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Conserved domains on  [gi|1622866678|ref|XP_028689825|]
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ubiquitin carboxyl-terminal hydrolase 28 isoform X9 [Macaca mulatta]

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 ...
736-1015 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: 575.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  736 LIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 815
Cdd:cd20487      1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  816 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 895
Cdd:cd20487     81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  896 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 975
Cdd:cd20487    161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622866678  976 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 1015
Cdd:cd20487    241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-524 8.99e-114

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: 349.93  E-value: 8.99e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsynlpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 117
Cdd:cd02665      1 GLKNVGNTCWFSAVIQSLFS------------------------------------------------------------ 20
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSsPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVN 197
Cdd:cd02665     21 ---------QQQDVSEFTHLLLDWLEDAFQAAAEAIS-PGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVN 90
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  198 GYRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrs 277
Cdd:cd02665     91 GYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------- 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  278 kelirnkrecirklkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcpvs 357
Cdd:cd02665        --------------------------------------------------------------------------------
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  358 dqtskeststesssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrseieqdiqdlkn 437
Cdd:cd02665        --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  438 ciasttqtieqmycdpllRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVS 517
Cdd:cd02665    160 ------------------QQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPS 221

                   ....*..
gi 1622866678  518 AYCLMYI 524
Cdd:cd02665    222 AYCLMYI 228
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
38-142 2.60e-10

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.


The actual alignment was detected with superfamily member cd02664:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 327  Bit Score: 62.89  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLPQNvlencrshTEKRNIMFMqeLQYLFALMMGSNRKfvdPSAALDLL 117
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--------GDSQSVMKK--LQLLQAHLMHTQRR---AEAPPDYF 67
                           90       100
                   ....*....|....*....|....*...
gi 1622866678  118 KGAFRS---SEEQQQDVSEFTHKLLDWL 142
Cdd:cd02664     68 LEASRPpwfTPGSQQDCSEYLRYLLDRL 95
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
736-1015 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: 575.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  736 LIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 815
Cdd:cd20487      1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  816 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 895
Cdd:cd20487     81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  896 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 975
Cdd:cd20487    161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622866678  976 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 1015
Cdd:cd20487    241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-524 8.99e-114

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: 349.93  E-value: 8.99e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsynlpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 117
Cdd:cd02665      1 GLKNVGNTCWFSAVIQSLFS------------------------------------------------------------ 20
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSsPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVN 197
Cdd:cd02665     21 ---------QQQDVSEFTHLLLDWLEDAFQAAAEAIS-PGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVN 90
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  198 GYRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrs 277
Cdd:cd02665     91 GYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------- 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  278 kelirnkrecirklkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcpvs 357
Cdd:cd02665        --------------------------------------------------------------------------------
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  358 dqtskeststesssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrseieqdiqdlkn 437
Cdd:cd02665        --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  438 ciasttqtieqmycdpllRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVS 517
Cdd:cd02665    160 ------------------QQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPS 221

                   ....*..
gi 1622866678  518 AYCLMYI 524
Cdd:cd02665    222 AYCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
37-274 1.53e-30

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.94  E-value: 1.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   37 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYnlpQNVLENCRSHTEkrnIMFMQELQYLF-ALMMGSNRKFVDPSAALD 115
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKD---INLLCALRDLFkALQKNSKSSSVSPKMFKK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  116 LLKGAFRS-SEEQQQDVSEFTHKLLDWLEDAFqlavnvNSSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET------ 188
Cdd:pfam00443   75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDL------NGNHSTENESLITDLFRGQLKSRLKCLS---CGEVSetfepf 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  189 -FGQYPLQVNGYRNLDECLEGAMVE-------GDVELLPSDHSVKYGQ---ERWFTKLPPVLTFELSRFEFNQSlgQPEK 257
Cdd:pfam00443  146 sDLSLPIPGDSAELKTASLQICFLQfskleelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEK 223
                          250
                   ....*....|....*..
gi 1622866678  258 IHNKLEFPQIIYMDRYM 274
Cdd:pfam00443  224 LNTEVEFPLELDLSRYL 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
37-279 8.11e-14

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 76.06  E-value: 8.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   37 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVlsYNLPQNvlencrsHTEKRNIMFMQeLQYLFALMMGSNrkfvDPSAALDL 116
Cdd:COG5077    194 VGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTD-------HPRGRDSVALA-LQRLFYNLQTGE----EPVDTTEL 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  117 LKGAFRSSEEQ--QQDVSEFTHKLLDWLEdafqlavnvNSSPRNKSENPMVQLFYGTFLT--EGVREGKPFCNNETFGQY 192
Cdd:COG5077    260 TRSFGWDSDDSfmQHDIQEFNRVLQDNLE---------KSMRGTVVENALNGIFVGKMKSyiKCVNVNYESARVEDFWDI 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  193 PLQVNGYRNLDECLEGAMvegDVELLPSDHsvKYGQERW----------FTKLPPVLTFELSRFEFNQSLGQPEKIHNKL 262
Cdd:COG5077    331 QLNVKGMKNLQESFRRYI---QVETLDGDN--RYNAEKHglqdakkgviFESLPPVLHLQLKRFEYDFERDMMVKINDRY 405
                          250       260
                   ....*....|....*....|.
gi 1622866678  263 EFPQII----YMDRYMYRSKE 279
Cdd:COG5077    406 EFPLEIdllpFLDRDADKSEN 426
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-142 2.60e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 62.89  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLPQNvlencrshTEKRNIMFMqeLQYLFALMMGSNRKfvdPSAALDLL 117
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--------GDSQSVMKK--LQLLQAHLMHTQRR---AEAPPDYF 67
                           90       100
                   ....*....|....*....|....*...
gi 1622866678  118 KGAFRS---SEEQQQDVSEFTHKLLDWL 142
Cdd:cd02664     68 LEASRPpwfTPGSQQDCSEYLRYLLDRL 95
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
736-1015 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: 575.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  736 LIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 815
Cdd:cd20487      1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  816 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 895
Cdd:cd20487     81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  896 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 975
Cdd:cd20487    161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622866678  976 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 1015
Cdd:cd20487    241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-524 8.99e-114

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: 349.93  E-value: 8.99e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsynlpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 117
Cdd:cd02665      1 GLKNVGNTCWFSAVIQSLFS------------------------------------------------------------ 20
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSsPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVN 197
Cdd:cd02665     21 ---------QQQDVSEFTHLLLDWLEDAFQAAAEAIS-PGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVN 90
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  198 GYRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrs 277
Cdd:cd02665     91 GYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------- 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  278 kelirnkrecirklkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcpvs 357
Cdd:cd02665        --------------------------------------------------------------------------------
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  358 dqtskeststesssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrseieqdiqdlkn 437
Cdd:cd02665        --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  438 ciasttqtieqmycdpllRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVS 517
Cdd:cd02665    160 ------------------QQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPS 221

                   ....*..
gi 1622866678  518 AYCLMYI 524
Cdd:cd02665    222 AYCLMYI 228
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
736-1007 2.36e-113

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: 350.83  E-value: 2.36e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  736 LIKAFHEEYSRLYQLAKETPTS--HSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLsyDERSISIMKVAQAKLKEI 813
Cdd:cd20485      1 LTEAIDEELDRLKSLARTLPSSlpEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  814 G-PDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGP-RRGVKESVIALYRRKCL 891
Cdd:cd20485     79 SiKSDDIEKEYELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKGPpGKGLDEKLLAHYRRKCL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  892 LELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDiSKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRL 971
Cdd:cd20485    159 LKLNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSASS-SEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKL 237
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1622866678  972 LDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 1007
Cdd:cd20485    238 LDPSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
728-1007 1.24e-112

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: 349.13  E-value: 1.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  728 DRDGSEAGLIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQ 807
Cdd:cd20486      2 EDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVAQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  808 AKLKEIGPDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYR 887
Cdd:cd20486     82 AKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHYR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  888 RKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEF 967
Cdd:cd20486    162 RECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTDF 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622866678  968 LPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 1007
Cdd:cd20486    242 LPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-279 1.25e-32

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 129.46  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLPQNV-LENCRSHTEKRNIMFMQELQYLFALMMGSNRKFVDPSAALDl 116
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVK- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  117 lkgAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNVNSSprnkseNPMVQLFYGTF--LTEGVREGKPFCNNETFGQYPL 194
Cdd:cd02668     80 ---ALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLK------NIVQDLFRGEYsyVTQCSKCGRESSLPSKFYELEL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  195 QVNGYRNLDECLEGAMVEgdvELLPSD---HSVKYGQERWFTK------LPPVLTFELSRFEFNQSLGQPEKIHNKLEFP 265
Cdd:cd02668    151 QLKGHKTLEECIDEFLKE---EQLTGDnqyFCESCNSKTDATRrirlttLPPTLNFQLLRFVFDRKTGAKKKLNASISFP 227
                          250
                   ....*....|....
gi 1622866678  266 QIIYMDRYMYRSKE 279
Cdd:cd02668    228 EILDMGEYLAESDE 241
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
38-524 1.66e-31

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


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 124.13  E-value: 1.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsynlpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 117
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNvNSSPRNKSENPMVQLFYGTFLTE----GVREGKPFCNNETFGQYP 193
Cdd:cd02257     21 ---------EQQDAHEFLLFLLDKLHEELKKSSK-RTSDSSSLKSLIHDLFGGKLESTivclECGHESVSTEPELFLSLP 90
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  194 LQVNG--YRNLDECLEGAMVEGDVELLPSDH-----SVKYGQERWFTKLPPVLTFELSRFEFNQSlGQPEKIHNKLEFPQ 266
Cdd:cd02257     91 LPVKGlpQVSLEDCLEKFFKEEILEGDNCYKcekkkKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPL 169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  267 IIYMDRYMYRskelirnkrecirklkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmt 346
Cdd:cd02257    170 ELDLSPYLSE---------------------------------------------------------------------- 179
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  347 lplssvhcpvsdqtskeststesssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrs 426
Cdd:cd02257        --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  427 eieqdiqdlknciasttqtiEQMYCDPLLRQVPYRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEV 505
Cdd:cd02257    180 --------------------GEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEV 239
                          490
                   ....*....|....*....
gi 1622866678  506 ERDsygGLRNVSAYCLMYI 524
Cdd:cd02257    240 LEF---GSLSSSAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
37-274 1.53e-30

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.94  E-value: 1.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   37 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYnlpQNVLENCRSHTEkrnIMFMQELQYLF-ALMMGSNRKFVDPSAALD 115
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKD---INLLCALRDLFkALQKNSKSSSVSPKMFKK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  116 LLKGAFRS-SEEQQQDVSEFTHKLLDWLEDAFqlavnvNSSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET------ 188
Cdd:pfam00443   75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDL------NGNHSTENESLITDLFRGQLKSRLKCLS---CGEVSetfepf 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  189 -FGQYPLQVNGYRNLDECLEGAMVE-------GDVELLPSDHSVKYGQ---ERWFTKLPPVLTFELSRFEFNQSlgQPEK 257
Cdd:pfam00443  146 sDLSLPIPGDSAELKTASLQICFLQfskleelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEK 223
                          250
                   ....*....|....*..
gi 1622866678  258 IHNKLEFPQIIYMDRYM 274
Cdd:pfam00443  224 LNTEVEFPLELDLSRYL 240
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
37-525 1.82e-24

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: 105.80  E-value: 1.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   37 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVlsYNLPQNVLEncrshTEKRNIMFmqELQYLFALMMGSNRKFVDPSAALDL 116
Cdd:cd02659      3 VGLKNQGATCYMNSLLQQLYMTPEFRNAV--YSIPPTEDD-----DDNKSVPL--ALQRLFLFLQLSESPVKTTELTDKT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  117 LKGAFRSSEE-QQQDVSEFTHKLLDWLEdafqlavnvNSSPRNKSENPMVQLFYGTFLTEGVREGkpfCNN-----ETFG 190
Cdd:cd02659     74 RSFGWDSLNTfEQHDVQEFFRVLFDKLE---------EKLKGTGQEGLIKNLFGGKLVNYIICKE---CPHesereEYFL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  191 QYPLQVNGYRNLDECLEgAMVEGdvELLPSD---HSVKYGQER------WFTKLPPVLTFELSRFEFNQSLGQPEKIHNK 261
Cdd:cd02659    142 DLQVAVKGKKNLEESLD-AYVQG--ETLEGDnkyFCEKCGKKVdaekgvCFKKLPPVLTLQLKRFEFDFETMMRIKINDR 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  262 LEFPQIIymdrymyrskelirnkrecirklkeeikilqqkleryvkygsgparfplpDMLKYVIEFASTKPASEscppes 341
Cdd:cd02659    219 FEFPLEL--------------------------------------------------DMEPYTEKGLAKKEGDS------ 242
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  342 dthmtlplssvhcpvsdqtskeststesssldvestfsspedslhkskpltssrssmempaqpaPRTVTDEEInfvktcl 421
Cdd:cd02659    243 ----------------------------------------------------------------EKKDSESYI------- 251
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  422 qrwrseieqdiqdlknciasttqtieqmycdpllrqvpYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESS 501
Cdd:cd02659    252 --------------------------------------YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFD 293
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1622866678  502 WEEVERDSYGG--------------LRNVSAYCLMYIN 525
Cdd:cd02659    294 PNDAEEECFGGeetqktydsgprafKRTTNAYMLFYER 331
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
36-505 9.59e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 88.70  E-value: 9.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   36 PVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNlpQNVLENCRS-HTEK-------------RNIMFMQELQYLFALMM 101
Cdd:cd02666      1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFD--ESKAELASDyPTERriggrevsrselqRSNQFVYELRSLFNDLI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  102 GSNRKFVDPSAALDLLkgAFRsseeqQQDVSEFTHKLLDWLEDAFQLAVNVNSSPRNKSENPMVQLFYGTFLtegvregk 181
Cdd:cd02666     79 HSNTRSVTPSKELAYL--ALR-----QQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFS-------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  182 pfcnnetfGQYPLQVNGyrnldeclegamvegdvELLPSDHSVKYGQERWFTKLPPVltfelsRFEFNQSLGQPEkihnk 261
Cdd:cd02666    144 --------GKTKQQLVP-----------------ESMGNQPSVRTKTERFLSLLVDV------GKKGREIVVLLE----- 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  262 lefPQIIYmdrymyrskelirnkrecirklkeeikilqQKLERYVKYGSgparfplpdmlkyviefastkpaSESCPPES 341
Cdd:cd02666    188 ---PKDLY------------------------------DALDRYFDYDS-----------------------LTKLPQRS 211
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  342 DTHMTLplssvhcpvsdqtskeststesssldvestfsspedslhkSKPLTSSRSSMEMPAQPAPRTVTDEeinfvktcL 421
Cdd:cd02666    212 QVQAQL----------------------------------------AQPLQRELISMDRYELPSSIDDIDE--------L 243
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  422 QRWRSEIEQD-IQDLKNCIASTTQTIEQMYCDplLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTES 500
Cdd:cd02666    244 IREAIQSESSlVRQAQNELAELKHEIEKQFDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVV 321

                   ....*
gi 1622866678  501 SWEEV 505
Cdd:cd02666    322 PASEV 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
37-279 8.11e-14

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 76.06  E-value: 8.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   37 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVlsYNLPQNvlencrsHTEKRNIMFMQeLQYLFALMMGSNrkfvDPSAALDL 116
Cdd:COG5077    194 VGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTD-------HPRGRDSVALA-LQRLFYNLQTGE----EPVDTTEL 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  117 LKGAFRSSEEQ--QQDVSEFTHKLLDWLEdafqlavnvNSSPRNKSENPMVQLFYGTFLT--EGVREGKPFCNNETFGQY 192
Cdd:COG5077    260 TRSFGWDSDDSfmQHDIQEFNRVLQDNLE---------KSMRGTVVENALNGIFVGKMKSyiKCVNVNYESARVEDFWDI 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  193 PLQVNGYRNLDECLEGAMvegDVELLPSDHsvKYGQERW----------FTKLPPVLTFELSRFEFNQSLGQPEKIHNKL 262
Cdd:COG5077    331 QLNVKGMKNLQESFRRYI---QVETLDGDN--RYNAEKHglqdakkgviFESLPPVLHLQLKRFEYDFERDMMVKINDRY 405
                          250       260
                   ....*....|....*....|.
gi 1622866678  263 EFPQII----YMDRYMYRSKE 279
Cdd:COG5077    406 EFPLEIdllpFLDRDADKSEN 426
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-266 1.97e-13

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 72.36  E-value: 1.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNlpqnvleNCRSHTEKRNIMFMQELQYLFAlMMGSNRKFVDPSAALDLL 117
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYN-------PARRGANQSSDNLTNALRDLFD-TMDKKQEPVPPIEFLQLL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 KGAFRSSEEQ-------QQDVSEFTHKLLDWLEdafqlavnvNSSPRNKSENPMV-QLFYGTFLTEGVREGKPFCNNETF 189
Cdd:cd02657     73 RMAFPQFAEKqnqggyaQQDAEECWSQLLSVLS---------QKLPGAGSKGSFIdQLFGIELETKMKCTESPDEEEVST 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  190 GQ-YPLQVN-----GYRNLDECLEGAMVEGDVELLPSDHS-VKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKL 262
Cdd:cd02657    144 ESeYKLQCHisittEVNYLQDGLKKGLEEEIEKHSPTLGRdAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKV 223

                   ....
gi 1622866678  263 EFPQ 266
Cdd:cd02657    224 KFPF 227
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
36-279 9.75e-13

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 70.00  E-value: 9.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   36 PVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLPQnvleNCRSHtekrNIMFMQELQYLFALMMGSNRKFVDP---SA 112
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSK----DCCNE----GFCMMCALEAHVERALASSGPGSAPrifSS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  113 ALDLLKGAFRSSeeQQQDVSEFTHKLLDWLEDA--FQLAVNVNSSPRNKSENPMVQLFyGTFLTEGVREGKpfCNNE--T 188
Cdd:cd02661     73 NLKQISKHFRIG--RQEDAHEFLRYLLDAMQKAclDRFKKLKAVDPSSQETTLVQQIF-GGYLRSQVKCLN--CKHVsnT 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  189 FGQY---PLQVNGYRNLDECLEGAMvegDVELLpsDHSVKYGQER---------WFT--KLPPVLTFELSRFEFNQSlgq 254
Cdd:cd02661    148 YDPFldlSLDIKGADSLEDALEQFT---KPEQL--DGENKYKCERckkkvkaskQLTihRAPNVLTIHLKRFSNFRG--- 219
                          250       260
                   ....*....|....*....|....*
gi 1622866678  255 pEKIHNKLEFPQIIYMDRYMYRSKE 279
Cdd:cd02661    220 -GKINKQISFPETLDLSPYMSQPND 243
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-142 2.60e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 62.89  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLPQNvlencrshTEKRNIMFMqeLQYLFALMMGSNRKfvdPSAALDLL 117
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--------GDSQSVMKK--LQLLQAHLMHTQRR---AEAPPDYF 67
                           90       100
                   ....*....|....*....|....*...
gi 1622866678  118 KGAFRS---SEEQQQDVSEFTHKLLDWL 142
Cdd:cd02664     68 LEASRPpwfTPGSQQDCSEYLRYLLDRL 95
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
460-524 6.66e-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: 60.38  E-value: 6.66e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866678  460 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsygglRNVSAYCLMYI 524
Cdd:cd02674    174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSV--------VSSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-278 7.66e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 61.62  E-value: 7.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLpqnvleNCRSHTEKRNIMFMQELQYLFALMMGSNRKfvDPSAALDLL 117
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRH------SCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--SPYGPINLL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 KGAFRSSEE----QQQDVSEFTHKLLDWLEDAFQLAVNVNSSPrNKSENPMVQLFYGTFLTEGVREGkpfCNNET----- 188
Cdd:cd02660     74 YLSWKHSRNlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDE-SHCNCIIHQTFSGSLQSSVTCQR---CGGVSttvdp 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  189 ---------------FGQYPLQVNGYRNLDECLEGAMVEgdvELLPSD----HSVKYGQE--RWFT--KLPPVLTFELSR 245
Cdd:cd02660    150 fldlsldipnkstpsWALGESGVSGTPTLSDCLDRFTRP---EKLGDFaykcSGCGSTQEatKQLSikKLPPVLCFQLKR 226
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622866678  246 FEFNQSlGQPEKIHNKLEFPQIIYMDRYMYRSK 278
Cdd:cd02660    227 FEHSLN-KTSRKIDTYVQFPLELNMTPYTSSSI 258
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-524 3.46e-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: 59.69  E-value: 3.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  441 STTQTIEQMYCDPLLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQsWLKYNDISVTESSWEEVerdsygglRNVSAYC 520
Cdd:cd02660    254 TSSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEV--------LKSQAYL 324

                   ....
gi 1622866678  521 LMYI 524
Cdd:cd02660    325 LFYH 328
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
38-263 9.46e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 57.89  E-value: 9.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSL-FQLPEFRRLVLSYNLPQNVLENcrSHTEKRNIMFMQELQYLFALMMGSnrkfvdpsaalDL 116
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKN--VIRKPEPDLNQEEALKLFTALWSS-----------KE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  117 LKGAFRSSEEQQQDVSEFTHKLLDWLEdafqlAVNVNSsprnksenpmVQLFYGTFLTEGVREG-KPFCNNETFGQYPLQ 195
Cdd:COG5533     68 HKVGWIPPMGSQEDAHELLGKLLDELK-----LDLVNS----------FTIRIFKTTKDKKKTStGDWFDIIIELPDQTW 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866678  196 VNGYRNLDECLEGAMVEGDVELL------PSDHSV-KYGQERWFTKLPPVLTFELSRFEFNqslGQPEKIHNKLE 263
Cdd:COG5533    133 VNNLKTLQEFIDNMEELVDDETGvkakenEELEVQaKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD 204
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-274 1.03e-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: 57.78  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLsynlpqnvlencrshtEKRNIMFMQelqylfalmmgsnrkfvdpsaaldLL 117
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLS----------------ETPKELFSQ------------------------VC 40
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  118 KGAFRSSEEQQQDVSEFTHKLLDWLedafqlavnvnssprnkseNPMVQLFYGTFLT-----EGVREGKpfCNNETFGQY 192
Cdd:cd02667     41 RKAPQFKGYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTstimcESCGTVS--LVYEPFLDL 99
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  193 PLQV----NGYRNLDECL----EGAMVEGDVELLpSDHSVKYGQERWFTKLPPVLTFELSRFeFNQSLGQPEKIHNKLEF 264
Cdd:cd02667    100 SLPRsdeiKSECSIESCLkqftEVEILEGNNKFA-CENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSF 177
                          250
                   ....*....|
gi 1622866678  265 PQIIYMDRYM 274
Cdd:cd02667    178 PEILDLAPFC 187
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
460-523 5.27e-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: 55.80  E-value: 5.27e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866678  460 YRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSyGGLRNVSAYCLMY 523
Cdd:cd02657    241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-266 3.96e-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 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: 53.08  E-value: 3.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLpefrrlvlsyNLpqnvlencrshtekrnimfMQELQYLFALMMGSNRKF--VDPSAALD 115
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYFE----------NL-------------------LTCLKDLFESISEQKKRTgvISPKKFIT 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  116 LLK---GAFRSSeeQQQDVSEFTHKLLDWLED---AFQLAVNVNSSPRNKSENPMV-----QLFYGTFLTEgVRegkpfC 184
Cdd:cd02663     52 RLKrenELFDNY--MHQDAHEFLNFLLNEIAEildAERKAEKANRKLNNNNNAEPQptwvhEIFQGILTNE-TR-----C 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  185 --------NNETFGQYPLQVNGYRNLDECLEGAMVEgdvELLPSDH--------SVKYGQERW-FTKLPPVLTFELSRFE 247
Cdd:cd02663    124 ltcetvssRDETFLDLSIDVEQNTSITSCLRQFSAT---ETLCGRNkfycdeccSLQEAEKRMkIKKLPKILALHLKRFK 200
                          250
                   ....*....|....*....
gi 1622866678  248 FNQSLGQPEKIHNKLEFPQ 266
Cdd:cd02663    201 YDEQLNRYIKLFYRVVFPL 219
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
456-523 1.33e-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: 51.72  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  456 RQVPYRLHAVLVHEG-QANAGHYWAYIYNQ--------------------PRQSWLKYNDISVTESSWEEVERDSYGGLR 514
Cdd:cd02664    239 RQVHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSRFPK 318

                   ....*....
gi 1622866678  515 NvSAYCLMY 523
Cdd:cd02664    319 D-TPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
460-506 2.96e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 50.19  E-value: 2.96e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622866678  460 YRLHAVLVHEGQANAGHYWAYIYNQPRqsWLKYNDISVTESSWEEVE 506
Cdd:COG5533    225 YDLVGFVLHQGSLEGGHYIAYVKKGGK--WEKANDSDVTPVSEEEAI 269
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
457-524 1.84e-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: 1.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866678  457 QVPYRLHAVLVHEG-QANAGHYWAYIyNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 524
Cdd:cd02661    245 PLKYKLYAVLVHSGfSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLSQ--------KAYILFYI 304
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
450-523 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: 45.07  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  450 YCDPLlRQVP-------YRLHAVLVHEGQANAGHYWAYIYNQPRQ---------------------SWLKYNDISVTESS 501
Cdd:cd02667    186 FCDPK-CNSSedkssvlYRLYGVVEHSGTMRSGHYVAYVKVRPPQqrlsdltkskpaadeagpgsgQWYYISDSDVREVS 264
                           90       100
                   ....*....|....*....|..
gi 1622866678  502 WEEVERdsygglrnVSAYCLMY 523
Cdd:cd02667    265 LEEVLK--------SEAYLLFY 278
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-273 3.87e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 43.85  E-value: 3.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   38 GLKNVGNTCWFSAVIQSLFQLPEF-RRLVLSYNLPQNVLENCRSHTEkrnimfMQELQYLFALMMGSNRK-FVDPSAALD 115
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDLN------CQLIKLADGLLSGRYSKpASLKSENDP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  116 LLKG----AFRS---------SEEQQQDVSEFTHKLLDWLEdafqlavnvNSSPRNKSENP--MVQLFYGTFL----TEG 176
Cdd:cd02658     75 YQVGikpsMFKAligkghpefSTMRQQDALEFLLHLIDKLD---------RESFKNLGLNPndLFKFMIEDRLeclsCKK 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  177 VREGKPFCNN---------ETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYG--QERWFTKLPPVLTFELSR 245
Cdd:cd02658    146 VKYTSELSEIlslpvpkdeATEKEEGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTTatKTTGFKTFPDYLVINMKR 225
                          250       260
                   ....*....|....*....|....*...
gi 1622866678  246 FEFNQSlGQPEKIHNKLEFPQIIYMDRY 273
Cdd:cd02658    226 FQLLEN-WVPKKLDVPIDVPEELGPGKY 252
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
447-524 5.24e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 44.10  E-value: 5.24e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622866678  447 EQMYCDPllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 524
Cdd:COG5560    754 EYMVDDP---RLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTS--------SAYVLFYR 820
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
454-523 7.92e-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: 42.35  E-value: 7.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  454 LLRQVPYRLHAVLVHEGQANAGHYWAY--------------------IYNQPRQSWLKYNDISVTESSWEEVerdsyggL 513
Cdd:cd02662    157 RLPKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV-------L 229
                           90
                   ....*....|
gi 1622866678  514 RNVSAYCLMY 523
Cdd:cd02662    230 EQKSAYMLFY 239
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
37-296 8.53e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 39.61  E-value: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678   37 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYNLPQNVLENCrSHTEKRNIMFMQEL-------------QYLFALMMGS 103
Cdd:cd02669    120 VGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRK-SELVKRLSELIRKIwnprnfkghvsphELLQAVSKVS 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  104 NRKFvdpsaaldllkgafrsSEEQQQDVSEF-------THKLLDW--------LEDAFQLAVNVNSSP--RNKSENPMVQ 166
Cdd:cd02669    199 KKKF----------------SITEQSDPVEFlswllntLHKDLGGskkpnssiIHDCFQGKVQIETQKikPHAEEEGSKD 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866678  167 LFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYR-------NLDECLEGamVEGDVELLPSDHSVKYGQerwfTKLPPVL 239
Cdd:cd02669    263 KFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEeniipqvPLKQLLKK--YDGKTETELKDSLKRYLI----SRLPKYL 336
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866678  240 TFELSRFEFNQslGQPEKihNK--LEFPQIIyMDRYMYRSKELIRNKRECIRKLKEEIK 296
Cdd:cd02669    337 IFHIKRFSKNN--FFKEK--NPtiVNFPIKN-LDLSDYVHFDKPSLNLSTKYNLVANIV 390
 
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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