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Conserved domains on  [gi|1060099231|ref|NP_001317323|]
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ubiquitin carboxyl-terminal hydrolase 48 isoform c [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119314)

ubiquitin carboxyl-terminal hydrolase family protein may remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds

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: 576.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL--KNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668    79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668   159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668   239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313

                         330
                  ....*....|.
gi 1060099231 409 CSRNAYMLVYR 419
Cdd:cd02668   314 SSRTAYMLVYK 324
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 909-982 1.60e-29

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: 112.76  E-value: 1.60e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099231 909 QIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD--DVMQVCMPEEGFKGTGLLG 982
Cdd:cd01795    24 QIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADeaDVSRARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 484-554 1.31e-09

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


:

Pssm-ID: 399383  Cd Length: 80  Bit Score: 55.45  E-value: 1.31e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099231 484 EPYEFVSLEWLQKWL----DESTPTKPIDNH--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 554
Cdd:pfam06337   2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
 
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: 576.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL--KNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668    79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668   159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668   239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313

                         330
                  ....*....|.
gi 1060099231 409 CSRNAYMLVYR 419
Cdd:cd02668   314 SSRTAYMLVYK 324
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-418 6.77e-61

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 209.99  E-value: 6.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMLGDGIQeekdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443  72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEkmegkklqlgiE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1060099231 388 EDLAEPSKSQtrkpkcgkgthcsrNAYMLVY 418
Cdd:pfam00443 294 VDEETAVLSS--------------SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 72-458 2.76e-46

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 180.84  E-value: 2.76e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231   72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdymlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077    179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077    244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077    320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDI---EKMEGK 380
Cdd:COG5077    399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQE----KPNTTVQVPAFLQELVDRDNSKFEEWCIEMAE 456
Cdd:COG5077    478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550


                   ..
gi 1060099231  457 MR 458
Cdd:COG5077    551 IH 552
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 909-982 1.60e-29

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: 112.76  E-value: 1.60e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099231 909 QIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD--DVMQVCMPEEGFKGTGLLG 982
Cdd:cd01795    24 QIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADeaDVSRARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 484-554 1.31e-09

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


Pssm-ID: 399383  Cd Length: 80  Bit Score: 55.45  E-value: 1.31e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099231 484 EPYEFVSLEWLQKWL----DESTPTKPIDNH--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 554
Cdd:pfam06337   2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
DUSP smart00695
Domain in ubiquitin-specific proteases;
483-556 9.52e-06

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 44.66  E-value: 9.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  483 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNHACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 552
Cdd:smart00695   5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84


                   ....
gi 1060099231  553 LCKE 556
Cdd:smart00695  85 VCQG 88
 
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: 576.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgDGIQEEKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAEL--KNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQGHKQL 249
Cdd:cd02668    79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 250 TDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEPY-VE 328
Cdd:cd02668   159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 329 HKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTH 408
Cdd:cd02668   239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTH 313

                         330
                  ....*....|.
gi 1060099231 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 5.48e-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: 266.05  E-value: 5.48e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdymlgdgiqEEKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659     2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELN 242
Cdd:cd02659    70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 243 IQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILD 322
Cdd:cd02659   147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 323 MEPYVEH------------KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659   227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1060099231 388 EDLAEPSKSQTRKPKCGkgthcsrNAYMLVYR 419
Cdd:cd02659   306 ETQKTYDSGPRAFKRTT-------NAYMLFYE 330
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-418 6.77e-61

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 209.99  E-value: 6.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMLGDGIQeekdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYE 238
Cdd:pfam00443  72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 239 LELNIQGHK------QLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443 148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 313 TYIGFSEILDMEPYV-----EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEkmegkklqlgiE 387
Cdd:pfam00443 226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------E 293

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1060099231 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 3.71e-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: 200.40  E-value: 3.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdymlgdgiqeekdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257     1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIQ 244
Cdd:cd02257    21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 245 GHKQ----LTDCISEFLKEEKLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEI 320
Cdd:cd02257    93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 321 LDMEPYVEHKG-------GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgiEEDLAEP 393
Cdd:cd02257   171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEF 242

                         330       340
                  ....*....|....*....|....*.
gi 1060099231 394 SKSqtrkpkcgkgthcSRNAYMLVYR 419
Cdd:cd02257   243 GSL-------------SSSAYILFYE 255
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 72-458 2.76e-46

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 180.84  E-value: 2.76e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231   72 FHNIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYlcpstcsdymlgdGIQEEKDYEPQTICEHLQYL 151
Cdd:COG5077    179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-------------GIPTDHPRGRDSVALALQRL 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077    244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077    320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  309 KKLNTYIGFSEILDMEPYVEH-----KGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDI---EKMEGK 380
Cdd:COG5077    399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVL 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  381 KLQLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTQE----KPNTTVQVPAFLQELVDRDNSKFEEWCIEMAE 456
Cdd:COG5077    478 EENFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLddllNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDE 550


                   ..
gi 1060099231  457 MR 458
Cdd:COG5077    551 IH 552
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 3.92e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 162.06  E-value: 3.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVwflnleLRQALYLcpstcSDYMLGDGIQEEKDYE-PQTICEHLQYLFALLQNSnRRYIDPSGF 168
Cdd:cd02661     3 GLQNLGNTCFLNSVLQC------LTHTPPL-----ANYLLSREHSKDCCNEgFCMMCALEAHVERALASS-GPGSAPRIF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 169 VKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQQQFCGEYAYVTVCNQCGRESKLLSK 235
Cdd:cd02661    71 SSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 236 FYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYI 315
Cdd:cd02661   151 FLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQI 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060099231 316 GFSEILDMEPYV-EHKGGSYVYELSAVLIHRGVSAYSGHYIAHVKDPqSGEWYKFND 371
Cdd:cd02661   227 SFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 178-419 1.64e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 157.83  E-value: 1.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 178 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674    21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 252 CISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGhkKKLNTYIGFS-EILDMEPYV--E 328
Cdd:cd02674    89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVdtR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 329 HKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 408
Cdd:cd02674   167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219

                         250
                  ....*....|.
gi 1060099231 409 CSRNAYMLVYR 419
Cdd:cd02674   220 VSSSAYILFYE 230
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 9.25e-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: 147.25  E-value: 9.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcsdymLGDGIQEEKDyePQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQV-----------LSLNLPRLGD--SQSVMKKLQLLQAHLMHTQRRAEAPpDYF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQQQFCGEYAYVTVCNQCGRESKLLSKFYELELNIqg 245
Cdd:cd02664    68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 246 hKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSEILDMEP 325
Cdd:cd02664   134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 326 YVEHKGGSYV--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQSGE-------------------- 365
Cdd:cd02664   213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendeskn 292


                  ....*.
gi 1060099231 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 3.24e-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: 142.90  E-value: 3.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYMLGDGIQEEKDY--EPQTICEHLQYLFA-LLQNSNRRyidPS 166
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLR-----------NYFLSDRHSCTCLScsPNSCLSCAMDEIFQeFYYSGDRS---PY 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 167 GFVKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQQQFCGEYAYVTVCNQCGRES 230
Cdd:cd02660    68 GPINLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 231 KLLSKFYELELNIQGHKQ---------------LTDCISEFLKEEKLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQ 295
Cdd:cd02660   145 TTVDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 296 LMRFVFDrQTGHKKKLNTYIGFSEILDMEPYV----------EHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKDpQSGE 365
Cdd:cd02660   224 LKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQ 300


                  ....*.
gi 1060099231 366 WYKFND 371
Cdd:cd02660   301 WFKFDD 306
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-379 5.78e-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 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: 135.54  E-value: 5.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYMlgdGIQEEKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 KALGL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQQQFCGEYAYVTVC-NQCGRESKLLSKF 236
Cdd:cd02657    70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVSTESE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 237 YELELNIqGHKQLTDCISEFLKEeKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIG 316
Cdd:cd02657   147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060099231 317 FSEILDMEPYVEHKGgsyVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFND--------EDIEKMEG 379
Cdd:cd02657   225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-418 8.55e-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: 8.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdymlgdgiqeekdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:cd02663    49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 229 ESKLLSKFYELELNIQGHKQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663   129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 309 KKLNTYIGFSEIL------DMEPYVEHKggsyvYELSAVLIHRGVSAYSGHYIAHVKdpQSGEWYKFNDEDIEKMEGKKL 382
Cdd:cd02663   209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV 281

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1060099231 383 qlgieEDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 418
Cdd:cd02663   282 -----EEFFGDSPNQA-------------TAYVLFY 299
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 78-401 8.00e-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: 8.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  78 PNCERRKK-NSFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSD--YMLGDGIQEEkdyEPQTICEHLQYLFal 154
Cdd:cd02671    13 TSCEKRENlLPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGlkHLVSLISSVE---QLQSSFLLNPEKY-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 155 lqNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCG-- 227
Cdd:cd02671    78 --NDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECEtf 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 228 --------------RESKLLSKFYELELNIQGH---KQLTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPC 290
Cdd:cd02671   144 terredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 291 TLNLQLMRF----VFDRQTGHKKKLNTYIGFSEILDMEPYVEhKGGSYVYELSAVLIHRGVSAYSGHYIAHVKdpqsgeW 366
Cdd:cd02671   224 VITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR------W 296

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1060099231 367 YKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 401
Cdd:cd02671   297 LLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 909-982 1.60e-29

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: 112.76  E-value: 1.60e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099231 909 QIMHAFSVAPFDQNLSIDGKILSDDCATLGTLGVIPESVILLKADEPIADYAAMD--DVMQVCMPEEGFKGTGLLG 982
Cdd:cd01795    24 QIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADeaDVSRARVPEEGFKGTALLG 99
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-419 3.57e-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: 3.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTflqvwflnleLRQALYLCPstcsdyMLGDGIQEEkdyePQTicehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667     1 GLSNLGNTCFFNA----------VMQNLSQTP------ALRELLSET----PKE-------LFSQVCRKAPQFKG----- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNIVQQQFCGEYAYVTVCNQCGRESKLLSKFYELEL----NIQG 245
Cdd:cd02667    49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 246 HKQLTDCISEFLKEEKLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSEILDMEP 325
Cdd:cd02667   110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 326 Y------VEHKGGSYVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGEWYKFNDEDIEkme 378
Cdd:cd02667   186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR--- 261

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1060099231 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 3.64e-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: 118.96  E-value: 3.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWF-------LNLELRQALYLCPS------TCSDYMLGDGIQEEKDYEPQTICEHlqylfallQ 156
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFsipsfqwRYDDLENKFPSDVVdpandlNCQLIKLADGLLSGRYSKPASLKSE--------N 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 157 NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQQQFCgeyayvtvCNQCG 227
Cdd:cd02658    73 DPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSCK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 228 RESKLLSKFYELELNIQGHKQ--------------LTDCISEFLKEEKLEgdnrYFCENCQSKQNATRKIRLLSLPCTLN 293
Cdd:cd02658   145 KVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 294 LQLMRFVFDrQTGHKKKLNTYIGFSEILDMEPYvehkggsyvyELSAVLIHRGVSAYSGHYIAHVK--DPQSGEWYKFND 371
Cdd:cd02658   221 INMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289


                  .
gi 1060099231 372 E 372
Cdd:cd02658   290 E 290
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
90-377 6.86e-20

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 91.02  E-value: 6.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYMlgdgIQE-EKDYEPQTICEHLqYLFALLQNSNRRYIDPSGf 168
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVL----KNViRKPEPDLNQEEAL-KLFTALWSSKEHKVGWIP- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 169 vkalglDTGQQQDAQEFSKLFMSLLEDTLSKQ--------KNPDVRNIVQQQFcgeyaYVTVCNQCGRESKLLSKFyele 240
Cdd:COG5533    75 ------PMGSQEDAHELLGKLLDELKLDLVNSftirifktTKDKKKTSTGDWF-----DIIIELPDQTWVNNLKTL---- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 241 lniqghKQLTDCISEFLKEEKL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNTYIGfs 318
Cdd:COG5533   140 ------QEFIDNMEELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060099231 319 EILDMEPYVEHKGG---SYVYELSAVLIHRGvSAYSGHYIAHVKdpQSGEWYKFNDEDIEKM 377
Cdd:COG5533   205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-376 9.98e-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: 89.35  E-value: 9.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdymlgdgiqeekdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662     1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqqqFCGEYAYVTVCNQCGRESKL-LSKFYELELNIQGHKQ 248
Cdd:cd02662    33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 249 -----LTDCISEFLKEEKLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSEILDm 323
Cdd:cd02662    93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060099231 324 epyvehkggSYVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGE--------------WYKFNDEDIEK 376
Cdd:cd02662   160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
89-371 1.20e-18

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 87.71  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpstcsdymlgdgIQEEKDYEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH------------LATECLKEHCLLCE-LGFLFDMLEKAKGKNCQASNF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQQQFCGEYAYVTVCNQCGR 228
Cdd:pfam13423  68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 229 ESKLLSKFYELELN------IQGHKQLTDCISEFLKEE-KLEGDNRYFCENCQSKQNATRKIRLLSLPC--TLNLQLMRF 299
Cdd:pfam13423 148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNE 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099231 300 VFDRQTGHKKKLNTYIGfseiLDMEPYVEHKGGSYVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGEWYKFND 371
Cdd:pfam13423 228 EWRQLWKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
220-376 8.40e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 88.79  E-value: 8.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 220 VTVCNQCGRESKLLSKFYE-----LELNIQGHKQ---LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKIRLLSLPCT 291
Cdd:COG5560   640 DAVVISCEWEEKRYLSLFSydplwTIREIGAAERtitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 292 LNLQLMRFVFDRQTghKKKLNTYIGFS-EILDMEPYVEHKGGSYV-YELSAVLIHRGVSAySGHYIAHVKDPQSGEWYKF 369
Cdd:COG5560   720 LIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLF 796


                  ....*..
gi 1060099231 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 6.06e-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: 80.23  E-value: 6.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  89 VGLTNLGATCYVNTFLQVWFLNLELRQA--------LYLCPSTCSDYMLGDGIQEEKDYE-PQTICEHLQYLFALLQNSN 159
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnfdeskAELASDYPTERRIGGREVSRSELQrSNQFVYELRSLFNDLIHSN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 160 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQQQFCGEY----AYVTVCNQ 225
Cdd:cd02666    82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGNQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 226 CGRESK---LLSKFYEL-----ELNIQGHKQ-LTDCISEFLKEEKLEGDNRYFCENCQSKQNATRKI---------RLLS 287
Cdd:cd02666   159 PSVRTKterFLSLLVDVgkkgrEIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 288 LPCTLNLQLMRFVFDRQTGHKKKLNTYIGfseilDMEPYVEHKGgSYVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWY 367
Cdd:cd02666   239 DIDELIREAIQSESSLVRQAQNELAELKH-----EIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVWR 311


                  ....*...
gi 1060099231 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 6.95e-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: 6.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnivqQQFCGEYAYVTVcnqcgRESKLLSK---FYELELNIQ 244
Cdd:cd02665    21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGV-----LEGKPFCNcetFGQYPLQVN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 245 GHKQLTDCISEFLKEEKLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSEILDME 324
Cdd:cd02665    91 GYGNLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 325 PYvehkggsyvyELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcG 404
Cdd:cd02665   163 PY----------ELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------S 213

                         250
                  ....*....|....
gi 1060099231 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 5.12e-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: 66.19  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  86 NSFVGLTNLGATCYVNTFLQvwflnlelrqALYLCPSTCSDYMLGDGIQEEKDYEPQTIcEHLQYLFALLQNSN--RRYI 163
Cdd:cd02669   117 PGFVGLNNIKNNDYANVIIQ----------ALSHVKPIRNFFLLYENYENIKDRKSELV-KRLSELIRKIWNPRnfKGHV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 164 DPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNIVQQQFCGEY-----AYVTVCNQCGRESKLL 233
Cdd:cd02669   186 SPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKVqietqKIKPHAEEEGSKDKFF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 234 ----------SKFYELELNIQG-----HKQLTDCISEFLKEEKLegdNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMR 298
Cdd:cd02669   266 kdsrvkktsvSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKR 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 299 FvfDRQTGHKKKLNTYIGFS-EILDMEPYVE---HKGGSYV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDED 373
Cdd:cd02669   343 F--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLN 420


                  ....*
gi 1060099231 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 3.93e-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: 61.39  E-value: 3.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQQQFCGEYAYVT----VCNQCGRESKLLSKFYELELNIQG 245
Cdd:cd02673    27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 246 HK--QLTDCISEFLKEEKLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfseildM 323
Cdd:cd02673   107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1060099231 324 EPYvEHKGGSYvyELSAVLIHRGVSAYSGHYIAHVKDPQSG-EWYKFNDEDI 374
Cdd:cd02673   175 KKY-CGTDAKY--SLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 484-554 1.31e-09

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


Pssm-ID: 399383  Cd Length: 80  Bit Score: 55.45  E-value: 1.31e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099231 484 EPYEFVSLEWLQKWL----DESTPTKPIDNH--ACLCSHDKLHPDKISIMK--RISEYAADIFYSRYGGGPRLTVKALC 554
Cdd:pfam06337   2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 75-371 2.17e-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: 50.20  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdymlgdgIQEEKDYEPQTICEhLQYLFAL 154
Cdd:cd02672     2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFST 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 155 LqnsnrryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqqqfcgeyayvtvcNQCGRESKLLS 234
Cdd:cd02672    68 L--------------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVS 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 235 KFYELELNIQGHKQLTD-----CISEFLKEEKlegDNRYFCENCQSKQNATRKIRLLSLPCTLNLQL---MRFV------ 300
Cdd:cd02672   100 LLYTLSLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefdd 176

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099231 301 FDRQTGHKKKLNTYIGFSEILDMEPYVEHKG-GSYVYELSAVLIHRGVSAYSGHYIAHVKDPQS----GEWYKFND 371
Cdd:cd02672   177 INVVLPSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
DUSP smart00695
Domain in ubiquitin-specific proteases;
483-556 9.52e-06

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 44.66  E-value: 9.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  483 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNHACLCSHD--KLHPDKI--SIMKRISEYAADIFYSRYGGGPR-LTVKA 552
Cdd:smart00695   5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84


                   ....
gi 1060099231  553 LCKE 556
Cdd:smart00695  85 VCQG 88
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
90-243 5.03e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 47.19  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231  90 GLTNLGATCYVNTFLQVWFLNLELRqalylcpstcsDYMLGDGIQEEKDYE-PQTICEHLQYLFA-LLQ---NSNRRYID 164
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWELR-----------DYFLSDEYEESINEEnPLGMHGSVASAYAdLIKqlyDGNLHAFT 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099231 165 PSGFVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSK------QKNPDV-----------------------RNIVQ 210
Cdd:COG5560   336 PSGFKKTIGsfneeFSGYDQQDSQEFIAFLLDGLHEDLNRiikkpyTSKPDLspgddvvvkkkakecwwehlkrnDSIIT 415

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1060099231 211 QQFCGEYAYVTVCNQCGRESKLLSKFYELELNI 243
Cdd:COG5560   416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
 
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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