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Conserved domains on  [gi|1068937215|ref|NP_001332958|]
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ubiquitin carboxyl-terminal hydrolase 45 isoform f [Homo sapiens]

Protein Classification

Peptidase_C19K domain-containing protein( domain architecture ID 10119289)

Peptidase_C19K domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
243-451 3.42e-74

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


:

Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 234.20  E-value: 3.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 243 AFQTLS-QSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKnkqkyqeetsfaekkvegvytnARKQLLISAVPAV 321
Cdd:cd02667    95 PFLDLSlPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK----------------------AKKQYLISKLPPV 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 322 LILHLKRFHQAGL-SLRKVNRHVDFPLMLDLAPFCSATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKVRTPSRKL 400
Cdd:cd02667   153 LVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRL 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1068937215 401 SEHNtkkkNVPGLKAADNESAGQWVHVSDTYLQVVPESRALSAQAYLLFYE 451
Cdd:cd02667   233 SDLT----KSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
 
Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
243-451 3.42e-74

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 234.20  E-value: 3.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 243 AFQTLS-QSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKnkqkyqeetsfaekkvegvytnARKQLLISAVPAV 321
Cdd:cd02667    95 PFLDLSlPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK----------------------AKKQYLISKLPPV 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 322 LILHLKRFHQAGL-SLRKVNRHVDFPLMLDLAPFCSATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKVRTPSRKL 400
Cdd:cd02667   153 LVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRL 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1068937215 401 SEHNtkkkNVPGLKAADNESAGQWVHVSDTYLQVVPESRALSAQAYLLFYE 451
Cdd:cd02667   233 SDLT----KSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
238-450 1.11e-30

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 120.24  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 238 YSPQNAFQTLSQSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKNKQKYqeetsfaekkvegvytnarKQLLISA 317
Cdd:pfam00443 142 FEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAI-------------------KQLKISR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 318 VPAVLILHLKRFHQAGLSLRKVNRHVDFPLMLDLAPFCsATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKvrtps 397
Cdd:pfam00443 203 LPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYL-AEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK----- 276
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1068937215 398 rklsehntkkknvpglkaadNESAGQWVHVSDTYLQVVPESRA-LSAQAYLLFY 450
Cdd:pfam00443 277 --------------------AYENNRWYKFDDEKVTEVDEETAvLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
212-452 1.41e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 76.08  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 212 QDFDRENQPLNIsNNLCFLEGKHLRSYSPQNAFQTLSQSyITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKNKQky 291
Cdd:COG5560   631 EEEGQMNFNDAV-VISCEWEEKRYLSLFSYDPLWTIREI-GAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQ-- 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 292 qeetsfaekkvegvytnARKQLLISAVPAVLILHLKRFHQAGLSLRKVNRHVDFPLM-LDLAPFCSATcknasVGDKVLY 370
Cdd:COG5560   707 -----------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGVEYMV-----DDPRLIY 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 371 GLYGIVEHSGSMREGHYTAYVKvrtpsrklsehntkkknvpglkaadNESAGQWVHVSDTYLQVVPESRALSAQAYLLFY 450
Cdd:COG5560   765 DLYAVDNHYGGLSGGHYTAYAR-------------------------NFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819

                  ..
gi 1068937215 451 ER 452
Cdd:COG5560   820 RR 821
 
Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
243-451 3.42e-74

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 234.20  E-value: 3.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 243 AFQTLS-QSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKnkqkyqeetsfaekkvegvytnARKQLLISAVPAV 321
Cdd:cd02667    95 PFLDLSlPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK----------------------AKKQYLISKLPPV 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 322 LILHLKRFHQAGL-SLRKVNRHVDFPLMLDLAPFCSATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKVRTPSRKL 400
Cdd:cd02667   153 LVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPQQRL 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1068937215 401 SEHNtkkkNVPGLKAADNESAGQWVHVSDTYLQVVPESRALSAQAYLLFYE 451
Cdd:cd02667   233 SDLT----KSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
252-451 1.03e-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: 124.52  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 252 ITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKnkqkyqeetsfaekkvegvyTNARKQLLISAVPAVLILHLKRFHQ 331
Cdd:cd02257    93 VKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKK--------------------QEATKRLKIKKLPPVLIIHLKRFSF 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 332 AGL-SLRKVNRHVDFPLMLDLAPFCSATCKNASVGDK-VLYGLYGIVEHSG-SMREGHYTAYVKVRTPsrklsehntkkk 408
Cdd:cd02257   153 NEDgTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGsYKYELVAVVVHSGtSADSGHYVAYVKDPSD------------ 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1068937215 409 nvpglkaadnesaGQWVHVSDTYLQVVPESRAL-----SAQAYLLFYE 451
Cdd:cd02257   221 -------------GKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
259-450 9.45e-32

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 123.15  E-value: 9.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 259 SIQSCLYQFTSMELLMGNNKLLCENCTKnkqkyqeetsfaekkvegvYTNARKQLLISAVPAVLILHLKRFhqAGLSLRK 338
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKK-------------------KVKASKQLTIHRAPNVLTIHLKRF--SNFRGGK 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 339 VNRHVDFPLMLDLAPFCSatcKNASVGDKvlYGLYGIVEHSG-SMREGHYTAYVKvrtpsrklsehntkkknvpglkaad 417
Cdd:cd02661   222 INKQISFPETLDLSPYMS---QPNDGPLK--YKLYAVLVHSGfSPHSGHYYCYVK------------------------- 271
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1068937215 418 nESAGQWVHVSDTYLQVVPESRALSAQAYLLFY 450
Cdd:cd02661   272 -SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
238-450 1.11e-30

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 120.24  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 238 YSPQNAFQTLSQSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKNKQKYqeetsfaekkvegvytnarKQLLISA 317
Cdd:pfam00443 142 FEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAI-------------------KQLKISR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 318 VPAVLILHLKRFHQAGLSLRKVNRHVDFPLMLDLAPFCsATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKvrtps 397
Cdd:pfam00443 203 LPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYL-AEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK----- 276
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1068937215 398 rklsehntkkknvpglkaadNESAGQWVHVSDTYLQVVPESRA-LSAQAYLLFY 450
Cdd:pfam00443 277 --------------------AYENNRWYKFDDEKVTEVDEETAvLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-451 2.91e-30

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 117.00  E-value: 2.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 256 KECSIQSCLYQFTSMELLMGNNKLLCENCTKNkqkyqeetsfaekkvegvyTNARKQLLISAVPAVLILHLKRFHQAGLS 335
Cdd:cd02674    82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKK-------------------RKATKKLTISRLPKVLIIHLKRFSFSRGS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 336 LRKVNRHVDFPL-MLDLAPFCSATCKNASvgdkVLYGLYGIVEHSGSMREGHYTAYVKvrtpsrklsehntkkknvpglk 414
Cdd:cd02674   143 TRKLTTPVTFPLnDLDLTPYVDTRSFTGP----FKYDLYAVVNHYGSLNGGHYTAYCK---------------------- 196
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1068937215 415 aadNESAGQWVHVSDTYLQVVPESRALSAQAYLLFYE 451
Cdd:cd02674   197 ---NNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
259-450 1.03e-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: 115.16  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 259 SIQSCLYQFTSMELLmGNNKLLCENCtknkqkyqeetsfaekkveGVYTNARKQLLISAVPAVLILHLKRF-HQAGLSLR 337
Cdd:cd02660   177 TLSDCLDRFTRPEKL-GDFAYKCSGC-------------------GSTQEATKQLSIKKLPPVLCFQLKRFeHSLNKTSR 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 338 KVNRHVDFPLMLDLAPFCSATC-----KNASVGDKVlYGLYGIVEHSGSMREGHYTAYVKVRTpsrklsehntkkknvpg 412
Cdd:cd02660   237 KIDTYVQFPLELNMTPYTSSSIgdtqdSNSLDPDYT-YDLFAVVVHKGTLDTGHYTAYCRQGD----------------- 298
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1068937215 413 lkaadnesaGQWVHVSDTYLQVVPESRALSAQAYLLFY 450
Cdd:cd02660   299 ---------GQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
259-453 3.95e-20

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 91.16  E-value: 3.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 259 SIQSCLYQFTSMELLMGNNKLLCENCtknkqkyqeetsfaEKKVEgvytnARKQLLISAVPAVLILHLKRFHQAGLSLR- 337
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKC--------------GKKVD-----AEKGVCFKKLPPVLTLQLKRFEFDFETMMr 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 338 -KVNRHVDFPLMLDLAPFCSATCKNASVGDKV------LYGLYGIVEHSGSMREGHYTAYVKVRTPSR----------KL 400
Cdd:cd02659   213 iKINDRFEFPLELDMEPYTEKGLAKKEGDSEKkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKwykfnddvvtPF 292
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1068937215 401 SEHNTKKKNVPGlkaadnesagqwvHVSDTYLQVVPESRALSAQAYLLFYERV 453
Cdd:cd02659   293 DPNDAEEECFGG-------------EETQKTYDSGPRAFKRTTNAYMLFYERK 332
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
310-451 1.40e-17

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 81.64  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 310 RKQLLISAVPAVLILHLKR--FHQAGLSLRKvNRHVDFPLMLDlapfcsatcknasvgdKVLYGLYGIVEHSGSMREGHY 387
Cdd:cd02662   118 RCQTVIVRLPQILCIHLSRsvFDGRGTSTKN-SCKVSFPERLP----------------KVLYRLRAVVVHYGSHSSGHY 180
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1068937215 388 TAYVKVRTPSRKLSEHNTKKknvpgLKAADNESAGQWVHVSDTYLQVVPESRAL-SAQAYLLFYE 451
Cdd:cd02662   181 VCYRRKPLFSKDKEPGSFVR-----MREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
256-451 9.30e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 77.74  E-value: 9.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 256 KECSIQSCLYQFTSMELLMGNNKLLCENCtknkQKYQEetsfaekkvegvytnARKQLLISAVPAVLILHLKRFHQAGls 335
Cdd:cd02663   145 QNTSITSCLRQFSATETLCGRNKFYCDEC----CSLQE---------------AEKRMKIKKLPKILALHLKRFKYDE-- 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 336 lrKVNRH------VDFPLMLDLapfcSATCKNASVGDKvLYGLYGIVEHSGS--MReGHYTAYVKvrtpsrklsehntkk 407
Cdd:cd02663   204 --QLNRYiklfyrVVFPLELRL----FNTTDDAENPDR-LYELVAVVVHIGGgpNH-GHYVSIVK--------------- 260
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1068937215 408 knvpglkaadneSAGQWV--------HVSDTYLQVVPESRALSAQAYLLFYE 451
Cdd:cd02663   261 ------------SHGGWLlfddetveKIDENAVEEFFGDSPNQATAYVLFYQ 300
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
212-452 1.41e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 76.08  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 212 QDFDRENQPLNIsNNLCFLEGKHLRSYSPQNAFQTLSQSyITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKNKQky 291
Cdd:COG5560   631 EEEGQMNFNDAV-VISCEWEEKRYLSLFSYDPLWTIREI-GAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQ-- 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 292 qeetsfaekkvegvytnARKQLLISAVPAVLILHLKRFHQAGLSLRKVNRHVDFPLM-LDLAPFCSATcknasVGDKVLY 370
Cdd:COG5560   707 -----------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGVEYMV-----DDPRLIY 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 371 GLYGIVEHSGSMREGHYTAYVKvrtpsrklsehntkkknvpglkaadNESAGQWVHVSDTYLQVVPESRALSAQAYLLFY 450
Cdd:COG5560   765 DLYAVDNHYGGLSGGHYTAYAR-------------------------NFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819

                  ..
gi 1068937215 451 ER 452
Cdd:COG5560   820 RR 821
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
266-392 2.72e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 73.77  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 266 QFTSMELLMGNNKLLCENCTKnkqkyqeetsfaekkvegvYTNARKQLLISAVPAVLILHLKRFHQAGLS------LRKV 339
Cdd:cd02671   188 QFASVERIVGEDKYFCENCHH-------------------YTEAERSLLFDKLPEVITIHLKCFAANGSEfdcyggLSKV 248
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1068937215 340 NRHVDFPLMLDLAPFCSATcknasvgDKVLYGLYGIVEHSG-SMREGHYTAYVK 392
Cdd:cd02671   249 NTPLLTPLKLSLEEWSTKP-------KNDVYRLFAVVMHSGaTISSGHYTAYVR 295
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
258-451 4.28e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 72.91  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 258 CSIQSCLYQFTSMELLMGNNKLLCENCTKNKQkyqeetsfAEKKVEgvytnarkqllISAVPAVLILHLKRFH--QAGLS 335
Cdd:cd02664   134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQD--------AEKEMK-----------VTGAPEYLILTLLRFSydQKTHV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 336 LRKVNRHVDFPLMLDLaPFCSATCKNASVGDK---------------VLYGLYGIVEHSG-SMREGHYTAYVKVRTPSRK 399
Cdd:cd02664   195 REKIMDNVSINEVLSL-PVRVESKSSESPLEKkeeesgddgelvtrqVHYRLYAVVVHSGySSESGHYFTYARDQTDADS 273
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1068937215 400 lsehnTKKKNVPGLKAADNESAGQWVHVSDTYlqvVPESRALSAQ----------AYLLFYE 451
Cdd:cd02664   274 -----TGQECPEPKDAEENDESKNWYLFNDSR---VTFSSFESVQnvtsrfpkdtPYILFYE 327
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
227-392 2.60e-13

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 70.53  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 227 LCFLEGKHLRSYSP--QNAFQTLSQ---SYITTSKEC---------------------SIQSCLYQFTSMELLMGNNKLL 280
Cdd:cd02668    99 LSLLEAKLSKSKNPdlKNIVQDLFRgeySYVTQCSKCgresslpskfyelelqlkghkTLEECIDEFLKEEQLTGDNQYF 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 281 CENCTKNkqkyqeetsfaekkvegvyTNARKQLLISAVPAVLILHLKR--FHQAGLSLRKVNRHVDFPLMLDLAPFCSAT 358
Cdd:cd02668   179 CESCNSK-------------------TDATRRIRLTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEILDMGEYLAES 239
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1068937215 359 CKNASVgdkvlYGLYGIVEHSG-SMREGHYTAYVK 392
Cdd:cd02668   240 DEGSYV-----YELSGVLIHQGvSAYSGHYIAHIK 269
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
259-392 3.87e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 68.74  E-value: 3.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215  259 SIQSCLYQFTSMELLMGNNKLLCEnctknKQKYQEetsfaekkvegvytnARKQLLISAVPAVLILHLKRFHQAGLS--L 336
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAE-----KHGLQD---------------AKKGVIFESLPPVLHLQLKRFEYDFERdmM 398
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1068937215  337 RKVNRHVDFPLMLDLAPFCSATCKNASVGDKVlYGLYGIVEHSGSMREGHYTAYVK 392
Cdd:COG5077    399 VKINDRYEFPLEIDLLPFLDRDADKSENSDAV-YVLYGVLVHSGDLHEGHYYALLK 453
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
284-452 3.53e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 63.67  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 284 CTKNKQKYQ--EETSFAEKKVEGVYTNARKQLLISAV--PAVLILHLKRFHQAGlSLRKVNRHVDFPLMLDLAPfcsatC 359
Cdd:COG5533   141 EFIDNMEELvdDETGVKAKENEELEVQAKQEYEVSFVklPKILTIQLKRFANLG-GNQKIDTEVDEKFELPVKH-----D 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 360 KNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKVRtpsrklsehntkkknvpglkaadnesaGQWVHVSDTYLQVVPESR 439
Cdd:COG5533   215 QILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKG---------------------------GKWEKANDSDVTPVSEEE 267
                         170
                  ....*....|....*.
gi 1068937215 440 AL---SAQAYLLFYER 452
Cdd:COG5533   268 AInekAKNAYLYFYER 283
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-407 1.11e-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 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: 62.35  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 288 KQKYQEETsfaEKKVEGVYTNA--RKQLLISAVPAVLILHLKRFHQAGLSLR--KVNRHVDFPLMLDLAPFCSATCknas 363
Cdd:cd02657   167 KKGLEEEI---EKHSPTLGRDAiyTKTSRISRLPKYLTVQFVRFFWKRDIQKkaKILRKVKFPFELDLYELCTPSG---- 239
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1068937215 364 vgdkvLYGLYGIVEHSG-SMREGHYTAYVKVRTPSR-------KLSEHNTKK 407
Cdd:cd02657   240 -----YYELVAVITHQGrSADSGHYVAWVRRKNDGKwikfdddKVSEVTEED 286
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
297-451 2.87e-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: 48.86  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 297 FAEKKVE------GVYTNARKQLLISAVPAVLILHLKRFH-QAGLSLRKVNRHVDFPLMLDLAPfcsatcknasvgdkvl 369
Cdd:cd02658   188 FAPETIEdfcstcKEKTTATKTTGFKTFPDYLVINMKRFQlLENWVPKKLDVPIDVPEELGPGK---------------- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 370 YGLYGIVEHSG-SMREGHYTAYVKvrtpsrklsehntkkknvpglKAADNEsaGQWVHVSDTYLQVVPESRALSAQAYLL 448
Cdd:cd02658   252 YELIAFISHKGtSVHSGHYVAHIK---------------------KEIDGE--GKWVLFNDEKVVASQDPPEMKKLGYIY 308

                  ...
gi 1068937215 449 FYE 451
Cdd:cd02658   309 FYQ 311
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
315-451 4.61e-05

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 44.83  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 315 ISAVPAVLILHLKRFHQAGLSLRKVNRHVDFPLMLDLAPF----------CSATCKNASVGD-------KVLYGLYGIVE 377
Cdd:cd02670    95 FAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFvaddpracskCQLECRVCYDDKdfsptcgKFKLSLCSAVC 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068937215 378 HSGSMRE-GHYTAYVKVrtpsrklsehNTKKKNVPGLKAADNesagQWVHVSD-------TYLQVVPESRALSaQAYLLF 449
Cdd:cd02670   175 HRGTSLEtGHYVAFVRY----------GSYSLTETDNEAYNA----QWVFFDDmadrdgvSNGFNIPAARLLE-DPYMLF 239

                  ..
gi 1068937215 450 YE 451
Cdd:cd02670   240 YQ 241
 
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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