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Conserved domains on  [gi|1622866681|ref|XP_028689826|]
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ubiquitin carboxyl-terminal hydrolase 28 isoform X10 [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 ...
527-806 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: 572.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 527 LIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 606
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 607 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 686
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 687 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 766
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866681 767 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 806
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1-315 7.06e-53

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 cd02665:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 228  Bit Score: 183.53  E-value: 7.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681   1 MVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrskelirnkrecir 80
Cdd:cd02665   103 MFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------------------- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681  81 klkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcpvsdqtskeststes 160
Cdd:cd02665       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 161 ssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrseieqdiqdlknciasttqtieqm 240
Cdd:cd02665       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866681 241 ycdpllRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 315
Cdd:cd02665   160 ------QQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
527-806 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: 572.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 527 LIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 606
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 607 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 686
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 687 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 766
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866681 767 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 806
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-315 7.06e-53

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: 183.53  E-value: 7.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681   1 MVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrskelirnkrecir 80
Cdd:cd02665   103 MFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------------------- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681  81 klkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcpvsdqtskeststes 160
Cdd:cd02665       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 161 ssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrseieqdiqdlknciasttqtieqm 240
Cdd:cd02665       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866681 241 ycdpllRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 315
Cdd:cd02665   160 ------QQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
251-314 4.82e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 70.93  E-value: 4.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866681 251 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsyggLRNVSAYCLMY 314
Cdd:pfam00443 254 YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETA-------VLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
251-346 1.30e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.81  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681  251 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYI- 315
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622866681  316 ----NDKLPYFNAEAAP-------NESDQMSEVEALSVELKH 346
Cdd:COG5077    511 ksmlDDLLNPVAAVDIPphveevlSEEIDKTEVRCKEIDEIH 552
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
527-806 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: 572.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 527 LIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 606
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 607 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 686
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 687 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 766
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866681 767 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 806
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
527-798 1.34e-114

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: 348.90  E-value: 1.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 527 LIKAFHEEYSRLYQLAKETPTS--HSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLsyDERSISIMKVAQAKLKEI 604
Cdd:cd20485     1 LTEAIDEELDRLKSLARTLPSSlpEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 605 G-PDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGP-RRGVKESVIALYRRKCL 682
Cdd:cd20485    79 SiKSDDIEKEYELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKGPpGKGLDEKLLAHYRRKCL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 683 LELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDiSKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRL 762
Cdd:cd20485   159 LKLNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSASS-SEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKL 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622866681 763 LDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 798
Cdd:cd20485   238 LDPSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
519-798 6.18e-114

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: 347.21  E-value: 6.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 519 DRDGSEAGLIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQ 598
Cdd:cd20486     2 EDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVAQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 599 AKLKEIGPDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYR 678
Cdd:cd20486    82 AKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHYR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 679 RKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEF 758
Cdd:cd20486   162 RECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTDF 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866681 759 LPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 798
Cdd:cd20486   242 LPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-315 7.06e-53

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: 183.53  E-value: 7.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681   1 MVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIymdrymyrskelirnkrecir 80
Cdd:cd02665   103 MFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQII--------------------- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681  81 klkeeikilqqkleryvkygsgparfplpdmlkyviefastkpasescppesdthmtlplssvhcpvsdqtskeststes 160
Cdd:cd02665       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 161 ssldvestfsspedslhkskpltssrssmempaqpaprtvtdeeinfvktclqrwrseieqdiqdlknciasttqtieqm 240
Cdd:cd02665       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866681 241 ycdpllRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 315
Cdd:cd02665   160 ------QQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
238-315 7.14e-20

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: 89.85  E-value: 7.14e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866681 238 EQMYCDPLLRQVPYRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygGLRNVSAYCLMYI 315
Cdd:cd02257   180 GEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF---GSLSSSAYILFYE 255
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
215-296 9.99e-16

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 79.46  E-value: 9.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 215 WRSEIEQD---IQDLKNCIASTTQTIEQMYCDplLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTES 291
Cdd:cd02666   244 IREAIQSEsslVRQAQNELAELKHEIEKQFDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVV 321

                  ....*
gi 1622866681 292 SWEEV 296
Cdd:cd02666   322 PASEV 326
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-316 2.19e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 72.29  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 251 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYIN 316
Cdd:cd02659   252 YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGeetqktydsgprafKRTTNAYMLFYER 331
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
251-314 4.82e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 70.93  E-value: 4.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866681 251 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsyggLRNVSAYCLMY 314
Cdd:pfam00443 254 YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETA-------VLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-315 4.20e-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: 60.76  E-value: 4.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866681 251 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsygglRNVSAYCLMYI 315
Cdd:cd02674   174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSV--------VSSSAYILFYE 230
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
251-346 1.30e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.81  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681  251 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYI- 315
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622866681  316 ----NDKLPYFNAEAAP-------NESDQMSEVEALSVELKH 346
Cdd:COG5077    511 ksmlDDLLNPVAAVDIPphveevlSEEIDKTEVRCKEIDEIH 552
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
232-315 2.55e-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: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 232 STTQTIEQMYCDPLLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQsWLKYNDISVTESSWEEVerdsygglRNVSAYC 311
Cdd:cd02660   254 TSSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEV--------LKSQAYL 324

                  ....
gi 1622866681 312 LMYI 315
Cdd:cd02660   325 LFYH 328
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-314 4.14e-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: 55.80  E-value: 4.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866681 251 YRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSyGGLRNVSAYCLMY 314
Cdd:cd02657   241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
23-65 7.76e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 54.76  E-value: 7.76e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622866681  23 FTKLPPVLTFELSRFEFNQSlgQPEKIHNKLEFPQIIYMDRYM 65
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
247-314 1.03e-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: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 247 RQVPYRLHAVLVHEG-QANAGHYWAYIYNQ--------------------PRQSWLKYNDISVTESSWEEVERDSYGGLR 305
Cdd:cd02664   239 RQVHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSRFPK 318

                  ....*....
gi 1622866681 306 NvSAYCLMY 314
Cdd:cd02664   319 D-TPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
251-297 2.41e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 50.19  E-value: 2.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622866681 251 YRLHAVLVHEGQANAGHYWAYIYNQPRqsWLKYNDISVTESSWEEVE 297
Cdd:COG5533   225 YDLVGFVLHQGSLEGGHYIAYVKKGGK--WEKANDSDVTPVSEEEAI 269
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
248-315 1.33e-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: 48.04  E-value: 1.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866681 248 QVPYRLHAVLVHEG-QANAGHYWAYIyNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 315
Cdd:cd02661   245 PLKYKLYAVLVHSGfSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLSQ--------KAYILFYI 304
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-314 3.59e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 46.64  E-value: 3.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622866681 251 YRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTE-----------SSWEEVERDSYGGLRNVS--AYCLMY 314
Cdd:cd02668   246 YELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEEmpgkplklgnsEDPAKPRKSEIKKGTHSSrtAYMLVY 323
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-70 8.38e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 45.49  E-value: 8.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622866681  24 TKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQIIYMDRYMYRSKE 70
Cdd:cd02668   195 TTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESDE 241
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
241-314 1.05e-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: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 241 YCDPLlRQVP-------YRLHAVLVHEGQANAGHYWAYIYNQPRQ---------------------SWLKYNDISVTESS 292
Cdd:cd02667   186 FCDPK-CNSSedkssvlYRLYGVVEHSGTMRSGHYVAYVKVRPPQqrlsdltkskpaadeagpgsgQWYYISDSDVREVS 264
                          90       100
                  ....*....|....*....|..
gi 1622866681 293 WEEVERdsygglrnVSAYCLMY 314
Cdd:cd02667   265 LEEVLK--------SEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
238-315 4.72e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.72  E-value: 4.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622866681 238 EQMYCDPllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 315
Cdd:COG5560   754 EYMVDDP---RLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTS--------SAYVLFYR 820
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-70 5.65e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 42.65  E-value: 5.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622866681  25 KLPPVLTFELSRFEFNQSlgqpEKIHNKLEFPQIIYMDRYMYRSKE 70
Cdd:cd02661   202 RAPNVLTIHLKRFSNFRG----GKINKQISFPETLDLSPYMSQPND 243
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
245-314 6.07e-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: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866681 245 LLRQVPYRLHAVLVHEGQANAGHYWAY--------------------IYNQPRQSWLKYNDISVTESSWEEVerdsyggL 304
Cdd:cd02662   157 RLPKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV-------L 229
                          90
                  ....*....|
gi 1622866681 305 RNVSAYCLMY 314
Cdd:cd02662   230 EQKSAYMLFY 239
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-69 1.32e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 41.59  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622866681  25 KLPPVLTFELSRFEFNQSlGQPEKIHNKLEFPQIIYMDRYMYRSK 69
Cdd:cd02660   215 KLPPVLCFQLKRFEHSLN-KTSRKIDTYVQFPLELNMTPYTSSSI 258
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
23-70 9.01e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 39.85  E-value: 9.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622866681   23 FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQII----YMDRYMYRSKE 70
Cdd:COG5077    375 FESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIdllpFLDRDADKSEN 426
 
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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