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Conserved domains on  [gi|1958802784|ref|XP_038939657|]
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ubiquitin carboxyl-terminal hydrolase 40 isoform X6 [Rattus norvegicus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10119155)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 40-381 5.92e-131

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: 397.40  E-value: 5.92e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  40 LSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEElgsledkDKPEAKVRIIPLQLQRLFAQLLLVDQEAASTTDLTD 119
Cdd:cd02659     2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTE-------DDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 120 SFGWTSDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGLE 199
Cdd:cd02659    75 SFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 200 DALWNmYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFCEQ 279
Cdd:cd02659   155 ESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 280 SDM---------DDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCQeeisDSAVNLKAPQNEEEtddplvvlka 350
Cdd:cd02659   234 GLAkkegdsekkDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDD-GKWYKF----NDDVVTPFDPNDAE---------- 298

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958802784 351 illqEEANQIPVDQLGQKLLIKTGISWNKKY 381
Cdd:cd02659   299 ----EECFGGEETQKTYDSGPRAFKRTTNAY 325
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 40-381 5.92e-131

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: 397.40  E-value: 5.92e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  40 LSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEElgsledkDKPEAKVRIIPLQLQRLFAQLLLVDQEAASTTDLTD 119
Cdd:cd02659     2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTE-------DDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 120 SFGWTSDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGLE 199
Cdd:cd02659    75 SFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 200 DALWNmYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFCEQ 279
Cdd:cd02659   155 ESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 280 SDM---------DDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCQeeisDSAVNLKAPQNEEEtddplvvlka 350
Cdd:cd02659   234 GLAkkegdsekkDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDD-GKWYKF----NDDVVTPFDPNDAE---------- 298

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958802784 351 illqEEANQIPVDQLGQKLLIKTGISWNKKY 381
Cdd:cd02659   299 ----EECFGGEETQKTYDSGPRAFKRTTNAY 325
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
42-346 6.68e-55

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 193.04  E-value: 6.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSlgpeelGSLEDKDKPEAKVRIIPLQLQRLFAQLLLVDQEAA-STTDLTDS 120
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 121 FGWTSDE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:pfam00443  76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 196 SGLE--DALWNMYVE---EEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTscYTFPLR 270
Cdd:pfam00443 156 SAELktASLQICFLQfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTE--VEFPLE 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958802784 271 INLKPFCEQSDMDDME--YMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCqeeISDSAVNLKAPQNEEETDDPLV 346
Cdd:pfam00443 234 LDLSRYLAEELKPKTNnlQDYRLVAVVVHSGSLSSGHYIAYIKAYEN-NRWYK---FDDEKVTEVDEETAVLSSSAYI 307
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 35-319 4.17e-53

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 201.64  E-value: 4.17e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784   35 REFTKLSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLgpeelgsleDKDKPEAKvRIIPLQLQRLFAQLLlVDQEAAST 114
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQ-TGEEPVDT 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  115 TDLTDSFGWTSDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKN 194
Cdd:COG5077    257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  195 VSGLEDALWNmYVEEEIFDYDNLYHCGTCDrLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLK 274
Cdd:COG5077    337 MKNLQESFRR-YIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958802784  275 PFCEQsDMDDME---YMYDLFSVIIHKGGCYGGHYHVYIK-DVDhlGNW 319
Cdd:COG5077    415 PFLDR-DADKSEnsdAVYVLYGVLVHSGDLHEGHYYALLKpEKD--GRW 460
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 40-381 5.92e-131

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: 397.40  E-value: 5.92e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  40 LSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEElgsledkDKPEAKVRIIPLQLQRLFAQLLLVDQEAASTTDLTD 119
Cdd:cd02659     2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTE-------DDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 120 SFGWTSDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGLE 199
Cdd:cd02659    75 SFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 200 DALWNmYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFCEQ 279
Cdd:cd02659   155 ESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 280 SDM---------DDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCQeeisDSAVNLKAPQNEEEtddplvvlka 350
Cdd:cd02659   234 GLAkkegdsekkDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDD-GKWYKF----NDDVVTPFDPNDAE---------- 298

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958802784 351 illqEEANQIPVDQLGQKLLIKTGISWNKKY 381
Cdd:cd02659   299 ----EECFGGEETQKTYDSGPRAFKRTTNAY 325
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
42-346 6.68e-55

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 193.04  E-value: 6.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSlgpeelGSLEDKDKPEAKVRIIPLQLQRLFAQLLLVDQEAA-STTDLTDS 120
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 121 FGWTSDE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:pfam00443  76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 196 SGLE--DALWNMYVE---EEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTscYTFPLR 270
Cdd:pfam00443 156 SAELktASLQICFLQfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTE--VEFPLE 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958802784 271 INLKPFCEQSDMDDME--YMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCqeeISDSAVNLKAPQNEEETDDPLV 346
Cdd:pfam00443 234 LDLSRYLAEELKPKTNnlQDYRLVAVVVHSGSLSSGHYIAYIKAYEN-NRWYK---FDDEKVTEVDEETAVLSSSAYI 307
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 35-319 4.17e-53

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 201.64  E-value: 4.17e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784   35 REFTKLSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLgpeelgsleDKDKPEAKvRIIPLQLQRLFAQLLlVDQEAAST 114
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQ-TGEEPVDT 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  115 TDLTDSFGWTSDEEMRQHDVQELNRILFSALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKN 194
Cdd:COG5077    257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  195 VSGLEDALWNmYVEEEIFDYDNLYHCGTCDrLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLK 274
Cdd:COG5077    337 MKNLQESFRR-YIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958802784  275 PFCEQsDMDDME---YMYDLFSVIIHKGGCYGGHYHVYIK-DVDhlGNW 319
Cdd:COG5077    415 PFLDR-DADKSEnsdAVYVLYGVLVHSGDLHEGHYYALLKpEKD--GRW 460
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 42-330 2.65e-47

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: 169.59  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHftpefrealfslgpeelgsledkdkpeakvriiplqlqrlfaqlllvdqeaasttdltdsf 121
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 122 gwtsdeeMRQHDVQELNRILFSALETSLVG--------TSGHDLIHRLYHGTIVNQIVCKECK--NVSERQEDFLDLTVA 191
Cdd:cd02257    20 -------SEQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGheSVSTEPELFLSLPLP 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 192 VKNVSG--LEDALwNMYVEEEIFDYDNLYHCGtCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvKCERYKDTSCYTFPL 269
Cdd:cd02257    93 VKGLPQvsLEDCL-EKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPL 169

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958802784 270 RINLKPFCEQSDMDD----MEYMYDLFSVIIHKGG-CYGGHYHVYIKDVDHlGNWQCqeeISDSAV 330
Cdd:cd02257   170 ELDLSPYLSEGEKDSdsdnGSYKYELVAVVVHSGTsADSGHYVAYVKDPSD-GKWYK---FNDDKV 231
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-324 7.64e-47

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 170.68  E-value: 7.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLED--KDKPEAKVRIIpLQLQRLFAQLLLVDQEAASTTDLTD 119
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmpPDKPHEPQTII-DQLQLIFAQLQFGNRSVVDPSGFVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 120 SFGWTSDEemrQHDVQELNRILFSALETSLVGTSGHDL---IHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVS 196
Cdd:cd02668    80 ALGLDTGQ---QQDAQEFSKLFLSLLEAKLSKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 197 GLEDALwNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPF 276
Cdd:cd02668   157 TLEECI-DEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958802784 277 CEQSDMDDmeYMYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW-QCQEE 324
Cdd:cd02668   236 LAESDEGS--YVYELSGVLIHQGvSAYSGHYIAHIKD-EQTGEWyKFNDE 282
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 41-330 4.88e-38

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: 144.34  E-value: 4.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  41 SGIRNQGGTCYLSSLLQTLHFTPEFreALFSLGPEElgSLEDKDKPEAKVRIIPLQLQRLfaqlLLVDQEAASTTDLTDS 120
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPL--ANYLLSREH--SKDCCNEGFCMMCALEAHVERA----LASSGPGSAPRIFSSN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 121 FGWTSDEEM--RQHDVQELNRILFSALETS----LVGTSGHD-------LIHRLYHGTIVNQIVCKECKNVSERQEDFLD 187
Cdd:cd02661    74 LKQISKHFRigRQEDAHEFLRYLLDAMQKAcldrFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 188 LTVAVKNVSGLEDALwNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvkceRYKDTSCYTF 267
Cdd:cd02661   154 LSLDIKGADSLEDAL-EQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR----GGKINKQISF 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958802784 268 PLRINLKPFceQSDMDDMEYMYDLFSVIIHKGG-CYGGHYHVYIKDVDhlGNWQCqeeISDSAV 330
Cdd:cd02661   229 PETLDLSPY--MSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSN--GKWYN---MDDSKV 285
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-306 1.14e-28

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 117.03  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFtpefrEALFSLGPEELGSLEDKDKpeaKVRIIPLQLqrlFAQLLLVDQEAASTTDLTDS- 120
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYF-----ENLLTCLKDLFESISEQKK---RTGVISPKK---FITRLKRENELFDNYMHQDAh 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 121 --FGW---TSDEEMRQHDVQELNRILFSALETSlvgTSGHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:cd02663    70 efLNFllnEIAEILDAERKAEKANRKLNNNNNA---EPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 196 SGLEDALWNMYvEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDfVKCERYKDTScYTFPLRINLKP 275
Cdd:cd02663   147 TSITSCLRQFS-ATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD-EQLNRYIKLF-YRVVFPLELRL 223

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958802784 276 FCEQSDMDDMEYMYDLFSVIIHKG-GCYGGHY 306
Cdd:cd02663   224 FNTTDDAENPDRLYELVAVVVHIGgGPNHGHY 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-319 2.29e-28

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 117.09  E-value: 2.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSlgpeELGSLEDKDKPEAKVriIPLQLQRLFAQLllvdqeaaSTTDLTDSF 121
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLS----DRHSCTCLSCSPNSC--LSCAMDEIFQEF--------YYSGDRSPY 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 122 G--------WTSDEEM---RQHDVQELNRILFSALETSLVGTSGHD--------LIHRLYHGTIVNQIVCKECKNVSERQ 182
Cdd:cd02660    68 GpinllylsWKHSRNLagySQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcncIIHQTFSGSLQSSVTCQRCGGVSTTV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 183 EDFLDLTVAVKNVSG---------------LEDALWNMYVEEEIFDYDnlYHCGTCDRLVKAAKSAKLRKLPPFLTISLL 247
Cdd:cd02660   148 DPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKLGDFA--YKCSGCGSTQEATKQLSIKKLPPVLCFQLK 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958802784 248 RFNFDFVKCERyKDTSCYTFPLRINLKPFCEQSDMDDME-------YMYDLFSVIIHKGGCYGGHYHVYIKdvDHLGNW 319
Cdd:cd02660   226 RFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdYTYDLFAVVVHKGTLDTGHYTAYCR--QGDGQW 301
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-314 3.28e-28

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 116.44  E-value: 3.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLEdkdkpeakvrIIPLQLQRLFAQLLLVDQEAASTTD--LTD 119
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ----------SVMKKLQLLQAHLMHTQRRAEAPPDyfLEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 120 SF-GWTSDEemRQHDVQELNRILFSALetslvgtsgHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVsgl 198
Cdd:cd02664    71 SRpPWFTPG--SQQDCSEYLRYLLDRL---------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSV--- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 199 EDALwNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTSCYTFPLRINLKPFCE 278
Cdd:cd02664   137 QDLL-NYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVE 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958802784 279 QSDMDDMEYM-----------------YDLFSVIIHKG-GCYGGHYHVYIKDVD 314
Cdd:cd02664   216 SKSSESPLEKkeeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTYARDQT 269
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-312 3.53e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 112.09  E-value: 3.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREaLFSLGPEELGSLEDKDKPEAKvriiplqlqrlfaqlllvdqeaasttdltdsf 121
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSETPKELFSQVCRKAPQFK-------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 122 gwtsdeEMRQHDVQELNRILFSALETslvgtsghdLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAV----KNVSG 197
Cdd:cd02667    48 ------GYQQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRsdeiKSECS 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 198 LEDALWNmYVEEEIFDYDNLYHCGTCDrlvKAAKSAKLRKLPPFLTISLLRF----NFDFVKCERYKDtscytFPLRINL 273
Cdd:cd02667   113 IESCLKQ-FTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFqqprSANLRKVSRHVS-----FPEILDL 183

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958802784 274 KPFC---EQSDMDDMEYMYDLFSVIIHKGGCYGGHYHVYIKD 312
Cdd:cd02667   184 APFCdpkCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 130-312 3.16e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 108.14  E-value: 3.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 130 RQHDVQELNRILFSALetslvgtsgHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG------LEDALw 203
Cdd:cd02674    21 DQQDAQEFLLFLLDGL---------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGdapkvtLEDCL- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 204 NMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFvkCERYKDTSCYTFPLRI-NLKPFCEQSDm 282
Cdd:cd02674    91 RLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPLNDlDLTPYVDTRS- 167

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958802784 283 DDMEYMYDLFSVIIHKGGCYGGHYHVYIKD 312
Cdd:cd02674   168 FTGPFKYDLYAVVNHYGSLNGGHYTAYCKN 197
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 40-311 9.03e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 97.66  E-value: 9.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  40 LSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLgpeeLGSLEDKDKPEAKVRIIPLQLQRLFA-----QLLLVDQEAAST 114
Cdd:cd02671    24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVEQLQSSFLLNPEKYNDELAnqaprRLLNALREVNPM 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 115 TdltdsfgwtsdEEMRQHDVQE-LNRILFSAletslvgtsgHDLIHRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAV- 192
Cdd:cd02671   100 Y-----------EGYLQHDAQEvLQCILGNI----------QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 193 ---------------KNVSGLEDALWNM--YVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVK 255
Cdd:cd02671   159 eselskseesseispDPKTEMKTLKWAIsqFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958802784 256 CERYKDTSCYTFPLRINLKPFCEQSDMDDMEYMYDLFSVIIHKGGCYG-GHYHVYIK 311
Cdd:cd02671   239 FDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISsGHYTAYVR 295
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
42-343 1.67e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 84.08  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHF-TPEFREALFSLgPEELGSLEDK-DKPEAKVRIipLQLQRLFAQLLLVDQEaasttdltd 119
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALyLPKLDELLDDL-SKELKVLKNViRKPEPDLNQ--EEALKLFTALWSSKEH--------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 120 SFGWTSDEEmRQHDVQELNRILFSALETSLVGTsghdlihrlyhGTIVNQIVCKEckNVSERQEDFLDLTVA------VK 193
Cdd:COG5533    69 KVGWIPPMG-SQEDAHELLGKLLDELKLDLVNS-----------FTIRIFKTTKD--KKKTSTGDWFDIIIElpdqtwVN 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 194 NVSGLEDALwnmyveeeifdyDNLYHCGTCDRLVKAAKSAKLR------------KLPPFLTISLLRF--NFDFVKCERY 259
Cdd:COG5533   135 NLKTLQEFI------------DNMEELVDDETGVKAKENEELEvqakqeyevsfvKLPKILTIQLKRFanLGGNQKIDTE 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 260 KDTscytfPLRINLKPfcEQSDMDDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlgnWqcqEEISDSAVNlkaPQNEE 339
Cdd:COG5533   203 VDE-----KFELPVKH--DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGK---W---EKANDSDVT---PVSEE 266


                  ....
gi 1958802784 340 ETDD 343
Cdd:COG5533   267 EAIN 270
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-309 1.48e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 80.10  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALfslgpeelgsledkdkpeakvriiplqlqrlfaqlllvdqeaasttdltdsf 121
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------------------------------------------- 28

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 122 gwtsDEEMRQHDVQELNRILFSALETSLVGtsghdlihrLYHGTIVNQIVCKECKNVSE-RQEDFLDLTVAVKNVSG--- 197
Cdd:cd02662    29 ----EEFLEQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSgsg 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 198 -LEDALWNMYVEEEIFDYDNLYHCgtcdrlvkaakSAKLRKLPPFLTISLLRFNFDfVKCERYKDTSCYTFPLRINlkpf 276
Cdd:cd02662    96 tTLEHCLDDFLSTEIIDDYKCDRC-----------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP---- 159

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958802784 277 ceqsdmddmEYMYDLFSVIIHKGGCYGGHYHVY 309
Cdd:cd02662   160 ---------KVLYRLRAVVVHYGSHSSGHYVCY 183
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-319 3.60e-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: 80.45  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLEDKDKpeakvriIPLQLQRLFAQLllvDQEAASTTDLT--- 118
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDN-------LTNALRDLFDTM---DKKQEPVPPIEflq 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 119 ------DSFGWTSDEEM-RQHDVQELNRILFSALETSLVGTSGH-DLIHRLYHGTIVNQIVCKECKNVSE---RQEDFLD 187
Cdd:cd02657    71 llrmafPQFAEKQNQGGyAQQDAEECWSQLLSVLSQKLPGAGSKgSFIDQLFGIELETKMKCTESPDEEEvstESEYKLQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 188 LTVAVK-NVSGLEDALwNMYVEEEIfdydnLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFnfdFVKCE---RYKDTS 263
Cdd:cd02657   151 CHISITtEVNYLQDGL-KKGLEEEI-----EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRF---FWKRDiqkKAKILR 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958802784 264 CYTFPLRINLKPFCEQSDmddmeyMYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW 319
Cdd:cd02657   222 KVKFPFELDLYELCTPSG------YYELVAVITHQGrSADSGHYVAWVRR-KNDGKW 271
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-319 1.25e-15

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 78.90  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLG---------PEE--------LG--------SLEDKDKPEAK---VRII 93
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkfpsdvvdPANdlncqlikLAdgllsgrySKPASLKSENDpyqVGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  94 PLQLQRLFAQlllvDQEAASTtdltdsfgwtsdeeMRQHDVQELNRILFSALETSLVGTSGHDLIhRLYHGTIVNQIVCK 173
Cdd:cd02658    81 PSMFKALIGK----GHPEFST--------------MRQQDALEFLLHLIDKLDRESFKNLGLNPN-DLFKFMIEDRLECL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 174 ECKNV--SERQEDFLDLTV-------------AVKNVSgLEDALwNMYVEEEIFDYdnlyHCGTCDRLVKAAKSAKLRKL 238
Cdd:cd02658   142 SCKKVkyTSELSEILSLPVpkdeatekeegelVYEPVP-LEDCL-KAYFAPETIED----FCSTCKEKTTATKTTGFKTF 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 239 PPFLTISLLRFNF--DFVkcerykdtscytfPLRINLkpfceQSDMDDME--YMYDLFSVIIHKG-GCYGGHYHVYI-KD 312
Cdd:cd02658   216 PDYLVINMKRFQLleNWV-------------PKKLDV-----PIDVPEELgpGKYELIAFISHKGtSVHSGHYVAHIkKE 277


                  ....*..
gi 1958802784 313 VDHLGNW 319
Cdd:cd02658   278 IDGEGKW 284
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 42-312 3.93e-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 [Multi-domain]  Cd Length: 343  Bit Score: 68.67  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  42 GIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEELGSLEDKDK----PEAKVRIIPL--------QLQRLFAQLLLVDQ 109
Cdd:cd02666     3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTerriGGREVSRSELqrsnqfvyELRSLFNDLIHSNT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 110 EAAsttdltdsfgwTSDEE-----MRQHDVQELNRILFSALETSLVGTSGH-------------DLIHRLYHGTIVNQIV 171
Cdd:cd02666    83 RSV-----------TPSKElaylaLRQQDVTECIDNVLFQLEVALEPISNAfagpdteddkeqsDLIKRLFSGKTKQQLV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 172 cKECKN----VSERQEDFLDLTVAV------KNVSG----LEDALwnmyveEEIFDYdnlyhcgtcDRLVKA-AKSAKLR 236
Cdd:cd02666   152 -PESMGnqpsVRTKTERFLSLLVDVgkkgreIVVLLepkdLYDAL------DRYFDY---------DSLTKLpQRSQVQA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 237 KLPPFLTISLLRfnfdfvkCERY-------------------KDTSCYTFPLRINLKPFCEQSDMDDM-EYMYDLFSVII 296
Cdd:cd02666   216 QLAQPLQRELIS-------MDRYelpssiddidelireaiqsESSLVRQAQNELAELKHEIEKQFDDLkSYGYRLHAVFI 288

                         330
                  ....*....|....*.
gi 1958802784 297 HKGGCYGGHYHVYIKD 312
Cdd:cd02666   289 HRGEASSGHYWVYIKD 304
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
41-311 1.63e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 66.53  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  41 SGIRNQGGTCYLSSLLQTLHFTPEFRE-ALFSLGPE---------ELGSLEDkdkPEAKVRIIPLQ---LQRLFAQLllv 107
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATEclkehcllcELGFLFD---MLEKAKGKNCQasnFLRALSSI--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 108 dqEAASTTDLTDSFGWTSDEEMRQHDVQELNRILFS-----ALETSLVGTSGHDLIHRLYHGTIVNQIVCKECKNVSERQ 182
Cdd:pfam13423  75 --PEASALGLLDEDRETNSAISLSSLIQSFNRFLLDqlsseENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 183 EDF--LDLTVAVKNVSGLEDALWN---MYVEEEIF-DYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKC 256
Cdd:pfam13423 153 SSThvLDLIYPRKPSSNNKKPPNQtfsSILKSSLErETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958802784 257 ERykdTSCYtFPLRINLKPFcEQSDMDDMEYMYDLFSVIIH-KGGCYGGHYHVYIK 311
Cdd:pfam13423 233 WK---TPGW-LPPEIGLTLS-DDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVK 283
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
198-337 1.86e-09

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 61.82  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 198 LEDALwNMYVEEEIFDYDNLYHCGTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDfvKCERYKDTSCYTFPL-RINLKPF 276
Cdd:COG5560   677 LQDCL-NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPIdDLDLSGV 753

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958802784 277 ceQSDMDDMEYMYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNWQCqeeISDSAVNLKAPQN 337
Cdd:COG5560   754 --EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFAN-NGWYL---FDDSRITEVDPED 808
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 131-326 7.34e-06

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 48.32  E-value: 7.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 131 QHDVQELNRILFSALE---------TSLVGTSGHDLIhRLYHGTIVNQIVCKECKnvSERQEDFLDLTVAVKNVSGLEDA 201
Cdd:cd02665    22 QQDVSEFTHLLLDWLEdafqaaaeaISPGEKSKNPMV-QLFYGTFLTEGVLEGKP--FCNCETFGQYPLQVNGYGNLHEC 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 202 LWNMYVEEEIfdyDNLyhcgTCDRLVKAAKSAKLRKLPPFLTISLLRFNFDFVKCERYKDTScyTFPLRINLKPfceqsd 281
Cdd:cd02665    99 LEAAMFEGEV---ELL----PSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKL--EFPQIIQQVP------ 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958802784 282 mddmeymYDLFSVIIHKGGCYGGHYHVYIKDvDHLGNWQCQEEIS 326
Cdd:cd02665   164 -------YELHAVLVHEGQANAGHYWAYIYK-QSRQEWEKYNDIS 200
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
40-190 4.08e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 44.10  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784  40 LSGIRNQGGTCYLSSLLQTLHFTPEFREALFSLGPEElgsledkDKPEAKVRIIPLQLQRLFAQLL--LVDQEAASTTDL 117
Cdd:COG5560   265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEE-------SINEENPLGMHGSVASAYADLIkqLYDGNLHAFTPS 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802784 118 TDSFGWTSDEEM----RQHDVQE------------LNRILFSALETSLVGTSGHDL-----------IHRLYHGTIVNQ- 169
Cdd:COG5560   338 GFKKTIGSFNEEfsgyDQQDSQEfiaflldglhedLNRIIKKPYTSKPDLSPGDDVvvkkkakecwwEHLKRNDSIITDl 417

                         170       180
                  ....*....|....*....|....*....
gi 1958802784 170 --------IVCKECKNVSERQEDFLDLTV 190
Cdd:COG5560   418 fqgmykstLTCPGCGSVSITFDPFMDLTL 446
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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