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Conserved domains on  [gi|2184285361|ref|NP_001387729|]
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ubiquitin carboxyl-terminal hydrolase 28 isoform 35 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
612-891 0e+00

carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the C-terminal domain of ubiquitin-specific protease USP28, a deubiquitinase (DUB), which shares high similarity with USP25 but varies in cellular function; USP28 is known for its tumor-promoting role while USP25 is a regulator of the innate immune system and may play a role in tumorigenesis. USP28 stabilizes c-MYC and other nuclear proteins, and USP25 regulates inflammatory TRAF signaling. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP28 and harbors the splicing site for isoform-specific sequences. Structure studies suggest that the C-terminal domain forms an independent entity.


:

Pssm-ID: 380452  Cd Length: 280  Bit Score: 575.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 612 LSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 691
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 692 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 771
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 772 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 851
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2184285361 852 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 891
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-494 8.85e-118

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: 357.64  E-value: 8.85e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQEkrnimfmqelqyLFAlmmgsnrkfvdpsaaldllkgafrsseeQQQDVSEFTHKLLDWLEDAF 117
Cdd:cd02665     1 GLKNVGNTCWFSAVIQS------------LFS----------------------------QQQDVSEFTHLLLDWLEDAF 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 118 QLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYG 197
Cdd:cd02665    41 QAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 198 QERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrskelirnkrecirklkeeikilqqkleryvk 277
Cdd:cd02665   121 QERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------------------------------------- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 278 ygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcsvsdqtskeststesssqdvestfsspedslpk 357
Cdd:cd02665       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 358 skpltssrssmempsqpaprtvtdeeinfvktclqrwrseieqdiqdlktciasttqtieqmycdpllRQVPYRLHAVLV 437
Cdd:cd02665   160 --------------------------------------------------------------------QQVPYELHAVLV 171
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2184285361 438 HEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 494
Cdd:cd02665   172 HEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
612-891 0e+00

carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the C-terminal domain of ubiquitin-specific protease USP28, a deubiquitinase (DUB), which shares high similarity with USP25 but varies in cellular function; USP28 is known for its tumor-promoting role while USP25 is a regulator of the innate immune system and may play a role in tumorigenesis. USP28 stabilizes c-MYC and other nuclear proteins, and USP25 regulates inflammatory TRAF signaling. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP28 and harbors the splicing site for isoform-specific sequences. Structure studies suggest that the C-terminal domain forms an independent entity.


Pssm-ID: 380452  Cd Length: 280  Bit Score: 575.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 612 LSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 691
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 692 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 771
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 772 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 851
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2184285361 852 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 891
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-494 8.85e-118

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: 357.64  E-value: 8.85e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQEkrnimfmqelqyLFAlmmgsnrkfvdpsaaldllkgafrsseeQQQDVSEFTHKLLDWLEDAF 117
Cdd:cd02665     1 GLKNVGNTCWFSAVIQS------------LFS----------------------------QQQDVSEFTHLLLDWLEDAF 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 118 QLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYG 197
Cdd:cd02665    41 QAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 198 QERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrskelirnkrecirklkeeikilqqkleryvk 277
Cdd:cd02665   121 QERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------------------------------------- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 278 ygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcsvsdqtskeststesssqdvestfsspedslpk 357
Cdd:cd02665       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 358 skpltssrssmempsqpaprtvtdeeinfvktclqrwrseieqdiqdlktciasttqtieqmycdpllRQVPYRLHAVLV 437
Cdd:cd02665   160 --------------------------------------------------------------------QQVPYELHAVLV 171
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2184285361 438 HEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 494
Cdd:cd02665   172 HEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
37-244 1.21e-20

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 93.66  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  37 VGLKNVGNTCWFSAVIQ-----------------------EKRNIMFMQELQYLF-ALMMGSNRKFVDPSAALDLLKGAF 92
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQslfsippfrdyllrisplsedsrYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  93 RS-SEEQQQDVSEFTHKLLDWLEDAFqlavnVNSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET-------FGQYPL 164
Cdd:pfam00443  81 PDfSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLS---CGEVSetfepfsDLSLPI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 165 QVNGYRNLDECLEGAMVE-------GDVELLPSDHSVKYGQ---ERWFTKLPPVLTFELSRFEFNQSlgQPEKIHNKLEF 234
Cdd:pfam00443 153 PGDSAELKTASLQICFLQfskleelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEF 230
                         250
                  ....*....|
gi 2184285361 235 PQIIYMDRYM 244
Cdd:pfam00443 231 PLELDLSRYL 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
430-494 2.27e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.42  E-value: 2.27e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2184285361  430 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYI 494
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYL 509
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
612-891 0e+00

carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the C-terminal domain of ubiquitin-specific protease USP28, a deubiquitinase (DUB), which shares high similarity with USP25 but varies in cellular function; USP28 is known for its tumor-promoting role while USP25 is a regulator of the innate immune system and may play a role in tumorigenesis. USP28 stabilizes c-MYC and other nuclear proteins, and USP25 regulates inflammatory TRAF signaling. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP28 and harbors the splicing site for isoform-specific sequences. Structure studies suggest that the C-terminal domain forms an independent entity.


Pssm-ID: 380452  Cd Length: 280  Bit Score: 575.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 612 LSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 691
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 692 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 771
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 772 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 851
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2184285361 852 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 891
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-494 8.85e-118

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: 357.64  E-value: 8.85e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQEkrnimfmqelqyLFAlmmgsnrkfvdpsaaldllkgafrsseeQQQDVSEFTHKLLDWLEDAF 117
Cdd:cd02665     1 GLKNVGNTCWFSAVIQS------------LFS----------------------------QQQDVSEFTHLLLDWLEDAF 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 118 QLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYG 197
Cdd:cd02665    41 QAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 198 QERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrskelirnkrecirklkeeikilqqkleryvk 277
Cdd:cd02665   121 QERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------------------------------------- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 278 ygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcsvsdqtskeststesssqdvestfsspedslpk 357
Cdd:cd02665       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 358 skpltssrssmempsqpaprtvtdeeinfvktclqrwrseieqdiqdlktciasttqtieqmycdpllRQVPYRLHAVLV 437
Cdd:cd02665   160 --------------------------------------------------------------------QQVPYELHAVLV 171
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2184285361 438 HEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 494
Cdd:cd02665   172 HEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
612-883 8.17e-115

carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar domains; This family contains the C-terminal domain of two deubiquitinases (DUBs), ubiquitin-specific proteases USP25 and USP28, which share high similarity but vary in their cellular functions. USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This alignment model represents the C-terminal region that has been implicated in substrate binding for both USP25 and USP28 and harbors the splicing site for isoform-specific sequences.


Pssm-ID: 380450  Cd Length: 273  Bit Score: 351.60  E-value: 8.17e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 612 LSEAFHEEYSRLYQLAKETPTS--HSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLsyDERSISIMKVAQAKLKEI 689
Cdd:cd20485     1 LTEAIDEELDRLKSLARTLPSSlpEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 690 G-PDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGP-RRGVKESVIALYRRKCL 767
Cdd:cd20485    79 SiKSDDIEKEYELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKGPpGKGLDEKLLAHYRRKCL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 768 LELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDiSKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRL 847
Cdd:cd20485   159 LKLNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSASS-SEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKL 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2184285361 848 LDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 883
Cdd:cd20485   238 LDPSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
603-883 1.78e-113

carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains the C-terminal domain of ubiquitin-specific protease USP25, a deubiquitinase (DUB), which shares high similarity with USP28 but varies in cellular function; USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. USP25 regulates inflammatory TRAF signaling and USP28 stabilizes c-MYC and other nuclear proteins. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP25 and harbors the splicing site for isoform-specific sequences. Structure studies show that the C-terminally extended USP25 is exclusively tetrameric.


Pssm-ID: 380451  Cd Length: 281  Bit Score: 348.36  E-value: 1.78e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 603 YEKSGVEAALSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVA 682
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 683 QAKLKEIGPDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALY 762
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 763 RRKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGE 842
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2184285361 843 FLPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 883
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
38-494 2.59e-35

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: 134.92  E-value: 2.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAViqekrnimfmqeLQYLFAlmmgsnrkfvdpsaaldllkgafrsseeQQQDVSEFTHKLLDWLEDAF 117
Cdd:cd02257     1 GLNNLGNTCYLNSV------------LQALFS----------------------------EQQDAHEFLLFLLDKLHEEL 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 118 QLAVNVNSPRNKSENPMVQLFYGTFLTE----GVREGKPFCNNETFGQYPLQVNG--YRNLDECLEGAMVEGDVELLPSD 191
Cdd:cd02257    41 KKSSKRTSDSSSLKSLIHDLFGGKLESTivclECGHESVSTEPELFLSLPLPVKGlpQVSLEDCLEKFFKEEILEGDNCY 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 192 H-----SVKYGQERWFTKLPPVLTFELSRFEFNQSlGQPEKIHNKLEFPQIIYMDRYMYRskelirnkrecirklkeeik 266
Cdd:cd02257   121 KcekkkKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLSE-------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 267 ilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcsvsdqtskeststesssqdves 346
Cdd:cd02257       --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 347 tfsspedslpkskpltssrssmempsqpaprtvtdeeinfvktclqrwrseieqdiqdlktciasttqtiEQMYCDPLLR 426
Cdd:cd02257   180 ----------------------------------------------------------------------GEKDSDSDNG 189
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2184285361 427 QVPYRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygGLRNVSAYCLMYI 494
Cdd:cd02257   190 SYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF---GSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-249 3.43e-25

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: 107.51  E-value: 3.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQ------EKRNIMF------------------------MQELQYLFALMMGSNRKFVDPSAALDl 87
Cdd:cd02668     1 GLKNLGATCYVNSFLQlwfmnlEFRKAVYecnstedaelknmppdkphepqtiIDQLQLIFAQLQFGNRSVVDPSGFVK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  88 lkgAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNvnsprNKSENPMVQLFYGTF--LTEGVREGKPFCNNETFGQYPLQ 165
Cdd:cd02668    80 ---ALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN-----PDLKNIVQDLFRGEYsyVTQCSKCGRESSLPSKFYELELQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 166 VNGYRNLDECLEGAMVEgdvELLPSD---HSVKYGQERWFTK------LPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQ 236
Cdd:cd02668   152 LKGHKTLEECIDEFLKE---EQLTGDnqyFCESCNSKTDATRrirlttLPPTLNFQLLRFVFDRKTGAKKKLNASISFPE 228
                         250
                  ....*....|...
gi 2184285361 237 IIYMDRYMYRSKE 249
Cdd:cd02668   229 ILDMGEYLAESDE 241
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
37-244 1.21e-20

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 93.66  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  37 VGLKNVGNTCWFSAVIQ-----------------------EKRNIMFMQELQYLF-ALMMGSNRKFVDPSAALDLLKGAF 92
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQslfsippfrdyllrisplsedsrYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  93 RS-SEEQQQDVSEFTHKLLDWLEDAFqlavnVNSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET-------FGQYPL 164
Cdd:pfam00443  81 PDfSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLS---CGEVSetfepfsDLSLPI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 165 QVNGYRNLDECLEGAMVE-------GDVELLPSDHSVKYGQ---ERWFTKLPPVLTFELSRFEFNQSlgQPEKIHNKLEF 234
Cdd:pfam00443 153 PGDSAELKTASLQICFLQfskleelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEF 230
                         250
                  ....*....|
gi 2184285361 235 PQIIYMDRYM 244
Cdd:pfam00443 231 PLELDLSRYL 240
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
37-495 5.48e-18

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: 86.16  E-value: 5.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  37 VGLKNVGNTCWFSAVIQ------EKRNIMFMQ--------------ELQYLFALMMGSNRKFVDPSAALDLLKGAFRSSE 96
Cdd:cd02659     3 VGLKNQGATCYMNSLLQqlymtpEFRNAVYSIppteddddnksvplALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  97 E-QQQDVSEFTHKLLDWLEDAfqlavnvnSPRNKSENPMVQLFYGTFLTEGVREGkpfCNN-----ETFGQYPLQVNGYR 170
Cdd:cd02659    83 TfEQHDVQEFFRVLFDKLEEK--------LKGTGQEGLIKNLFGGKLVNYIICKE---CPHesereEYFLDLQVAVKGKK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 171 NLDECLEgAMVEGdvELLPSD---HSVKYGQER------WFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQIIymd 241
Cdd:cd02659   152 NLEESLD-AYVQG--ETLEGDnkyFCEKCGKKVdaekgvCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLEL--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 242 rymyrskelirnkrecirklkeeikilqqkleryvkygsgparfplpDMLKYVIEFASTKPASEscppesdthmtlplss 321
Cdd:cd02659   226 -----------------------------------------------DMEPYTEKGLAKKEGDS---------------- 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 322 vhcsvsdqtskeststesssqdvestfsspedslpkskpltssrssmempsqpaPRTVTDEEInfvktclqrwrseieqd 401
Cdd:cd02659   243 ------------------------------------------------------EKKDSESYI----------------- 251
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 402 iqdlktciasttqtieqmycdpllrqvpYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYG 481
Cdd:cd02659   252 ----------------------------YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFG 303
                         490       500
                  ....*....|....*....|....*...
gi 2184285361 482 G--------------LRNVSAYCLMYIN 495
Cdd:cd02659   304 GeetqktydsgprafKRTTNAYMLFYER 331
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
394-475 3.02e-15

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: 77.92  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 394 WRSEIEQD---IQDLKTCIASTTQTIEQMYCDplLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTES 470
Cdd:cd02666   244 IREAIQSEsslVRQAQNELAELKHEIEKQFDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVV 321

                  ....*
gi 2184285361 471 SWEEV 475
Cdd:cd02666   322 PASEV 326
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
430-494 8.14e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 59.99  E-value: 8.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2184285361 430 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsygglRNVSAYCLMYI 494
Cdd:cd02674   174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSV--------VSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
36-249 9.46e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 60.75  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  36 PVGLKNVGNTCWFSAVIQ-------------------EKRNIMF--MQELQYLFALMMGSNRKFVDP---SAALDLLKGA 91
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQclthtpplanyllsrehskDCCNEGFcmMCALEAHVERALASSGPGSAPrifSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  92 FRSSeeQQQDVSEFTHKLLDWLE----DAFQLAVNVNsPRNKSENPMVQLFyGTFLTEGVREGKpfCNNE--TFGQY--- 162
Cdd:cd02661    81 FRIG--RQEDAHEFLRYLLDAMQkaclDRFKKLKAVD-PSSQETTLVQQIF-GGYLRSQVKCLN--CKHVsnTYDPFldl 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 163 PLQVNGYRNLDECLEGAMvegDVELLpsDHSVKYGQER---------WFT--KLPPVLTFELSRFEFNQSlgqpEKIHNK 231
Cdd:cd02661   155 SLDIKGADSLEDALEQFT---KPEQL--DGENKYKCERckkkvkaskQLTihRAPNVLTIHLKRFSNFRG----GKINKQ 225
                         250
                  ....*....|....*...
gi 2184285361 232 LEFPQIIYMDRYMYRSKE 249
Cdd:cd02661   226 ISFPETLDLSPYMSQPND 243
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
430-494 2.27e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.42  E-value: 2.27e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2184285361  430 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYI 494
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYL 509
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
411-494 3.67e-09

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: 59.31  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 411 STTQTIEQMYCDPLLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQsWLKYNDISVTESSWEEVerdsygglRNVSAYC 490
Cdd:cd02660   254 TSSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEV--------LKSQAYL 324

                  ....
gi 2184285361 491 LMYI 494
Cdd:cd02660   325 LFYH 328
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-236 1.55e-08

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: 56.93  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQEKRNIMFMQELQYLFALMMGSNRKF--VDPSAALDLLK---GAFRSSeeQQQDVSEFTHKLL-- 110
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFENLLTCLKDLFESISEQKKRTgvISPKKFITRLKrenELFDNY--MHQDAHEFLNFLLne 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 111 --DWLEDAFQLAVNVNSPRNKSENPMV-----QLFYGTFLTEgVRegkpfC--------NNETFGQYPLQVNGYRNLDEC 175
Cdd:cd02663    79 iaEILDAERKAEKANRKLNNNNNAEPQptwvhEIFQGILTNE-TR-----CltcetvssRDETFLDLSIDVEQNTSITSC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 176 LEGAMVEgdvELLPSDH--------SVKYGQERW-FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQ 236
Cdd:cd02663   153 LRQFSAT---ETLCGRNkfycdeccSLQEAEKRMkIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
37-249 2.20e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 58.34  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361   37 VGLKNVGNTCWFSAVIQEK------RNIMFMQE-------------LQYLFALMMGSNrkfvDPSAALDLLKGAFRSSEE 97
Cdd:COG5077    194 VGLRNQGATCYMNSLLQSLffiakfRKDVYGIPtdhprgrdsvalaLQRLFYNLQTGE----EPVDTTELTRSFGWDSDD 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361   98 Q--QQDVSEFTHKLLDWLEDafqlavnvNSPRNKSENPMVQLFYGTFLT--EGVREGKPFCNNETFGQYPLQVNGYRNLD 173
Cdd:COG5077    270 SfmQHDIQEFNRVLQDNLEK--------SMRGTVVENALNGIFVGKMKSyiKCVNVNYESARVEDFWDIQLNVKGMKNLQ 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  174 ECLEGAMvegDVELLPSDHsvKYGQERW----------FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQII----Y 239
Cdd:COG5077    342 ESFRRYI---QVETLDGDN--RYNAEKHglqdakkgviFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIdllpF 416
                          250
                   ....*....|
gi 2184285361  240 MDRYMYRSKE 249
Cdd:COG5077    417 LDRDADKSEN 426
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-244 4.08e-08

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: 55.47  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQEkrnimfMQELQYLFALMMGSNRKFVDpsaalDLLKGAFRSSEEQQQDVSEFTHKLLDWLedaf 117
Cdd:cd02667     1 GLSNLGNTCFFNAVMQN------LSQTPALRELLSETPKELFS-----QVCRKAPQFKGYQQQDSHELLRYLLDGL---- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 118 qlavnvnsprnkseNPMVQLFYGTFLT-----EGVREGKpfCNNETFGQYPLQV----NGYRNLDECL----EGAMVEGD 184
Cdd:cd02667    66 --------------RTFIDSIFGGELTstimcESCGTVS--LVYEPFLDLSLPRsdeiKSECSIESCLkqftEVEILEGN 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 185 VELLpSDHSVKYGQERWFTKLPPVLTFELSRFeFNQSLGQPEKIHNKLEFPQIIYMDRYM 244
Cdd:cd02667   130 NKFA-CENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSFPEILDLAPFC 187
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
430-493 5.14e-08

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: 55.41  E-value: 5.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2184285361 430 YRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSyGGLRNVSAYCLMY 493
Cdd:cd02657   241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-236 5.33e-07

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: 52.33  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQ----------------------EKRNIMFMQELQYLFAlMMGSNRKFVDPSAALDLLKGAFRSS 95
Cdd:cd02657     1 GLTNLGNTCYLNSTLQclrsvpelrdalknynparrgaNQSSDNLTNALRDLFD-TMDKKQEPVPPIEFLQLLRMAFPQF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  96 EEQ-------QQDVSEFTHKLLdwleDAFQLAVnvnsPRNKSENPMV-QLFYGTFLTEGVREGKPFCNNETFGQ-YPLQV 166
Cdd:cd02657    80 AEKqnqggyaQQDAEECWSQLL----SVLSQKL----PGAGSKGSFIdQLFGIELETKMKCTESPDEEEVSTESeYKLQC 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2184285361 167 N-----GYRNLDECLEGAMVEGDVELLPSDHS-VKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQ 236
Cdd:cd02657   152 HisittEVNYLQDGLKKGLEEEIEKHSPTLGRdAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPF 227
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
426-493 1.39e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 51.34  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 426 RQVPYRLHAVLVHEG-QANAGHYWAYIYNQ--------------------PRQSWLKYNDISVTESSWEEVERDSYGGLR 484
Cdd:cd02664   239 RQVHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSRFPK 318

                  ....*....
gi 2184285361 485 NvSAYCLMY 493
Cdd:cd02664   319 D-TPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
430-476 2.53e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 50.19  E-value: 2.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2184285361 430 YRLHAVLVHEGQANAGHYWAYIYNQPRqsWLKYNDISVTESSWEEVE 476
Cdd:COG5533   225 YDLVGFVLHQGSLEGGHYIAYVKKGGK--WEKANDSDVTPVSEEEAI 269
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-248 3.19e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 50.06  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQ----------------EKRNIMFMQ-------ELQYLFALMMGSNRKfvDPSAALDLLKGAFRS 94
Cdd:cd02660     2 GLINLGATCFMNVILQallhnpllrnyflsdrHSCTCLSCSpnsclscAMDEIFQEFYYSGDR--SPYGPINLLYLSWKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  95 SEE----QQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET------------ 158
Cdd:cd02660    80 SRNlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQR---CGGVSttvdpfldlsld 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 159 --------FGQYPLQVNGYRNLDECLEGAMVEgdvELLPSD----HSVKYGQE--RWFT--KLPPVLTFELSRFEFNQSl 222
Cdd:cd02660   157 ipnkstpsWALGESGVSGTPTLSDCLDRFTRP---EKLGDFaykcSGCGSTQEatKQLSikKLPPVLCFQLKRFEHSLN- 232
                         250       260
                  ....*....|....*....|....*.
gi 2184285361 223 GQPEKIHNKLEFPQIIYMDRYMYRSK 248
Cdd:cd02660   233 KTSRKIDTYVQFPLELNMTPYTSSSI 258
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
427-494 1.98e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 47.66  E-value: 1.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2184285361 427 QVPYRLHAVLVHEG-QANAGHYWAYIyNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 494
Cdd:cd02661   245 PLKYKLYAVLVHSGfSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLSQ--------KAYILFYI 304
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
420-493 1.39e-04

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: 44.68  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 420 YCDPLlRQVP-------YRLHAVLVHEGQANAGHYWAYIYNQPRQ---------------------SWLKYNDISVTESS 471
Cdd:cd02667   186 FCDPK-CNSSedkssvlYRLYGVVEHSGTMRSGHYVAYVKVRPPQqrlsdltkskpaadeagpgsgQWYYISDSDVREVS 264
                          90       100
                  ....*....|....*....|..
gi 2184285361 472 WEEVERdsygglrnVSAYCLMY 493
Cdd:cd02667   265 LEEVLK--------SEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
417-494 4.79e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 44.10  E-value: 4.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2184285361 417 EQMYCDPllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 494
Cdd:COG5560   754 EYMVDDP---RLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTS--------SAYVLFYR 820
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
424-493 7.88e-04

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: 41.97  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361 424 LLRQVPYRLHAVLVHEGQANAGHYWAY--------------------IYNQPRQSWLKYNDISVTESSWEEVerdsyggL 483
Cdd:cd02662   157 RLPKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV-------L 229
                          90
                  ....*....|
gi 2184285361 484 RNVSAYCLMY 493
Cdd:cd02662   230 EQKSAYMLFY 239
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-113 4.39e-03

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 40.17  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285361  38 GLKNVGNTCWFSAVIQ-------------------EKRNIMFMQELQYLFALMMGSNRKfvdPSAALDLLKGAFRS---S 95
Cdd:cd02664     1 GLINLGNTCYMNSVLQalfmakdfrrqvlslnlprLGDSQSVMKKLQLLQAHLMHTQRR---AEAPPDYFLEASRPpwfT 77
                          90
                  ....*....|....*...
gi 2184285361  96 EEQQQDVSEFTHKLLDWL 113
Cdd:cd02664    78 PGSQQDCSEYLRYLLDRL 95
 
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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