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Conserved domains on  [gi|966915356|ref|XP_014985823|]
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ubiquitin carboxyl-terminal hydrolase 48 isoform X5 [Macaca mulatta]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein; ubiquitin family protein( domain architecture ID 10119293)

ubiquitin carboxyl-terminal hydrolase family protein may remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds| ubiquitin family protein belongs to a diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes; has an N-terminal domain with similarity to the N-terminus of ubiquitin fusion degradation UFD1 which functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-419 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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 575.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYvlGDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668   79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668  159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668  239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313

                        330
                 ....*....|.
gi 966915356 409 CSRNAYMLVYR 419
Cdd:cd02668  314 SSRTAYMLVYK 324
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 873-968 1.76e-40

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


:

Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 143.96  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 873 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 949
Cdd:cd01795    1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80

                         90
                 ....*....|....*....
gi 966915356 950 DVMQVCMPEEGFKGTGLLG 968
Cdd:cd01795   81 DVSRARVPEEGFKGTALLG 99
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-419 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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 575.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYvlGDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668   79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668  159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668  239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313

                        330
                 ....*....|.
gi 966915356 409 CSRNAYMLVYR 419
Cdd:cd02668  314 SSRTAYMLVYK 324
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-418 1.31e-60

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 209.22  E-value: 1.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356   89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYvlgdgiQEEKDYEpqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDS------RYNKDIN---LLCALRDLFkALQKNSKSSSVSPKM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443  72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEkmegkklqlgiE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293

                         330       340       350
                  ....*....|....*....|....*....|.
gi 966915356  388 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 418
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 72-458 5.08e-47

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 182.76  E-value: 5.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356   72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdyvlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077   179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077   244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077   320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDI---EKMEGK 380
Cdd:COG5077   399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQE----KPNTAVQVPAFLQELVDRDNSKFEEWCIEMAE 456
Cdd:COG5077   478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550


                  ..
gi 966915356  457 MR 458
Cdd:COG5077   551 IH 552
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 873-968 1.76e-40

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 143.96  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 873 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 949
Cdd:cd01795    1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80

                         90
                 ....*....|....*....
gi 966915356 950 DVMQVCMPEEGFKGTGLLG 968
Cdd:cd01795   81 DVSRARVPEEGFKGTALLG 99
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 878-936 3.14e-05

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 43.02  E-value: 3.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 966915356   878 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCaTLGTLGVIPESVILL 936
Cdd:smart00213  12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 868-936 9.22e-04

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 38.69  E-value: 9.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915356  868 RSMRHRKVrgekALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDcATLGTLGVIPESVILL 936
Cdd:pfam00240   4 KTLDGKKI----TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-419 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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 575.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYvlGDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668   79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668  159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668  239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313

                        330
                 ....*....|.
gi 966915356 409 CSRNAYMLVYR 419
Cdd:cd02668  314 SSRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 88-419 3.72e-81

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: 266.43  E-value: 3.72e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdyvlgdgiqEEKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659    2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELN 242
Cdd:cd02659   70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 243 IQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILD 322
Cdd:cd02659  147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 323 MEPYVEH------------KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659  227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305

                        330       340       350
                 ....*....|....*....|....*....|..
gi 966915356 388 EDLAEPSKSQTRKPKCGkgthcsrNAYMLVYR 419
Cdd:cd02659  306 ETQKTYDSGPRAFKRTT-------NAYMLFYE 330
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-418 1.31e-60

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 209.22  E-value: 1.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356   89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYvlgdgiQEEKDYEpqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDS------RYNKDIN---LLCALRDLFkALQKNSKSSSVSPKM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443  72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEkmegkklqlgiE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293

                         330       340       350
                  ....*....|....*....|....*....|.
gi 966915356  388 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 418
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 90-419 2.50e-58

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: 200.79  E-value: 2.50e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdyvlgdgiqeekdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257    1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQ 244
Cdd:cd02257   21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 245 GHKQ----LTDCISEFLKEEKLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEI 320
Cdd:cd02257   93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 321 LDMEPYVEHKG-------GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgiEEDLAEP 393
Cdd:cd02257  171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEF 242

                        330       340
                 ....*....|....*....|....*.
gi 966915356 394 SKSqtrkpkcgkgthcSRNAYMLVYR 419
Cdd:cd02257  243 GSL-------------SSSAYILFYE 255
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 72-458 5.08e-47

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 182.76  E-value: 5.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356   72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdyvlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077   179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077   244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077   320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDI---EKMEGK 380
Cdd:COG5077   399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQE----KPNTAVQVPAFLQELVDRDNSKFEEWCIEMAE 456
Cdd:COG5077   478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550


                  ..
gi 966915356  457 MR 458
Cdd:COG5077   551 IH 552
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 178-419 8.34e-44

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: 158.60  E-value: 8.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 178 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674   21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 252 CISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFS-EILDMEPYV--E 328
Cdd:cd02674   89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 329 HKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 408
Cdd:cd02674  167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219

                        250
                 ....*....|.
gi 966915356 409 CSRNAYMLVYR 419
Cdd:cd02674  220 VSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 3.55e-43

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 159.36  E-value: 3.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVwflnleLRQALYLcpstcSDYVLGDGIQEEKDYE-PQTICEHLQYLFALLQNSnRRYIDPSGF 168
Cdd:cd02661    3 GLQNLGNTCFLNSVLQC------LTHTPPL-----ANYLLSREHSKDCCNEgFCMMCALEAHVERALASS-GPGSAPRIF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 169 VKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQQQFCGEYAYVTVCNQCGRESKLLSK 235
Cdd:cd02661   71 SSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 236 FYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYI 315
Cdd:cd02661  151 FLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQI 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966915356 316 GFSEILDMEPYV-EHKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPqSGEWYKFND 371
Cdd:cd02661  227 SFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 873-968 1.76e-40

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 143.96  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 873 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 949
Cdd:cd01795    1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80

                         90
                 ....*....|....*....
gi 966915356 950 DVMQVCMPEEGFKGTGLLG 968
Cdd:cd01795   81 DVSRARVPEEGFKGTALLG 99
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 2.72e-39

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: 148.79  E-value: 2.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdYVLGDGIQEekdyepQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-------LNLPRLGDS------QSVMKKLQLLQAHLMHTQRRAEAPpDYF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIqg 245
Cdd:cd02664   68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 246 hKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEP 325
Cdd:cd02664  134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 326 YVEHKGGSYV--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQSGE-------------------- 365
Cdd:cd02664  213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendeskn 292


                 ....*.
gi 966915356 366 WYKFND 371
Cdd:cd02664  293 WYLFND 298
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 8.87e-37

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 141.74  E-value: 8.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYVLGDGIQEEKDY--EPQTICEHLQYLFA-LLQNSNRRyidPS 166
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLR-----------NYFLSDRHSCTCLScsPNSCLSCAMDEIFQeFYYSGDRS---PY 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 167 GFVKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRES 230
Cdd:cd02660   68 GPINLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 231 KLLSKFYELELNIQGHKQ---------------LTDCISEFLKEEKLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQ 295
Cdd:cd02660  145 TTVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 296 LMRFVFDrQTGHKKKLNTYIGFSEILDMEPYV----------EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDpQSGE 365
Cdd:cd02660  224 LKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQ 300


                 ....*.
gi 966915356 366 WYKFND 371
Cdd:cd02660  301 WFKFDD 306
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-418 8.31e-35

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: 135.13  E-value: 8.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdyvlgdgiqeekdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:cd02663   49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663  129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 309 KKLNTYIGFSEIL------DMEPYVEHKggsyvYELSAVLIHRGVSAYSGHYIAHVKdpQSGEWYKFNDEDIEKMEGKKL 382
Cdd:cd02663  209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV 281

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 966915356 383 qlgieEDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 418
Cdd:cd02663  282 -----EEFFGDSPNQA-------------TAYVLFY 299
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-379 1.18e-34

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: 134.77  E-value: 1.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYvlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNY---NPARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 KALGL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQQQFCGEYAYVTVC-NQCGRESKLLSKF 236
Cdd:cd02657   70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVSTESE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 237 YELELNIqGHKQLTDCISEFLKEeKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIG 316
Cdd:cd02657  147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915356 317 FSEILDMEPYVEHKGgsyVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFND--------EDIEKMEG 379
Cdd:cd02657  225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 78-401 6.68e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 121.54  E-value: 6.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  78 PNCERRKK-NSFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSD--YVLGDGIQEEkdyEPQTICEHLQYLFal 154
Cdd:cd02671   13 TSCEKRENlLPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGlkHLVSLISSVE---QLQSSFLLNPEKY-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 155 lqNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCG-- 227
Cdd:cd02671   78 --NDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECEtf 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 228 --------------RESKLLSKFYELELNIQGH---KQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPC 290
Cdd:cd02671  144 terredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPE 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 291 TLNLQLMRF----VFDRQTGHKKKLNTYIGFSEILDMEPYVEhKGGSYVYELSAVLIHRGVSAYSGHYIAHVKdpqsgeW 366
Cdd:cd02671  224 VITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR------W 296

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 966915356 367 YKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 401
Cdd:cd02671  297 LLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-419 4.33e-29

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 117.87  E-value: 4.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTflqvwflnleLRQALYLCPstcsdyVLGDGIQEEkdyePQTicehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667    1 GLSNLGNTCFFNA----------VMQNLSQTP------ALRELLSET----PKE-------LFSQVCRKAPQFKG----- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELEL----NIQG 245
Cdd:cd02667   49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 246 HKQLTDCISEFLKEEKLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSEILDMEP 325
Cdd:cd02667  110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 326 Y------VEHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGEWYKFNDEDIEkme 378
Cdd:cd02667  186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR--- 261

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 966915356 379 gkklqlgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 419
Cdd:cd02667  262 --------EVSLEEVLKSE---------------AYLLFYE 279
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-372 5.69e-29

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 118.19  E-value: 5.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWF-------LNLELRQALYLCPS------TCSDYVLGDGIQEEKDYEPQTICEHlqylfallQ 156
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFsipsfqwRYDDLENKFPSDVVdpandlNCQLIKLADGLLSGRYSKPASLKSE--------N 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 157 NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQQQFCgeyayvtvCNQCG 227
Cdd:cd02658   73 DPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSCK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 228 RESKLLSKFYELELNIQGHKQ--------------LTDCISEFLKEEKLEgdnrYFCENCQSKQNATRKIRLLSLPCTLN 293
Cdd:cd02658  145 KVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 294 LQLMRFVFDrQTGHKKKLNTYIGFSEILDMEPYvehkggsyvyELSAVLIHRGVSAYSGHYIAHVK--DPQSGEWYKFND 371
Cdd:cd02658  221 INMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289


                 .
gi 966915356 372 E 372
Cdd:cd02658  290 E 290
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-376 8.51e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 89.73  E-value: 8.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdyvlgdgiqeekdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662    1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqqqFCGEYAYVTVCNQCGRESKL-LSKFYELELNIQGHKQ 248
Cdd:cd02662   33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 249 -----LTDCISEFLKEEKLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEILDm 323
Cdd:cd02662   93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915356 324 epyvehkggSYVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGE--------------WYKFNDEDIEK 376
Cdd:cd02662  160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
90-377 8.77e-20

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 90.63  E-value: 8.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDyVLGDGIQeeKDYEPQTICEHLqYLFALLQNSNRRYIDPSGfv 169
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELK-VLKNVIR--KPEPDLNQEEAL-KLFTALWSSKEHKVGWIP-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 170 kalglDTGQQQDAQEFSKLFMSLLEDTLSKQ--------KNPDVRNIVQQQFcgeyaYVTVCNQCGRESKLLSKFyelel 241
Cdd:COG5533   75 -----PMGSQEDAHELLGKLLDELKLDLVNSftirifktTKDKKKTSTGDWF-----DIIIELPDQTWVNNLKTL----- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 242 niqghKQLTDCISEFLKEEKL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNTYIGfsE 319
Cdd:COG5533  140 -----QEFIDNMEELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD--E 205

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915356 320 ILDMEPYVEHKGG---SYVYELSAVLIHRGvSAYSGHYIAHVKdpQSGEWYKFNDEDIEKM 377
Cdd:COG5533  206 KFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
89-371 1.19e-18

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 87.71  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356   89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpstcsdyvlgdgIQEEKDYEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH------------LATECLKEHCLLCE-LGFLFDMLEKAKGKNCQASNF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:pfam13423  68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  229 ESKLLSKFYELELN------IQGHKQLTDCISEFLKEE-KLEGDNRYFCENCQSKQNATRKIRLLSLPC--TLNLQLMRF 299
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNE 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915356  300 VFDRQTGHKKKLNTYIGfseiLDMEPYVEHKGGSYVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGEWYKFND 371
Cdd:pfam13423 228 EWRQLWKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
220-376 5.53e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 89.17  E-value: 5.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 220 VTVCNQCGRESKLLSKFYE-----LELNIQGHKQ---LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCT 291
Cdd:COG5560  640 DAVVISCEWEEKRYLSLFSydplwTIREIGAAERtitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 292 LNLQLMRFVFDRQTghKKKLNTYIGFS-EILDMEPYVEHKGGSYV-YELSAVLIHRGVSAySGHYIAHVKDPQSGEWYKF 369
Cdd:COG5560  720 LIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLF 796


                 ....*..
gi 966915356 370 NDEDIEK 376
Cdd:COG5560  797 DDSRITE 803
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 89-375 9.58e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 79.84  E-value: 9.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  89 VGLTNLGATCYVNTFLQVWFLNLELRQA--------LYLCPSTCSDYVLGDGIQEEKDYE-PQTICEHLQYLFALLQNSN 159
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnfdeskAELASDYPTERRIGGREVSRSELQrSNQFVYELRSLFNDLIHSN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 160 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQQQFCGEY----AYVTVCNQ 225
Cdd:cd02666   82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGNQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 226 CGRESK---LLSKFYEL-----ELNIQGHKQ-LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKI---------RLLS 287
Cdd:cd02666  159 PSVRTKterFLSLLVDVgkkgrEIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 288 LPCTLNLQLMRFVFDRQTGHKKKLNTYIGfseilDMEPYVEHKGgSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWY 367
Cdd:cd02666  239 DIDELIREAIQSESSLVRQAQNELAELKH-----EIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVWR 311


                 ....*...
gi 966915356 368 KFNDEDIE 375
Cdd:cd02666  312 KYNDETVT 319
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 178-418 5.99e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 72.21  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnivqQQFCGEYAYVTVcnqcgRESKLLSK---FYELELNIQ 244
Cdd:cd02665   21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGV-----LEGKPFCNcetFGQYPLQVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 245 GHKQLTDCISEFLKEEKLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSEILDME 324
Cdd:cd02665   91 GYGNLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 325 PYvehkggsyvyELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcG 404
Cdd:cd02665  163 PY----------ELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------S 213

                        250
                 ....*....|....
gi 966915356 405 KGTHCSRNAYMLVY 418
Cdd:cd02665  214 FGGGRNPSAYCLMY 227
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 86-378 7.01e-11

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: 65.42  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  86 NSFVGLTNLGATCYVNTFLQvwflnlelrqALYLCPSTCSDYVLGDGIQEEKDYEPQTIcEHLQYLFALLQNSN--RRYI 163
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQ----------ALSHVKPIRNFFLLYENYENIKDRKSELV-KRLSELIRKIWNPRnfKGHV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 164 DPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNIVQQQFCGEY-----AYVTVCNQCGRESKLL 233
Cdd:cd02669  186 SPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKVqietqKIKPHAEEEGSKDKFF 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 234 ----------SKFYELELNIQG-----HKQLTDCISEFLKEEKLegdNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMR 298
Cdd:cd02669  266 kdsrvkktsvSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKR 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 299 FvfDRQTGHKKKLNTYIGFS-EILDMEPYVE---HKGGSYV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDED 373
Cdd:cd02669  343 F--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLN 420


                 ....*
gi 966915356 374 IEKME 378
Cdd:cd02669  421 VKEVL 425
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 173-374 3.07e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 61.78  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQQQFCGEYAYVT----VCNQCGRESKLLSKFYELELNIQG 245
Cdd:cd02673   27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 246 HK--QLTDCISEFLKEEKLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfseildM 323
Cdd:cd02673  107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966915356 324 EPYvEHKGGSYvyELSAVLIHRGVSAYSGHYIAHVKDPQSG-EWYKFNDEDI 374
Cdd:cd02673  175 KKY-CGTDAKY--SLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 75-371 1.72e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 50.59  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdyvlgdgIQEEKDYEPQTICEhLQYLFAL 154
Cdd:cd02672    2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFST 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 155 LqnsnrryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqqqfcgeyayvtvcNQCGRESKLLS 234
Cdd:cd02672   68 L--------------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVS 99

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 235 KFYELELNIQGHKQLTD-----CISEFLKEEKlegDNRYFCENCQSKQNATRKIRLLSLPCTLNLQL---MRFV------ 300
Cdd:cd02672  100 LLYTLSLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefdd 176

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915356 301 FDRQTGHKKKLNTYIGFSEILDMEPYVEHKG-GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQS----GEWYKFND 371
Cdd:cd02672  177 INVVLPSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 883-936 3.81e-06

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 45.28  E-value: 3.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966915356 883 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCaTLGTLGVIPESVILL 936
Cdd:cd17039   15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 878-936 3.14e-05

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 43.02  E-value: 3.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 966915356   878 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDCaTLGTLGVIPESVILL 936
Cdd:smart00213  12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
90-243 4.54e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 47.57  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356  90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYVLGDGIQEEKDYE-PQTICEHLQYLFA-LLQ---NSNRRYID 164
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELR-----------DYFLSDEYEESINEEnPLGMHGSVASAYAdLIKqlyDGNLHAFT 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915356 165 PSGFVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSK--QK----NPDV-----------------------RNIVQ 210
Cdd:COG5560  336 PSGFKKTIGsfneeFSGYDQQDSQEFIAFLLDGLHEDLNRiiKKpytsKPDLspgddvvvkkkakecwwehlkrnDSIIT 415

                        170       180       190
                 ....*....|....*....|....*....|...
gi 966915356 211 QQFCGEYAYVTVCNQCGRESKLLSKFYELELNI 243
Cdd:COG5560  416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 868-936 9.22e-04

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 38.69  E-value: 9.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915356  868 RSMRHRKVrgekALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILSDDcATLGTLGVIPESVILL 936
Cdd:pfam00240   4 KTLDGKKI----TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
Ubl_AtNPL4_like cd17055
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ...
 865-928 3.26e-03

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.


Pssm-ID: 340575  Cd Length: 73  Bit Score: 37.19  E-value: 3.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915356 865 VIRrsMRHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILSDDCATLGTLGV 928
Cdd:cd17055    2 LLR--VRSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
 
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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