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Conserved domains on  [gi|376319203|ref|NP_001243656|]
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ubiquitin carboxyl-terminal hydrolase 39 isoform 3 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119323)

ubiquitin carboxyl-terminal hydrolase family protein contains a zinc finger ubiquitin binding domain (ZnF-UBP) and an inactive ubiquitin-specific protease (iUSP) domain, similar to human U4/U6.U5 tri-snRNP-associated protein 2 that plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the precatalytic spliceosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 28-475 0e+00

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: 703.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  28 PYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSS 107
Cdd:cd02669    1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 108 LEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKrp 187
Cdd:cd02669   81 LDDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIK-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 188 pgDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIV 267
Cdd:cd02669  159 --DRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSII 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 268 TDVFQGSMRIFTKKLPHPDLPAEEKeQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGI 347
Cdd:cd02669  237 HDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 348 TEKEYKTYkenfLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVH 427
Cdd:cd02669  316 TETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVH 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 376319203 428 DGKPSE-GSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWK 475
Cdd:cd02669  392 EGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
 
Name Accession Description Interval E-value
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 28-475 0e+00

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: 703.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  28 PYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSS 107
Cdd:cd02669    1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 108 LEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKrp 187
Cdd:cd02669   81 LDDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIK-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 188 pgDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIV 267
Cdd:cd02669  159 --DRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSII 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 268 TDVFQGSMRIFTKKLPHPDLPAEEKeQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGI 347
Cdd:cd02669  237 HDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 348 TEKEYKTYkenfLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVH 427
Cdd:cd02669  316 TETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVH 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 376319203 428 DGKPSE-GSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWK 475
Cdd:cd02669  392 EGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
147-474 9.87e-51

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 9.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  147 VGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLvqRFGELMRKLWnPRNFKAHVSPHeMLQAVV 226
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLC--ALRDLFKALQ-KNSKSSSVSPK-MFKKSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  227 LCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKT-IVTDVFQGSMRIFTKKLphpdlpaeekeqllhNDEYQETm 305
Cdd:pfam00443  77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENEsLITDLFRGQLKSRLKCL---------------SCGEVSE- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  306 VESTFMYLTLDLPTAPlYKDEKEQLIIPQVPLFNILAKFNGITEKEYKTY-KENFLKRFQLTKLPPYLIFCIKRFTKNNF 384
Cdd:pfam00443 141 TFEPFSDLSLPIPGDS-AELKTASLQICFLQFSKLEELDDEEKYYCDKCGcKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  385 FVEKNPTIVNFPITnVDLREYLSEEVQAVHKN-TTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQM 463
Cdd:pfam00443 220 TWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET 298

                         330
                  ....*....|..
gi 376319203  464 ITLSE-AYIQIW 474
Cdd:pfam00443 299 AVLSSsAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
290-477 3.04e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 72.22  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 290 EEKEQLLHND------EYQETMVESTFMYltldlptAPLYKDEKEQLIIPQVPLFNILAKFN-----GITEKEY-KTYKE 357
Cdd:COG5560  631 EEEGQMNFNDavviscEWEEKRYLSLFSY-------DPLWTIREIGAAERTITLQDCLNEFSkpeqlGLSDSWYcPGCKE 703

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 358 N--FLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYlseEVQAVHKNTTYDLIANIVHDGKPSEGS 435
Cdd:COG5560  704 FrqASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGV---EYMVDDPRLIYDLYAVDNHYGGLSGGH 780

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 376319203 436 YRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWKRR 477
Cdd:COG5560  781 YTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
46-94 1.71e-11

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 58.92  E-value: 1.71e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 376319203    46 CSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKF 94
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 28-475 0e+00

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: 703.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  28 PYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSS 107
Cdd:cd02669    1 PYLDTINRSVLDFDFEKVCSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 108 LEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKrp 187
Cdd:cd02669   81 LDDIKYVLNPTYTKEQISDLDRDPKLSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIK-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 188 pgDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIV 267
Cdd:cd02669  159 --DRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSII 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 268 TDVFQGSMRIFTKKLPHPDLPAEEKeQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGI 347
Cdd:cd02669  237 HDCFQGKVQIETQKIKPHAEEEGSK-DKFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEENIIPQVPLKQLLKKYDGK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 348 TEKEYKTYkenfLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVH 427
Cdd:cd02669  316 TETELKDS----LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVH 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 376319203 428 DGKPSE-GSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWK 475
Cdd:cd02669  392 EGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
147-474 9.87e-51

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 9.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  147 VGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLvqRFGELMRKLWnPRNFKAHVSPHeMLQAVV 226
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLC--ALRDLFKALQ-KNSKSSSVSPK-MFKKSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  227 LCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKT-IVTDVFQGSMRIFTKKLphpdlpaeekeqllhNDEYQETm 305
Cdd:pfam00443  77 GKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENEsLITDLFRGQLKSRLKCL---------------SCGEVSE- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  306 VESTFMYLTLDLPTAPlYKDEKEQLIIPQVPLFNILAKFNGITEKEYKTY-KENFLKRFQLTKLPPYLIFCIKRFTKNNF 384
Cdd:pfam00443 141 TFEPFSDLSLPIPGDS-AELKTASLQICFLQFSKLEELDDEEKYYCDKCGcKQDAIKQLKISRLPPVLIIHLKRFSYNRS 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  385 FVEKNPTIVNFPITnVDLREYLSEEVQAVHKN-TTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQM 463
Cdd:pfam00443 220 TWEKLNTEVEFPLE-LDLSRYLAEELKPKTNNlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEET 298

                         330
                  ....*....|..
gi 376319203  464 ITLSE-AYIQIW 474
Cdd:pfam00443 299 AVLSSsAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 237-475 2.45e-32

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: 124.13  E-value: 2.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 237 KQGDGVDFLSWFLNALHSALGGTKKKKKT------IVTDVFQGSMRIFTKKLphpdlpaeekeqllhnDEYQETMVESTF 310
Cdd:cd02257   21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDssslksLIHDLFGGKLESTIVCL----------------ECGHESVSTEPE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 311 MYLTLDLPTAPlykdekeqliIPQVPLFNILAKFNG--ITEKEYKTY-----KENFLKRFQLTKLPPYLIFCIKRFTKNN 383
Cdd:cd02257   85 LFLSLPLPVKG----------LPQVSLEDCLEKFFKeeILEGDNCYKcekkkKQEATKRLKIKKLPPVLIIHLKRFSFNE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 384 -FFVEKNPTIVNFPITNVDLREYLSEEVQAV--HKNTTYDLIANIVHDGK-PSEGSYRIHVLHHGTGKWYELQDLQVTDI 459
Cdd:cd02257  155 dGTKEKLNTKVSFPLELDLSPYLSEGEKDSDsdNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEV 234

                        250       260
                 ....*....|....*....|.
gi 376319203 460 LPQMITL-----SEAYIQIWK 475
Cdd:cd02257  235 SEEEVLEfgslsSSAYILFYE 255
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 237-471 4.26e-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: 94.66  E-value: 4.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 237 KQGDGVDFLSWFLNALHSalggtkkkkktIVTDVFQGSMRIFTKKLphpdlpaeekeqllhNDEYQETMVEsTFMYLTLD 316
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHS-----------IIVDLFQGQLKSRLTCL---------------TCGKTSTTFE-PFTYLSLP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 317 LPtaplykdeKEQLIIPQVPLF---------NILAKFNGITEKEYKTyKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVE 387
Cdd:cd02674   74 IP--------SGSGDAPKVTLEdclrlftkeETLDGDNAWKCPKCKK-KRKATKKLTISRLPKVLIIHLKRFSFSRGSTR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 388 KNPTIVNFPITNVDLREYLSEEVQAvhKNTTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQMITLS 467
Cdd:cd02674  145 KLTTPVTFPLNDLDLTPYVDTRSFT--GPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSS 222


                 ....
gi 376319203 468 EAYI 471
Cdd:cd02674  223 SAYI 226
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
46-108 1.21e-20

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 85.39  E-value: 1.21e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 376319203   46 CSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSSL 108
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 148-471 2.96e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 79.24  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 148 GLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLVQRfgeLMRKLWNPRNFKAHVSPHEMLQavvl 227
Cdd:cd02661    3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAH---VERALASSGPGSAPRIFSSNLK---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 228 CSKKTFQITKQGDGVDFLSWFLNALHSAlGGTKKKKKTIVTDVFQGSM---RIFTKKLphpdlpaeeKEQLL-HN----- 298
Cdd:cd02661   76 QISKHFRIGRQEDAHEFLRYLLDAMQKA-CLDRFKKLKAVDPSSQETTlvqQIFGGYL---------RSQVKcLNckhvs 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 299 DEYQEtmvestFMYLTLDLPTAPLYKDEKEQLIIPQvplfnILAKFNgitekEYKTYKENFL----KRFQLTKLPPYLIF 374
Cdd:cd02661  146 NTYDP------FLDLSLDIKGADSLEDALEQFTKPE-----QLDGEN-----KYKCERCKKKvkasKQLTIHRAPNVLTI 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 375 CIKRFTknNFFVEKNPTIVNFPITnVDLREYLSeevQAVHKNTTYDLIANIVHDG-KPSEGSYRIHVlHHGTGKWYELQD 453
Cdd:cd02661  210 HLKRFS--NFRGGKINKQISFPET-LDLSPYMS---QPNDGPLKYKLYAVLVHSGfSPHSGHYYCYV-KSSNGKWYNMDD 282

                        330
                 ....*....|....*....
gi 376319203 454 LQVTDILPQMItLSE-AYI 471
Cdd:cd02661  283 SKVSPVSIETV-LSQkAYI 300
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 148-470 7.84e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 72.41  E-value: 7.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 148 GLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKN--IKRPPGDIMFLLVQRFGELmrklwnprNFKAHVSPHEMLqAV 225
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTclSCSPNSCLSCAMDEIFQEF--------YYSGDRSPYGPI-NL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 226 VLCS---KKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKT------IVTDVFQGSMRiftkklphpdlpaeekEQLL 296
Cdd:cd02660   73 LYLSwkhSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDeshcncIIHQTFSGSLQ----------------SSVT 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 297 HNDEYQETMVESTFMYLTLDLP-TAPLYKDEKEQLIIPQVPLFNILAKFngiTEKEYKTY----------KENFLKRFQL 365
Cdd:cd02660  137 CQRCGGVSTTVDPFLDLSLDIPnKSTPSWALGESGVSGTPTLSDCLDRF---TRPEKLGDfaykcsgcgsTQEATKQLSI 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 366 TKLPPYLIFCIKRFTKNNFFV-EKNPTIVNFPITnVDLREYLSEEVQAVH------KNTTYDLIANIVHDGKPSEGSYrI 438
Cdd:cd02660  214 KKLPPVLCFQLKRFEHSLNKTsRKIDTYVQFPLE-LNMTPYTSSSIGDTQdsnsldPDYTYDLFAVVVHKGTLDTGHY-T 291

                        330       340       350
                 ....*....|....*....|....*....|..
gi 376319203 439 HVLHHGTGKWYELQDLQVTDILPQMITLSEAY 470
Cdd:cd02660  292 AYCRQGDGQWFKFDDAMITRVSEEEVLKSQAY 323
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
290-477 3.04e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 72.22  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 290 EEKEQLLHND------EYQETMVESTFMYltldlptAPLYKDEKEQLIIPQVPLFNILAKFN-----GITEKEY-KTYKE 357
Cdd:COG5560  631 EEEGQMNFNDavviscEWEEKRYLSLFSY-------DPLWTIREIGAAERTITLQDCLNEFSkpeqlGLSDSWYcPGCKE 703

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 358 N--FLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYlseEVQAVHKNTTYDLIANIVHDGKPSEGS 435
Cdd:COG5560  704 FrqASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGV---EYMVDDPRLIYDLYAVDNHYGGLSGGH 780

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 376319203 436 YRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWKRR 477
Cdd:COG5560  781 YTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
46-94 1.71e-11

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 58.92  E-value: 1.71e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 376319203    46 CSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKF 94
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 148-459 2.25e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 61.67  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 148 GLNNIKANDYANAVLQALSNVPPLRNYFL-----EEDNYKNIKRPPGDIMFLLVQRFGELMRKLWNPRnfKAHVSPHEML 222
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGN--RSVVDPSGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 223 QAVVLCSkktfqiTKQGDGVDFLSWFLNALHSALGGTK-KKKKTIVTDVFQGSMRIFTKklphpdlpaeekeqllHNDEY 301
Cdd:cd02668   79 KALGLDT------GQQQDAQEFSKLFLSLLEAKLSKSKnPDLKNIVQDLFRGEYSYVTQ----------------CSKCG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 302 QETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQvplfnilaKFNGitEKEYK----TYKENFLKRFQLTKLPPYLIFCIK 377
Cdd:cd02668  137 RESSLPSKFYELELQLKGHKTLEECIDEFLKEE--------QLTG--DNQYFcescNSKTDATRRIRLTTLPPTLNFQLL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 378 RFT--KNNFFVEKNPTIVNFPiTNVDLREYLSEEVQAVHkntTYDLIANIVHDG-KPSEGSYRIHVLHHGTGKWYELQDL 454
Cdd:cd02668  207 RFVfdRKTGAKKKLNASISFP-EILDMGEYLAESDEGSY---VYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDE 282


                 ....*
gi 376319203 455 QVTDI 459
Cdd:cd02668  283 DVEEM 287
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
143-325 1.27e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 57.59  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 143 LPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRP-PGDIMFLLVQRFGELMRKLWNPRNfkaHVSPHEM 221
Cdd:COG5560  262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEnPLGMHGSVASAYADLIKQLYDGNL---HAFTPSG 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 222 LQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIVTDVFQGSMRIFTKKlphpdlpAEEK--EQLLHND 299
Cdd:COG5560  339 FKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKK-------AKECwwEHLKRND 411

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 376319203 300 E---------YQETMVEST----------FMYLTLDLPTAPLYKD 325
Cdd:COG5560  412 SiitdlfqgmYKSTLTCPGcgsvsitfdpFMDLTLPLPVSMVWKH 456
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 148-475 3.83e-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 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: 48.48  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 148 GLNNIKANDYANAVLQALSNVPPLRNYFLeedNYKNIKRPPGDIMFLLVQRFGELMRKLWNPRNfkaHVSPHEMLQAVVL 227
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALK---NYNPARRGANQSSDNLTNALRDLFDTMDKKQE---PVPPIEFLQLLRM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 228 C----SKKTFQ-ITKQGDGVDFLSWFLNALHSALGGTKKKkktivTDVFQGSMRI-FTKKLPHPDLPAEEkeqllhndey 301
Cdd:cd02657   75 AfpqfAEKQNQgGYAQQDAEECWSQLLSVLSQKLPGAGSK-----GSFIDQLFGIeLETKMKCTESPDEE---------- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 302 QETMVESTFMYLTLDLPTAPLYKDEKeqliipqvplfnILAKFNGITEKEYKTYKEN--FLKRFQLTKLPPYLIFCIKRF 379
Cdd:cd02657  140 EVSTESEYKLQCHISITTEVNYLQDG------------LKKGLEEEIEKHSPTLGRDaiYTKTSRISRLPKYLTVQFVRF 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 380 tknnFFVE---KNPTI---VNFPItNVDLREYLSEevqavhkNTTYDLIANIVHDGKPSE-GSYRIHVLHHGTGKWYELQ 452
Cdd:cd02657  208 ----FWKRdiqKKAKIlrkVKFPF-ELDLYELCTP-------SGYYELVAVITHQGRSADsGHYVAWVRRKNDGKWIKFD 275

                        330       340       350
                 ....*....|....*....|....*....|
gi 376319203 453 DLQVTDILPQMI-TLS------EAYIQIWK 475
Cdd:cd02657  276 DDKVSEVTEEDIlKLSgggdwhIAYILLYK 305
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 148-448 4.32e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 48.47  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 148 GLNNIKANDYANAVLQALSNVPPLRNYFLEEDN--YKNIKRPPGDIMF--------LLVQRFGELMRKLWNPRNFKAHVS 217
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfPSDVVDPANDLNCqlikladgLLSGRYSKPASLKSENDPYQVGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 218 PhEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKkkkktivTDVFQGSMRIFTkklphpdlpaEEKEQLLH 297
Cdd:cd02658   81 P-SMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNL-------GLNPNDLFKFMI----------EDRLECLS 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 298 NDEYQETMVEStfMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGITEKEY--KTYKE--NFLKRFQLTKLPPYLI 373
Cdd:cd02658  143 CKKVKYTSELS--EILSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDfcSTCKEktTATKTTGFKTFPDYLV 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 376319203 374 FCIKRFTknnFFVEKNPTIVNFPITnVDlreylseEVQAVHKnttYDLIANIVHDGK-PSEGSYRIHVL--HHGTGKW 448
Cdd:cd02658  221 INMKRFQ---LLENWVPKKLDVPID-VP-------EELGPGK---YELIAFISHKGTsVHSGHYVAHIKkeIDGEGKW 284
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 145-457 9.79e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 47.64  E-value: 9.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 145 GIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNiKRPPGDIMFLLVQRFGELmrklwnprnfkaHVSPHEMLQA 224
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED-DDDNKSVPLALQRLFLFL------------QLSESPVKTT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 225 VVLCSKKTFQITK-----QGDGVDFLSWFLNALHSALGGTKKKKktIVTDVFQGSMR--IFTKKLPHpdlpaeekeqllh 297
Cdd:cd02659   68 ELTDKTRSFGWDSlntfeQHDVQEFFRVLFDKLEEKLKGTGQEG--LIKNLFGGKLVnyIICKECPH------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 298 ndEYQEtmvESTFMYLTLDLptaplyKDEKeqliipqvplfNILAKFNGITEKE-------YKTYKENF----LKRFQLT 366
Cdd:cd02659  133 --ESER---EEYFLDLQVAV------KGKK-----------NLEESLDAYVQGEtlegdnkYFCEKCGKkvdaEKGVCFK 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 367 KLPPYLIFCIKRFTKNnfFVEKNPTIVN----FPITnVDLREYLSEEVQA--------VHKNTTYDLIANIVHDGKPSEG 434
Cdd:cd02659  191 KLPPVLTLQLKRFEFD--FETMMRIKINdrfeFPLE-LDMEPYTEKGLAKkegdsekkDSESYIYELHGVLVHSGDAHGG 267

                        330       340
                 ....*....|....*....|...
gi 376319203 435 SYRIHVLHHGTGKWYELQDLQVT 457
Cdd:cd02659  268 HYYSYIKDRDDGKWYKFNDDVVT 290
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 310-471 5.63e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 45.07  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 310 FMYLTLDLPTAPLYKDEKeqliipqvplfNILAKFNGITEKEYKTYKENFL--------KRFQLTKLPPYLIFCIKRFTK 381
Cdd:cd02667   94 EPFLDLSLPRSDEIKSEC-----------SIESCLKQFTEVEILEGNNKFAcenctkakKQYLISKLPPVLVIHLKRFQQ 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 382 NNFF-VEKNPTIVNFPiTNVDLREYLSEEVQAVHKNTT--YDLIANIVHDGKPSEGSYRIHVLHH--------------- 443
Cdd:cd02667  163 PRSAnLRKVSRHVSFP-EILDLAPFCDPKCNSSEDKSSvlYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpa 241

                        170       180       190
                 ....*....|....*....|....*....|....
gi 376319203 444 ------GTGKWYELQDLQVTDILPQMITLSEAYI 471
Cdd:cd02667  242 adeagpGSGQWYYISDSDVREVSLEEVLKSEAYL 275
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 368-457 2.16e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 44.09  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203  368 LPPYLIFCIKRFTKNnfFVEKNPTIVN----FPITnVDLREYLSEEV-QAVHKNTTYDLIANIVHDGKPSEGSYRIHVLH 442
Cdd:COG5077   378 LPPVLHLQLKRFEYD--FERDMMVKINdryeFPLE-IDLLPFLDRDAdKSENSDAVYVLYGVLVHSGDLHEGHYYALLKP 454

                          90
                  ....*....|....*
gi 376319203  443 HGTGKWYELQDLQVT 457
Cdd:COG5077   455 EKDGRWYKFDDTRVT 469
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 342-457 1.50e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 40.23  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319203 342 AKFNGITEKEYKTYKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPitnvdlreylsEEVQAVhkntTYDL 421
Cdd:cd02665  102 AMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKLEFP-----------QIIQQV----PYEL 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 376319203 422 IANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVT 457
Cdd:cd02665  167 HAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVT 202
 
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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