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Conserved domains on  [gi|75571442|sp|Q5ZM45|]
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RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48; AltName: Full=Deubiquitinating enzyme 48; AltName: Full=Ubiquitin thioesterase 48; AltName: Full=Ubiquitin-specific-processing protease 48

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 ...
90-417 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: 583.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCSSNEHAAGESIPKDKDYEPQTICEHLQYLFALLQNSKRRYIDPSGFVKA 169
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  170 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 249
Cdd:cd02668   81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 328
Cdd:cd02668  161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  329 NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 408
Cdd:cd02668  241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315

                 ....*....
gi 75571442  409 RNAYMLVYR 417
Cdd:cd02668  316 RTAYMLVYK 324
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
937-1032 3.39e-41

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: 146.28  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  937 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTATLGSLGIIPESVILLKADEPIADYAAMD-- 1013
Cdd:cd01795    1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
                         90
                 ....*....|....*....
gi 75571442 1014 DVMQVCMPEEGFKGTGLLG 1032
Cdd:cd01795   81 DVSRARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
481-552 1.27e-13

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: 67.01  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    481 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKICIMK--RISEYVADFFYRRYGGGPRLNVKALC 552
Cdd:pfam06337    1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-417 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: 583.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCSSNEHAAGESIPKDKDYEPQTICEHLQYLFALLQNSKRRYIDPSGFVKA 169
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  170 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 249
Cdd:cd02668   81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 328
Cdd:cd02668  161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  329 NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 408
Cdd:cd02668  241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315

                 ....*....
gi 75571442  409 RNAYMLVYR 417
Cdd:cd02668  316 RTAYMLVYK 324
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-416 3.24e-61

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 211.53  E-value: 3.24e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442     89 VGLTNLGATCYVNTFLQMWFLNLELRQALYlcssNEHAAGESIPKDKDYEpqtICEHLQYLF-ALLQNSKRRYIDPSGFV 167
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDIN---LLCALRDLFkALQKNSKSSSVSPKMFK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    168 KALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELE 238
Cdd:pfam00443   74 KSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    239 LNIQGHK------QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTY 312
Cdd:pfam00443  150 LPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTE 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    313 IGFSELLDMEPFM-----EQKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEkmegkklqlgiEED 387
Cdd:pfam00443  228 VEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------EVD 295
                          330       340
                   ....*....|....*....|....*....
gi 75571442    388 LAEPSKSQtrkpkcgkgthcsrNAYMLVY 416
Cdd:pfam00443  296 EETAVLSS--------------SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
72-455 2.36e-47

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 184.30  E-value: 2.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   72 FHNIDDPNceRRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYlcssnehaageSIPKDKDYEPQTICEHLQYLFA 151
Cdd:COG5077  179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-----------GIPTDHPRGRDSVALALQRLFY 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  152 LLQNSkRRYIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:COG5077  246 NLQTG-EEPVDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNYES 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  229 KLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKK 308
Cdd:COG5077  322 ARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVK 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  309 LNTYIGFSELLDMEPFMEQ-----KNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDI---EKMEGKKL 380
Cdd:COG5077  401 INDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVLEE 479
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  381 QLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTREKSL-----TVEVPAFLQELVERDNCKFEEWCNEMAEMR 455
Cdd:COG5077  480 NFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLDDLlnpvaAVDIPPHVEEVLSEEIDKTEVRCKEIDEIH 552
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
937-1032 3.39e-41

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: 146.28  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  937 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTATLGSLGIIPESVILLKADEPIADYAAMD-- 1013
Cdd:cd01795    1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
                         90
                 ....*....|....*....
gi 75571442 1014 DVMQVCMPEEGFKGTGLLG 1032
Cdd:cd01795   81 DVSRARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
481-552 1.27e-13

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: 67.01  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    481 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKICIMK--RISEYVADFFYRRYGGGPRLNVKALC 552
Cdd:pfam06337    1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
DUSP smart00695
Domain in ubiquitin-specific proteases;
477-554 1.88e-10

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 58.14  E-value: 1.88e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442     477 PAEAGSPYDFISLEWLQKWLD-----ESTPPKPIDNTACLCSHG--KLHPDKI--CIMKRISEYVADFFYRRYGGGPR-L 546
Cdd:smart00695    1 PLEEGLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpI 80

                    ....*...
gi 75571442     547 NVKALCKD 554
Cdd:smart00695   81 PRKVVCQG 88
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
942-1000 1.97e-06

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: 46.48  E-value: 1.97e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 75571442     942 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTaTLGSLGIIPESVILL 1000
Cdd:smart00213   12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
947-1000 5.44e-05

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: 42.16  E-value: 5.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 75571442    947 VSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTaTLGSLGIIPESVILL 1000
Cdd:pfam00240   15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTIHL 67
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-417 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: 583.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFLNLELRQALYLCSSNEHAAGESIPKDKDYEPQTICEHLQYLFALLQNSKRRYIDPSGFVKA 169
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  170 LGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTD 249
Cdd:cd02668   81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPF-MEQK 328
Cdd:cd02668  161 CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAESD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  329 NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPsksqtRKPKCGKGTHCS 408
Cdd:cd02668  241 EGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKP-----RKSEIKKGTHSS 315

                 ....*....
gi 75571442  409 RNAYMLVYR 417
Cdd:cd02668  316 RTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
88-417 3.27e-80

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: 264.89  E-value: 3.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   88 FVGLTNLGATCYVNTFLQMWFLNLELRQALYlcssnehaageSIP--KDKDYEPQTICeHLQYLFALLQNSKRRYIDPSG 165
Cdd:cd02659    2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVY-----------SIPptEDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  166 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELN 240
Cdd:cd02659   70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  241 IQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLD 320
Cdd:cd02659  147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  321 MEPFMEQ------------KNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKM---EGKKLQLGIE 385
Cdd:cd02659  227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305
                        330       340       350
                 ....*....|....*....|....*....|..
gi 75571442  386 EDLAEPSKSQTRKPKCGkgthcsrNAYMLVYR 417
Cdd:cd02659  306 ETQKTYDSGPRAFKRTT-------NAYMLFYE 330
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-416 3.24e-61

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 211.53  E-value: 3.24e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442     89 VGLTNLGATCYVNTFLQMWFLNLELRQALYlcssNEHAAGESIPKDKDYEpqtICEHLQYLF-ALLQNSKRRYIDPSGFV 167
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDIN---LLCALRDLFkALQKNSKSSSVSPKMFK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    168 KALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELE 238
Cdd:pfam00443   74 KSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    239 LNIQGHK------QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTY 312
Cdd:pfam00443  150 LPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTE 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    313 IGFSELLDMEPFM-----EQKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEkmegkklqlgiEED 387
Cdd:pfam00443  228 VEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVT-----------EVD 295
                          330       340
                   ....*....|....*....|....*....
gi 75571442    388 LAEPSKSQtrkpkcgkgthcsrNAYMLVY 416
Cdd:pfam00443  296 EETAVLSS--------------SAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
90-417 1.01e-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: 202.33  E-value: 1.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNtflqmwflnlelrqalylcssnehaageSIpkdkdyepqticehLQYLFAllqnskrryidpsgfvka 169
Cdd:cd02257    1 GLNNLGNTCYLN----------------------------SV--------------LQALFS------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  170 lgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGH 244
Cdd:cd02257   21 ------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVK 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  245 KQ----LTDCITEFLKEEKLEGDNRYFCEtCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSELLD 320
Cdd:cd02257   95 GLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELD 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  321 MEPFMEQK-------NGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEgkklqlgiEEDLAEPSK 393
Cdd:cd02257  173 LSPYLSEGekdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVLEFGS 244
                        330       340
                 ....*....|....*....|....
gi 75571442  394 SqtrkpkcgkgthcSRNAYMLVYR 417
Cdd:cd02257  245 L-------------SSSAYILFYE 255
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
72-455 2.36e-47

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 184.30  E-value: 2.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   72 FHNIDDPNceRRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYlcssnehaageSIPKDKDYEPQTICEHLQYLFA 151
Cdd:COG5077  179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY-----------GIPTDHPRGRDSVALALQRLFY 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  152 LLQNSkRRYIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:COG5077  246 NLQTG-EEPVDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNYES 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  229 KLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKK 308
Cdd:COG5077  322 ARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVK 400
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  309 LNTYIGFSELLDMEPFMEQ-----KNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDI---EKMEGKKL 380
Cdd:COG5077  401 INDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVtraTEKEVLEE 479
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  381 QLGIEEDLAEPSKSQTRKPKcgkgthcSRNAYMLVYRLQTREKSL-----TVEVPAFLQELVERDNCKFEEWCNEMAEMR 455
Cdd:COG5077  480 NFGGDHPYKDKIRDHSGIKR-------FMSAYMLVYLRKSMLDDLlnpvaAVDIPPHVEEVLSEEIDKTEVRCKEIDEIH 552
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
176-417 1.89e-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: 1.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  176 QQQDAQEFsklfMSLLEDTLskqknpdvRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNI-----QGHKQ-LTD 249
Cdd:cd02674   21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  250 CITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFS-ELLDMEPFM--E 326
Cdd:cd02674   89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  327 QKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEgkklqlgieedlaepsksqtrkpkcgKGTH 406
Cdd:cd02674  167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS--------------------------ESSV 219
                        250
                 ....*....|.
gi 75571442  407 CSRNAYMLVYR 417
Cdd:cd02674  220 VSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-369 8.61e-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: 158.59  E-value: 8.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQ--MWFLNLelrqALYLCSSNEHAAGesipkdKDYEPQTICEHLQYLFALLQNSkRRYIDPSGFV 167
Cdd:cd02661    3 GLQNLGNTCFLNSVLQclTHTPPL----ANYLLSREHSKDC------CNEGFCMMCALEAHVERALASS-GPGSAPRIFS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  168 KAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NIVQKQFCGEYAYVTVCNQCGRESKLVSKF 234
Cdd:cd02661   72 SNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTYDPF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  235 YELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNTYIG 314
Cdd:cd02661  152 LDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQIS 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 75571442  315 FSELLDMEPFMEQKNGV-YVYELSAVLIHRGVSAYSGHYIAHVKDPqTGEWYKFND 369
Cdd:cd02661  228 FPETLDLSPYMSQPNDGpLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDD 282
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
937-1032 3.39e-41

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: 146.28  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  937 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTATLGSLGIIPESVILLKADEPIADYAAMD-- 1013
Cdd:cd01795    1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80
                         90
                 ....*....|....*....
gi 75571442 1014 DVMQVCMPEEGFKGTGLLG 1032
Cdd:cd01795   81 DVSRARVPEEGFKGTALLG 99
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-369 1.40e-38

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 146.87  E-value: 1.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFLNLELRQALyLCSSNEHAAGESIPKDKdyepqticehLQYLFALLQNSKRRYIDP-SGFVK 168
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQV-LSLNLPRLGDSQSVMKK----------LQLLQAHLMHTQRRAEAPpDYFLE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  169 AL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrniVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIqghK 245
Cdd:cd02664   70 ASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF---P 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  246 QLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKL---------------- 309
Cdd:cd02664  135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKImdnvsinevlslpvrv 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  310 -NTYIGFSELLDMEPFMEQKNGVYV---YELSAVLIHRGVSAYSGHYIAHVKDPQTGE--------------------WY 365
Cdd:cd02664  215 eSKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendesknWY 294

                 ....
gi 75571442  366 KFND 369
Cdd:cd02664  295 LFND 298
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-416 3.43e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 142.06  E-value: 3.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQmwflnlelrqALYlcssnehaagesipkdkdYEpqTICEHLQYLFALLQNSKRRY--IDPSGFV 167
Cdd:cd02663    1 GLENFGNTCYCNSVLQ----------ALY------------------FE--NLLTCLKDLFESISEQKKRTgvISPKKFI 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  168 KALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:cd02663   51 TRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCETVS 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  229 KLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKK 308
Cdd:cd02663  131 SRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIK 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  309 LNTYIGFSelLDMEPFMEQKNGVYV---YELSAVLIHRGVSAYSGHYIAHVKdpQTGEWYKFNDEDIEKMEGKKLqlgie 385
Cdd:cd02663  211 LFYRVVFP--LELRLFNTTDDAENPdrlYELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAV----- 281
                        330       340       350
                 ....*....|....*....|....*....|.
gi 75571442  386 EDLAEPSKSQTrkpkcgkgthcsrNAYMLVY 416
Cdd:cd02663  282 EEFFGDSPNQA-------------TAYVLFY 299
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-369 4.44e-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: 142.51  E-value: 4.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMwFLNLELRQALYLcsSNEHAAGESIPKdkdyEPQTICEHLQYLFA-LLQNSKRRyidPSGFVK 168
Cdd:cd02660    2 GLINLGATCFMNVILQA-LLHNPLLRNYFL--SDRHSCTCLSCS----PNSCLSCAMDEIFQeFYYSGDRS---PYGPIN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  169 AL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVS 232
Cdd:cd02660   72 LLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  233 KFYELELNIQGHKQ---------------LTDCITEFLKEEKLeGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRF 297
Cdd:cd02660  149 PFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  298 VFDrQTGHKKKLNTYIGFSELLDMEPFM----------EQKNGVYVYELSAVLIHRGvSAYSGHYIAHVKDpQTGEWYKF 367
Cdd:cd02660  228 EHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQWFKF 304

                 ..
gi 75571442  368 ND 369
Cdd:cd02660  305 DD 306
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-377 2.99e-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: 136.69  E-value: 2.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFLNLELRQALylcsSNEHAAGESIpkdkdyepqtiCEHLQYLFALLQN------SKRRYIDP 163
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDAL----KNYNPARRGA-----------NQSSDNLTNALRDlfdtmdKKQEPVPP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  164 SGFVKALGL---------DTGQ--QQDAQE-FSKLFMSLLEDTLSKQKNPDVrniVQKQFCGEYAYVTVC-NQCGRESKL 230
Cdd:cd02657   66 IEFLQLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVLSQKLPGAGSKGSF---IDQLFGIELETKMKCtESPDEEEVS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  231 VSKFYELELNIqGHKQLTDCITEFLKEeKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLN 310
Cdd:cd02657  143 TESEYKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75571442  311 TYIGFSELLDMEPFMEQKNgvyVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFND--------EDIEKMEG 377
Cdd:cd02657  221 RKVKFPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-417 1.85e-28

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 115.95  E-value: 1.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFLNLELRQALylcssnehaaGESiPKDkdyepqticehlqyLFALLQNSKRRYIDpsgfvka 169
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELL----------SET-PKE--------------LFSQVCRKAPQFKG------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  170 lgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELEL----NIQGHK 245
Cdd:cd02667   49 -----YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSEC 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  246 QLTDCITEFLKEEKLEGDNRYFCETCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNTYIGFSELLDMEPFM 325
Cdd:cd02667  112 SIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAPFC 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  326 EQKNGV------YVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQTGEWYKFNDEDIEkmegk 378
Cdd:cd02667  188 DPKCNSsedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVR----- 261
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 75571442  379 klqlgiEEDLAEPSKSQtrkpkcgkgthcsrnAYMLVYR 417
Cdd:cd02667  262 ------EVSLEEVLKSE---------------AYLLFYE 279
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
78-399 2.58e-28

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 116.92  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   78 PNCERRKKNA--FVGLTNLGATCYVNTFLQMWFLNLELRQAL-YLCSSNEHAagesipkdkdyepqticEHLQYLFALLQ 154
Cdd:cd02671   12 ATSCEKRENLlpFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLkHLVSLISSV-----------------EQLQSSFLLNP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  155 ---NSKRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNIVQKQFCGEYAYVTVCNQCG- 225
Cdd:cd02671   75 ekyNDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECEt 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  226 ---------------RESKLVSKFYELELNIQGH---KQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLP 287
Cdd:cd02671  143 fterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLP 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  288 CTLNLQLMRF----VFDRQTGHKKKLNTYIGFSELLDMEPFMEqKNGVYVYELSAVLIHRGVSAYSGHYIAHVKdpqtge 363
Cdd:cd02671  223 EVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR------ 295
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 75571442  364 WYKFNDEDIEKMEGKKLqlgieEDLAEPSKSQTRKP 399
Cdd:cd02671  296 WLLFDDSEVKVTEEKDF-----LEALSPNTSSTSTP 326
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-370 2.99e-27

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 113.57  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWFlNLELRQALYLcssnehaageSIPKDKDYEPQTICEHLQYLFALL---------------- 153
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRYD----------DLENKFPSDVVDPANDLNCQLIKLadgllsgryskpaslk 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  154 --QNSKRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNIVQKQFCgeyayvtvCN 222
Cdd:cd02658   70 seNDPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  223 QCGRESKLVSKFYELELNIQGHKQ--------------LTDCITEFLKEEKLEgdnrYFCETCQSKQNATRKIRLLSLPC 288
Cdd:cd02658  142 SCKKVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  289 TLNLQLMRFVFDrQTGHKKKLNTYIGFSELLDMEPfmeqkngvyvYELSAVLIHRGVSAYSGHYIAHVK--DPQTGEWYK 366
Cdd:cd02658  218 YLVINMKRFQLL-ENWVPKKLDVPIDVPEELGPGK----------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVL 286

                 ....
gi 75571442  367 FNDE 370
Cdd:cd02658  287 FNDE 290
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
90-374 3.07e-19

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: 88.19  E-value: 3.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWflnlelrqalylcssnehaagESIPkdkdyepqticehlqylfallqnSKRRYIDpsgfvka 169
Cdd:cd02662    1 GLVNLGNTCFMNSVLQAL---------------------ASLP-----------------------SLIEYLE------- 29
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  170 lglDTGQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnivqkqFCGEYAYVTVCNQCGRESKL-VSKFYELELNIQGHKQ-- 246
Cdd:cd02662   30 ---EFLEQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSSgs 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  247 ---LTDCITEFLKEEKLEGdnrYFCETCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNTYIGFSELLDmep 323
Cdd:cd02662   95 gttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP--- 159
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75571442  324 fmeqkngVYVYELSAVLIHRGvSAYSGHYIAH------VKDPQTGE--------------WYKFNDEDIEK 374
Cdd:cd02662  160 -------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKE 222
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
89-369 8.03e-19

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 88.48  E-value: 8.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442     89 VGLTNLGATCYVNTFLQMWFLNLELRQALylcssNEHAAGESIPKDKdyepqTICEhLQYLFALLQNSKRRYIDPSGFVK 168
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLA-----LSHLATECLKEHC-----LLCE-LGFLFDMLEKAKGKNCQASNFLR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    169 ALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNIVQKQFCGEYAYVTVCNQCGRES 228
Cdd:pfam13423   70 ALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGHES 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    229 KLVSKFYELELN------IQGHKQLTDCITEFLKEE-KLEGDNRYFCETCQSKQNATRKIRLLSLPC--TLNLQLMRFVF 299
Cdd:pfam13423  150 VRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSSlERETTTKAWCEKCKRYQPLESRRTVRNLPPvlSLNAALTNEEW 229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75571442    300 DRQTGHKKKLNTYIGfselLDMEPFMEQKNGVYVYELSAVLIHRGVSAYSGHYIAHVK-------DPQTGEWYKFND 369
Cdd:pfam13423  230 RQLWKTPGWLPPEIG----LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
90-375 2.07e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 86.78  E-value: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   90 GLTNLGATCYVNTFLQMWflnlelrqALYLCSSNEHAAGESIP-KD------KDYEPQTICEHLqYLFALLQNSKRRYID 162
Cdd:COG5533    1 GLPNLGNTCFMNSVLQIL--------ALYLPKLDELLDDLSKElKVlknvirKPEPDLNQEEAL-KLFTALWSSKEHKVG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  163 PSGfvkalglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnivqkqfCGEYAYVTVCNQCGRESK------LVSKFYE 236
Cdd:COG5533   72 WIP-------PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  237 LELNIQGHKQ-LTDCITEFLKEEKL--EGDNRYFCETCQSKQNATRKirllSLPCTLNLQLMRFVFDrqtGHKKKLNTYI 313
Cdd:COG5533  131 TWVNNLKTLQeFIDNMEELVDDETGvkAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANL---GGNQKIDTEV 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75571442  314 GfsELLDMEPFMEQKNGV---YVYELSAVLIHRGvSAYSGHYIAHVKdpQTGEWYKFNDEDIEKM 375
Cdd:COG5533  204 D--EKFELPVKHDQILNIvkeTYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
247-374 1.02e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 88.79  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  247 LTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNTYIGFS-ELLDMEPFM 325
Cdd:COG5560  677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 75571442  326 EQK-NGVYVYELSAVLIHRGVSAySGHYIAHVKDPQTGEWYKFNDEDIEK 374
Cdd:COG5560  755 YMVdDPRLIYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
89-373 2.10e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 75.99  E-value: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   89 VGLTNLGATCYVNTFLQMWFLNLELRQA-------LYLCSSNEHA----AGESIPKDKDYEPQTICEHLQYLFALLQNSK 157
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLvlnfdesKAELASDYPTerriGGREVSRSELQRSNQFVYELRSLFNDLIHSN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  158 RRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNIVQKQFCGEY----AYVTVCNQ 223
Cdd:cd02666   82 TRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGNQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  224 CGRESK-------LV-SKFYELELNIQGHKQ-LTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKI---------RLLS 285
Cdd:cd02666  159 PSVRTKterflslLVdVGKKGREIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSID 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  286 LPCTLNLQLMRFVFDRQTGHKKKLNTYigfseLLDMEP-FMEQKNgvYVYELSAVLIHRGvSAYSGHYIAHVKDPQTGEW 364
Cdd:cd02666  239 DIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKqFDDLKS--YGYRLHAVFIHRG-EASSGHYWVYIKDFEENVW 310

                 ....*....
gi 75571442  365 YKFNDEDIE 373
Cdd:cd02666  311 RKYNDETVT 319
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
176-416 9.60e-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: 71.82  E-value: 9.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  176 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVRNivqkqFCGEYAYVTVCNqcGRESKLVSKFYELELNIQGHK 245
Cdd:cd02665   21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMVQL-----FYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  246 QLTDCITEFLKEEKLEGDnryfcETCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNTYIGFSELLDMEPfm 325
Cdd:cd02665   94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVP-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  326 eqkngvyvYELSAVLIHRGvSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKlqlgIEEDlaepsksqtrkpkcGKGT 405
Cdd:cd02665  164 --------YELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD--------------SFGG 216
                        250
                 ....*....|.
gi 75571442  406 HCSRNAYMLVY 416
Cdd:cd02665  217 GRNPSAYCLMY 227
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
481-552 1.27e-13

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: 67.01  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442    481 GSPYDFISLEWLQKWL----DESTPPKPIDNT--ACLCSHGKLHPDKICIMK--RISEYVADFFYRRYGGGPRLNVKALC 552
Cdd:pfam06337    1 GDKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
86-376 5.41e-12

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 69.27  E-value: 5.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   86 NAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLcssnehaaGESIPKDKDYEPQTIcEHLQYLFALLQNSK--RRYIDP 163
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL--------YENYENIKDRKSELV-KRLSELIRKIWNPRnfKGHVSP 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  164 SGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNIVQKQFCGE-----YAYVTVCNQCGRESKL--- 230
Cdd:cd02669  188 HELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKvqietQKIKPHAEEEGSKDKFfkd 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  231 -------VSKFYELELNIQG-----HKQLTDCITEFLKEEKLegdNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFv 298
Cdd:cd02669  268 srvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKRF- 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  299 fDRQTGHKKKLNTYIGFS-ELLDMEPFMEQ---KNGVYV-YELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIE 373
Cdd:cd02669  344 -SKNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVK 422

                 ...
gi 75571442  374 KME 376
Cdd:cd02669  423 EVL 425
DUSP smart00695
Domain in ubiquitin-specific proteases;
477-554 1.88e-10

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 58.14  E-value: 1.88e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442     477 PAEAGSPYDFISLEWLQKWLD-----ESTPPKPIDNTACLCSHG--KLHPDKI--CIMKRISEYVADFFYRRYGGGPR-L 546
Cdd:smart00695    1 PLEEGLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpI 80

                    ....*...
gi 75571442     547 NVKALCKD 554
Cdd:smart00695   81 PRKVVCQG 88
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
171-372 7.49e-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: 60.62  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  171 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNIVQKQFCGEYAYVT----VCNQCGRESKLVSKFYELELNIQG 243
Cdd:cd02673   27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  244 HK--QLTDCITEFLKEEKLEGDnryfCETCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIgfselldM 321
Cdd:cd02673  107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 75571442  322 EPFMEQKNGvyvYELSAVLIHRGVSAYSGHYIAHVKDPQTG-EWYKFNDEDI 372
Cdd:cd02673  175 KKYCGTDAK---YSLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
947-1000 1.43e-07

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: 49.52  E-value: 1.43e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 75571442  947 VSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTaTLGSLGIIPESVILL 1000
Cdd:cd17039   15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
942-1000 1.97e-06

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: 46.48  E-value: 1.97e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 75571442     942 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTaTLGSLGIIPESVILL 1000
Cdd:smart00213   12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
75-369 1.02e-05

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 48.28  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442   75 IDDPNCERRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLCSSNEHAagesipkdkdyEPQTICEhLQYLFALLq 154
Cdd:cd02672    2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAIILVACPK-----------ESCLLCE-LGYLFSTL- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  155 nskrryidpsgfvkalgldtgqqqdAQEFSKLFmslLEDTLSKQKNPDvrnivqkqfcgeyayvtvcNQCGRESKLVSKF 234
Cdd:cd02672   69 -------------------------IQNFTRFL---LETISQDQLGTP-------------------FSCGTSRNSVSLL 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75571442  235 YELELNIQGHKQLTD-----CITEFLKEEKlegDNRYFCETCQSKQNATRKIRLLSLPCTLNLQL---MRFV------FD 300
Cdd:cd02672  102 YTLSLPLGSTKTSKEstflqLLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLvinLSVTngefddIN 178
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75571442  301 RQTGHKKKLNTYIGFSELLDMEPFMEQKN-GVYVYELSAVLIHRGVSAYSGHYIAHVKDPQT----GEWYKFND 369
Cdd:cd02672  179 VVLPSGKVMQNKVSPKAIDHDKLVKNRGQeSIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthGRWYLFND 252
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
947-1000 5.44e-05

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: 42.16  E-value: 5.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 75571442    947 VSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTaTLGSLGIIPESVILL 1000
Cdd:pfam00240   15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQ-TLGEYGIEDGSTIHL 67
Ubl_Ddi1_like cd01796
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ...
947-1001 7.78e-05

ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.


Pssm-ID: 340494 [Multi-domain]  Cd Length: 73  Bit Score: 41.77  E-value: 7.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 75571442  947 VSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTATLGSLGIIPESVILLK 1001
Cdd:cd01796   18 VSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLTDDKKTLEALGLKDGDLLLLR 72
Ubl_TMUB1_like cd17057
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ...
942-998 7.40e-03

ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing proteins TMUB1, TMUB2, and similar proteins; TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. TMUB2 is an uncharacterized transmembrane domain and Ubl domain-containing protein that shows high sequence similarity to TMUB1.


Pssm-ID: 340577  Cd Length: 74  Bit Score: 36.43  E-value: 7.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75571442  942 EKALLVSANQTLKELKIQimhAFSVApFDQNLLI----DGKILSDDTATLGSLGIIPESVI 998
Cdd:cd17057   13 ERVVYARPEDTVGDFKRR---HFPDE-LAQGKRVrliyQGQLLRDDSRTLSSYGIQDGSVI 69
 
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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