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 95.07  E-value: 3.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 733 DCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYN-RYWR-DKLDTVVEFP--IRGLNMSEFV 808
Cdd:cd02663 151 SCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyIKLFYRVVFPleLRLFNTTDDA 230
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40795667 809 CNLSArpyVYDLIAVSNHYGAMGV-GHYTAYAKNKlnGKWYYFDDSNVSLASEDQIV--------TKAAYVLFYQ 874
Cdd:cd02663 231 ENPDR---LYELVAVVVHIGGGPNhGHYVSIVKSH--GGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
731-873 1.39e-20

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: 94.02  E-value: 1.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 731 LRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY--WRDKLDTVVEFPiRGLNMSEFV 808
Cdd:cd02668 158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKtgAKKKLNASISFP-EILDMGEYL 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 809 CNLSARPYVYDLIAVSNHYG--AMGvGHYTAYAKNKLNGKWYYFDDSNVS--------------LASEDQ-------IVT 865
Cdd:cd02668 237 AESDEGSYVYELSGVLIHQGvsAYS-GHYIAHIKDEQTGEWYKFNDEDVEempgkplklgnsedPAKPRKseikkgtHSS 315

                ....*...
gi 40795667 866 KAAYVLFY 873
Cdd:cd02668 316 RTAYMLVY 323
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-435 1.50e-20

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: 92.83  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNTAPLTDYFLKDeyeaeinrdnplgmkgeiaeayaelikqmwsgrdahvaPRMFKTQVGRF 335
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 336 APQFSGYQQQDSQELLAFLLDGLhedlnrvkkkpylelkdangrpdavvakeawenhRLRNDSVivdtFHGLFKSTLVCP 415
Cdd:cd02667  43 APQFKGYQQQDSHELLRYLLDGL----------------------------------RTFIDSI----FGGELTSTIMCE 84
                       170       180
                ....*....|....*....|
gi 40795667 416 ECAKVSVTFDPFcyLTLPLP 435
Cdd:cd02667  85 SCGTVSLVYEPF--LDLSLP 102
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
256-439 5.53e-20

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: 90.62  E-value: 5.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNtapltdyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdahvaprmfktqvgrf 335
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 336 apqfsgyQQQDSQELLAFLLDGLHEDLNRVKKKpylelkdangrpdavvakeawENHRLRNDSVIVDTFHGLFKSTLVCP 415
Cdd:cd02257  21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                       170       180
                ....*....|....*....|....
gi 40795667 416 ECAKVSVTFDPFCYLTLPLPLKKD 439
Cdd:cd02257  73 ECGHESVSTEPELFLSLPLPVKGL 96
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
684-874 2.77e-17

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 83.91  E-value: 2.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 684 KLNSRSTLAMDWDSETRRLYYDEQESEAYEKhvsmlqpqkkkkttVALRDCIELFTTMETLGEhdpwYCPNCKKHQQATK 763
Cdd:cd02658 147 KYTSELSEILSLPVPKDEATEKEEGELVYEP--------------VPLEDCLKAYFAPETIED----FCSTCKEKTTATK 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 764 KFDLWSLPKILVVHLKRFSYNRYWRD-KLDTVVEFPIRGLnmsefvcnlsarPYVYDLIAVSNHYGA-MGVGHYTAYAKN 841
Cdd:cd02658 209 TTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVPEELG------------PGKYELIAFISHKGTsVHSGHYVAHIKK 276
                       170       180       190
                ....*....|....*....|....*....|....*
gi 40795667 842 KLN--GKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 874
Cdd:cd02658 277 EIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
718-875 5.69e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 82.16  E-value: 5.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 718 MLQPQKKKKTTVALRDCIELFTTMET---LGEHDPWYCPNCKKHQQATKKfdlwsLPKILVVHLKRFSYNRYWRdKLDTV 794
Cdd:COG5533 129 DQTWVNNLKTLQEFIDNMEELVDDETgvkAKENEELEVQAKQEYEVSFVK-----LPKILTIQLKRFANLGGNQ-KIDTE 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 795 VEFPIrglnmsefvcNLSARP---------YVYDLIAVSNHYGAMGVGHYTAYAKNklNGKWYYFDDSNVSLASEDQIVT 865
Cdd:COG5533 203 VDEKF----------ELPVKHdqilnivkeTYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVTPVSEEEAIN 270
                       170
                ....*....|...
gi 40795667 866 ---KAAYVLFYQR 875
Cdd:COG5533 271 ekaKNAYLYFYER 283
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
762-873 1.21e-16

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 81.61  E-value: 1.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 762 TKKFDlwSLPKILVVHLKRFsynrYWRDKLDT------VVEFPIRgLNMSEFvCNLSArpyVYDLIAVSNHYGAMG-VGH 834
Cdd:cd02657 190 TSRIS--RLPKYLTVQFVRF----FWKRDIQKkakilrKVKFPFE-LDLYEL-CTPSG---YYELVAVITHQGRSAdSGH 258
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 40795667 835 YTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKA-------AYVLFY 873
Cdd:cd02657 259 YVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
707-873 7.62e-16

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 79.94  E-value: 7.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 707 QESEAYEKHVSMLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY 786
Cdd:cd02671 158 QESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGS 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 787 WRD------KLDTVVEFPirgLNMSEFVCNLSARPYVYDLIAVSNHYGA-MGVGHYTAYAknklngKWYYFDDSNVSLAS 859
Cdd:cd02671 238 EFDcygglsKVNTPLLTP---LKLSLEEWSTKPKNDVYRLFAVVMHSGAtISSGHYTAYV------RWLLFDDSEVKVTE 308
                       170       180
                ....*....|....*....|...
gi 40795667 860 EDQIV---------TKAAYVLFY 873
Cdd:cd02671 309 EKDFLealspntssTSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
721-874 3.41e-14

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 73.17  E-value: 3.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 721 PQKKKKTTVALRDCIELFTTMETLgehDPWYCPNCkkhQQATKKfdlwsLPKILVVHLKRFSYNRYwrdkldtvVEFPIR 800
Cdd:cd02662  88 PNQSSGSGTTLEHCLDDFLSTEII---DDYKCDRC---QTVIVR-----LPQILCIHLSRSVFDGR--------GTSTKN 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 801 GLNMSefvCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGK--------------------WYYFDDSNVSLASE 860
Cdd:cd02662 149 SCKVS---FPERLPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKEVSE 225
                       170
                ....*....|....*
gi 40795667 861 DQIV-TKAAYVLFYQ 874
Cdd:cd02662 226 SEVLeQKSAYMLFYE 240
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
763-874 6.80e-14

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 75.05  E-value: 6.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 763 KKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVC---NLSARPYVYDLIAVSNHYGAMGV-GHYTAY 838
Cdd:cd02669 325 KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHfdkPSLNLSTKYNLVANIVHEGTPQEdGTWRVQ 404
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 40795667 839 AKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 874
Cdd:cd02669 405 LRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-436 1.27e-13

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 72.74  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPL------------GMKGEiAEAYAELIKQMWSGRDAHV 323
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladGLLSG-RYSKPASLKSENDPYQVGI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 324 APRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDglhedlnrvkkkpylelkdangrpdaVVAKEAWENHrlrnDSVIVDT 403
Cdd:cd02658  80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLID--------------------------KLDRESFKNL----GLNPNDL 129
                       170       180       190
                ....*....|....*....|....*....|...
gi 40795667 404 FHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPL 436
Cdd:cd02658 130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
252-437 3.70e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 72.74  E-value: 3.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 252 PGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFL-KDEYEAEINRdnplgmKGEIAEAYAELIKQMWSGRD--AHVAPRMF 328
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDR------KSELVKRLSELIRKIWNPRNfkGHVSPHEL 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 329 KTQVG-RFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKpylelkdangrpdavvakeawenhrlrNDSVIVDTFHGL 407
Cdd:cd02669 191 LQAVSkVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSIIHDCFQGK 243
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 40795667 408 FK---------------STLVCPECAKVSVTFDPFCYLTLPLPLK 437
Cdd:cd02669 244 VQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLLLTLDLPPP 288
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
731-863 1.16e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 72.21  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667  731 LRDCIELFTTMETL-GEHdpwyCPNCKKH--QQATKKFDLWSLPKILVVHLKRFSYNrYWRD---KLDTVVEFPIRgLNM 804
Cdd:COG5077  340 LQESFRRYIQVETLdGDN----RYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDL 413
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40795667  805 SEFVCNLSAR----PYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQI 863
Cdd:COG5077  414 LPFLDRDADKsensDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
731-874 4.39e-12

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 68.29  E-value: 4.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 731 LRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNR--YWRDKL------DTVVEFPIR-G 801
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPVRvE 215
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 802 LNMSEFVCN-----------LSARPYVYDLIAVSNHYG-AMGVGHYTAYAKN--------------------KLNGKWYY 849
Cdd:cd02664 216 SKSSESPLEkkeeesgddgeLVTRQVHYRLYAVVVHSGySSESGHYFTYARDqtdadstgqecpepkdaeenDESKNWYL 295
                       170       180       190
                ....*....|....*....|....*....|..
gi 40795667 850 FDDSNVSLAS--EDQIVTK-----AAYVLFYQ 874
Cdd:cd02664 296 FNDSRVTFSSfeSVQNVTSrfpkdTPYILFYE 327
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-434 8.69e-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 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: 66.97  E-value: 8.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLsNTAP-----LTDYFLKDEYEAEINRDnplgmkgeIAEAYAELIKQMWSGRDAhVAPRMFKT 330
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDN--------LTNALRDLFDTMDKKQEP-VPPIEFLQ 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 331 QVGRFAPQFS------GYQQQDSQELLAFLLDGLHEDLNRVKKKPylelkdangrpdavvakeawenhrlrndSVIVDTF 404
Cdd:cd02657  71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG----------------------------SFIDQLF 122
                       170       180       190
                ....*....|....*....|....*....|.
gi 40795667 405 HGLFKSTLVCPEC-AKVSVTFDPFCYLTLPL 434
Cdd:cd02657 123 GIELETKMKCTESpDEEEVSTESEYKLQCHI 153
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
256-362 2.78e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 62.13  E-value: 2.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLS-NTAPLTDYFLKDEYE-----AEINRDNPLgMKGEIAEAyaeLIKQMWSGRdahvaprmfK 329
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPD-LNQEEALK---LFTALWSSK---------E 67
                        90       100       110
                ....*....|....*....|....*....|...
gi 40795667 330 TQVGRFAPQfsgYQQQDSQELLAFLLDGLHEDL 362
Cdd:COG5533  68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDL 97
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-448 7.50e-10

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 61.35  E-value: 7.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLsntapltdyFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMW---SGRDAHVAPRMFKTQV 332
Cdd:cd02664   1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 333 grFAPQFSGYQQQDSQELLAFLLDGLHedlnrvkkkpylelkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTL 412
Cdd:cd02664  72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 40795667 413 VCPECAKVSVTFDPFCYLTLPLPLKKDrVMEVFLVP 448
Cdd:cd02664 112 RCLNCNSTSARTERFRDLDLSFPSVQD-LLNYFLSP 146
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-435 9.65e-09

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 57.70  E-value: 9.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNTAPLTDyfLKDEYEAEINRDNPLGMkgeiaeayaelikqmwsgrdahVAPRMFKTQVGRF 335
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYFENLLTC--LKDLFESISEQKKRTGV----------------------ISPKKFITRLKRE 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 336 APQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKpylelkdangrpDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCP 415
Cdd:cd02663  57 NELFDNYMHQDAHEFLNFLLNEIAEILDAERKA------------EKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCL 124
                       170       180
                ....*....|....*....|
gi 40795667 416 ECAKVSVTFDPFCYLTLPLP 435
Cdd:cd02663 125 TCETVSSRDETFLDLSIDVE 144
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
752-873 3.01e-07

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: 52.53  E-value: 3.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 752 CPNCKkHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTvvefpirglNMSEFVCnLSARPYVYDLIAVSNHYG-AM 830
Cdd:cd02673 129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYLKK---------NEEIMKK-YCGTDAKYSLVAVICHLGeSP 197
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40795667 831 GVGHYTAYAKNKLNG-KWYYFDDSNVSLASEDQIVTKA---AYVLFY 873
Cdd:cd02673 198 YDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVSTNArssGYLIFY 244
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
252-360 4.20e-07

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: 52.97  E-value: 4.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 252 PGLCGLGNLGNTCFMNSALQCLsntapltdYFLKDeYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQ 331
Cdd:cd02671  22 LPFVGLNNLGNTCYLNSVLQVL--------YFCPG-FKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAPRRLLNA 92
                        90       100
                ....*....|....*....|....*....
gi 40795667 332 VGRFAPQFSGYQQQDSQELLAFLLDGLHE 360
Cdd:cd02671  93 LREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
253-437 2.98e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 47.25  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 253 GLCGLGNLGNTCFMNSALQCLSNTApltdYFLKDEYEAEINRDNPlGMKGEIaeayAELIKQMWSgrdAHVAPRMFKTQV 332
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD-DNKSVP----LALQRLFLF---LQLSESPVKTTE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 333 GRFAPQFSG------YQQQDSQELLAFLLDGLHEDLnrvkkkPYLELKDAngrpdavvakeawenhrlrndsvIVDTFHG 406
Cdd:cd02659  69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKLEEKL------KGTGQEGL-----------------------IKNLFGG 119
                       170       180       190
                ....*....|....*....|....*....|.
gi 40795667 407 LFKSTLVCPECAKVSVTFDPFcyLTLPLPLK 437
Cdd:cd02659 120 KLVNYIICKECPHESEREEYF--LDLQVAVK 148
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
770-873 5.09e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 45.63  E-value: 5.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 770 LPKILVVHLKRFSYNRYWRDKLDTVVEFP--IRGLNmsefvcnlsarpyvYDLIAVSNHYGAMGVGHYTAYAKNKLNGKW 847
Cdd:cd02665 128 LPPVLTFELSRFEFNQGRPEKIHDKLEFPqiIQQVP--------------YELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
                        90       100       110
                ....*....|....*....|....*....|....
gi 40795667 848 YYFDDSNVSLASEDQIVTKA--------AYVLFY 873
Cdd:cd02665 194 EKYNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-437 1.25e-04

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 45.10  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQCLSNTAPLTDYFLK-----DEYEAEINRDNPLGMKGeIAEAYAELIKQMWSGRDAHVAPRMFKT 330
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 331 QVGrfapqFSGYQQQDSQELLAFLLDGLHEDLNRVKKkpylelkdangrPDAVvakeawenhrlrndSVIVDTFHGLFKS 410
Cdd:cd02668  80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKN------------PDLK--------------NIVQDLFRGEYSY 128
                       170       180
                ....*....|....*....|....*..
gi 40795667 411 TLVCPECAKVSVTFDPFcyLTLPLPLK 437
Cdd:cd02668 129 VTQCSKCGRESSLPSKF--YELELQLK 153
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-438 1.53e-04

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 44.28  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 256 GLGNLGNTCFMNSALQclsntapltdyflkdeyeaeinrdnplgmkgeiaeAYAELikqmwsgrdahvaprmfktqvgrf 335
Cdd:cd02662   1 GLVNLGNTCFMNSVLQ-----------------------------------ALASL------------------------ 21
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 336 aPQFSGY-----QQQDSQELLAFLLDGLHEDLnrvkKKPylelkdangrpdavvakeawenhrlrndsvivdtFHGLFKS 410
Cdd:cd02662  22 -PSLIEYleeflEQQDAHELFQVLLETLEQLL----KFP----------------------------------FDGLLAS 62
                       170       180
                ....*....|....*....|....*....
gi 40795667 411 TLVCPECAKVS-VTFDPFCYLTLPLPLKK 438
Cdd:cd02662  63 RIVCLQCGESSkVRYESFTMLSLPVPNQS 91
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
716-855 2.94e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 43.80  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667   716 VSMLQPQKKKKTTVA--LRDCIELFTTmetlgeHDPWyCPNCKKHQQATKKFDLWSLPKILVVHLKRfsYNRYWRDKLDT 793
Cdd:pfam13423 165 KPSSNNKKPPNQTFSsiLKSSLERETT------TKAW-CEKCKRYQPLESRRTVRNLPPVLSLNAAL--TNEEWRQLWKT 235
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40795667   794 VVEFPIR-GLNMSEFVCNlSARPYVYDLIAV---------SNHYGAM-GVGHytAYAKNKLNGKWYYFDDSNV 855
Cdd:pfam13423 236 PGWLPPEiGLTLSDDLQG-DNEIVKYELRGVvvhigdsgtSGHLVSFvKVAD--SELEDPTESQWYLFNDFLV 305
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
248-358 6.34e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 43.71  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667  248 SHIQPGLCGLGNLGNTCFMNSALQCLSNTApltdYFLKDEYeaEINRDNPLGmKGEIAEAYAELIKQMWSGRDAhVAPRM 327
Cdd:COG5077  187 SKKETGYVGLRNQGATCYMNSLLQSLFFIA----KFRKDVY--GIPTDHPRG-RDSVALALQRLFYNLQTGEEP-VDTTE 258
                         90       100       110
                 ....*....|....*....|....*....|.
gi 40795667  328 FKTQVGrfAPQFSGYQQQDSQELLAFLLDGL 358
Cdd:COG5077  259 LTRSFG--WDSDDSFMQHDIQEFNRVLQDNL 287
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
717-874 2.15e-03

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: 40.96  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 717 SMLQPQKKKKTTVALRDCIELFTTMEtlgEHDPWYCPNCKKHQQATKKFDLWSLPKI----LVVHLKRFSYNRywrdKLD 792
Cdd:cd02672 105 SLPLGSTKTSKESTFLQLLKRSLDLE---KVTKAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEF----DDI 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40795667 793 TVVEFpiRGLNMSEFV-----CNLSARP-------YVYDLIAV-----SNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNV 855
Cdd:cd02672 178 NVVLP--SGKVMQNKVspkaiDHDKLVKnrgqesiYKYELVGYvceinDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLV 255
                       170
                ....*....|....*....
gi 40795667 856 SLASEDqivtkaAYVLFYQ 874
Cdd:cd02672 256 TPVSEL------AYILLYQ 268
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
457-520 2.19e-03

Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.


Pssm-ID: 464201  Cd Length: 204  Bit Score: 40.54  E-value: 2.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40795667   457 QYRVTVPLMGAVSDLCEALSRLSGIAAE---NMVVADVYNHRFHKIFQMDEGLNHIMPRDDIFVYEV 520
Cdd:pfam14533  34 ELELLVPKNGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKELSEDEPIDSLNDYLTLYAEEI 100
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
814-864 8.02e-03

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: 39.40  E-value: 8.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 40795667 814 RPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIV 864
Cdd:cd02666 277 KSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVF 327
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-297 9.54e-03

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: 39.40  E-value: 9.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 40795667 256 GLGNLGNTCFMNSALQCLSNTAPLTDYFLK-DEYEAEINRDNP 297
Cdd:cd02666   3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfDESKAELASDYP 45
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH