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Conserved domains on  [gi|1622866695|ref|XP_028689831|]
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ubiquitin carboxyl-terminal hydrolase 28 isoform X14 [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 ...
414-693 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: 570.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 414 LSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 493
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 494 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 573
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 574 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 653
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866695 654 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 693
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
148-296 8.58e-52

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: 178.91  E-value: 8.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 148 STFSSPEDSLH--KSKPLTSSRSSMEMPAqpaprTVTDEEINFVK----TCLQRWRSEIEQDIQdlknciasttqtieqm 221
Cdd:cd02665   102 AMFEGEVELLPsdHSVKSGQERWFTELPP-----VLTFELSRFEFnqgrPEKIHDKLEFPQIIQ---------------- 160
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866695 222 ycdpllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 296
Cdd:cd02665   161 -------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
4-46 1.09e-07

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 pfam00443:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 310  Bit Score: 53.99  E-value: 1.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622866695   4 FTKLPPVLTFELSRFEFNQSlgQPEKIHNKLEFPQIIYMDRYM 46
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL 240
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
414-693 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: 570.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 414 LSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 493
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 494 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 573
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 574 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 653
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866695 654 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 693
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
148-296 8.58e-52

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: 178.91  E-value: 8.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 148 STFSSPEDSLH--KSKPLTSSRSSMEMPAqpaprTVTDEEINFVK----TCLQRWRSEIEQDIQdlknciasttqtieqm 221
Cdd:cd02665   102 AMFEGEVELLPsdHSVKSGQERWFTELPP-----VLTFELSRFEFnqgrPEKIHDKLEFPQIIQ---------------- 160
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866695 222 ycdpllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 296
Cdd:cd02665   161 -------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
232-295 7.79e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 69.78  E-value: 7.79e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866695 232 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsyggLRNVSAYCLMY 295
Cdd:pfam00443 254 YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETA-------VLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
232-327 1.28e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.81  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695  232 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYI- 296
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622866695  297 ----NDKLPYFNAEAAP-------NESDQMSEVEALSVELKH 327
Cdd:COG5077    511 ksmlDDLLNPVAAVDIPphveevlSEEIDKTEVRCKEIDEIH 552
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
4-46 1.09e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 53.99  E-value: 1.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622866695   4 FTKLPPVLTFELSRFEFNQSlgQPEKIHNKLEFPQIIYMDRYM 46
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL 240
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
5-51 9.35e-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: 45.10  E-value: 9.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622866695   5 TKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQIIYMDRYMYRSKE 51
Cdd:cd02668   195 TTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESDE 241
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
4-51 8.48e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 39.47  E-value: 8.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622866695    4 FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQII----YMDRYMYRSKE 51
Cdd:COG5077    375 FESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIdllpFLDRDADKSEN 426
 
Name Accession Description Interval E-value
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
414-693 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: 570.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 414 LSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVAQAKLKEIGP 493
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 494 DDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALYRRKCLLELN 573
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 574 AKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRLLDPS 653
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1622866695 654 AEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK 693
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGTSTVTVK 280
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
414-685 1.57e-115

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


Pssm-ID: 380450  Cd Length: 273  Bit Score: 347.74  E-value: 1.57e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 414 LSEAFHEEYSRLYQLAKETPTS--HSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLsyDERSISIMKVAQAKLKEI 491
Cdd:cd20485     1 LTEAIDEELDRLKSLARTLPSSlpEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 492 G-PDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGP-RRGVKESVIALYRRKCL 569
Cdd:cd20485    79 SiKSDDIEKEYELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKGPpGKGLDEKLLAHYRRKCL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 570 LELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDiSKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGEFLPRL 649
Cdd:cd20485   159 LKLNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSASS-SEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKL 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622866695 650 LDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 685
Cdd:cd20485   238 LDPSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
405-685 1.14e-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: 346.05  E-value: 1.14e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 405 YEKSGVEAALSEAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADKNLSYDERSISIMKVA 484
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 485 QAKLKEIGPDDMNMEEYKKWHEDYSLFRKVSVYLLTGLELYQKGKYQEALSYLVYAYQSNAALLMKGPRRGVKESVIALY 564
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 565 RRKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGQDIAENLQLCLGE 644
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1622866695 645 FLPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQ 685
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
148-296 8.58e-52

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: 178.91  E-value: 8.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 148 STFSSPEDSLH--KSKPLTSSRSSMEMPAqpaprTVTDEEINFVK----TCLQRWRSEIEQDIQdlknciasttqtieqm 221
Cdd:cd02665   102 AMFEGEVELLPsdHSVKSGQERWFTELPP-----VLTFELSRFEFnqgrPEKIHDKLEFPQIIQ---------------- 160
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866695 222 ycdpllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYI 296
Cdd:cd02665   161 -------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
219-296 1.76e-19

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: 88.69  E-value: 1.76e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866695 219 EQMYCDPLLRQVPYRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygGLRNVSAYCLMYI 296
Cdd:cd02257   180 GEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF---GSLSSSAYILFYE 255
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
196-277 8.02e-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: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 196 WRSEIEQD---IQDLKNCIASTTQTIEQMYCDplLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTES 272
Cdd:cd02666   244 IREAIQSEsslVRQAQNELAELKHEIEKQFDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVV 321

                  ....*
gi 1622866695 273 SWEEV 277
Cdd:cd02666   322 PASEV 326
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
232-297 2.60e-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: 71.52  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 232 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYIN 297
Cdd:cd02659   252 YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGeetqktydsgprafKRTTNAYMLFYER 331
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
232-295 7.79e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 69.78  E-value: 7.79e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866695 232 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsyggLRNVSAYCLMY 295
Cdd:pfam00443 254 YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETA-------VLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
232-296 7.08e-10

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 59.61  E-value: 7.08e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866695 232 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVerdsygglRNVSAYCLMYI 296
Cdd:cd02674   174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSV--------VSSSAYILFYE 230
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
232-327 1.28e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.81  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695  232 YRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGG--------------LRNVSAYCLMYI- 296
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622866695  297 ----NDKLPYFNAEAAP-------NESDQMSEVEALSVELKH 327
Cdd:COG5077    511 ksmlDDLLNPVAAVDIPphveevlSEEIDKTEVRCKEIDEIH 552
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
213-296 3.54e-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: 58.92  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 213 STTQTIEQMYCDPLLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQsWLKYNDISVTESSWEEVerdsygglRNVSAYC 292
Cdd:cd02660   254 TSSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEV--------LKSQAYL 324

                  ....
gi 1622866695 293 LMYI 296
Cdd:cd02660   325 LFYH 328
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
232-295 3.92e-08

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 55.41  E-value: 3.92e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622866695 232 YRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSyGGLRNVSAYCLMY 295
Cdd:cd02657   241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
4-46 1.09e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 53.99  E-value: 1.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622866695   4 FTKLPPVLTFELSRFEFNQSlgQPEKIHNKLEFPQIIYMDRYM 46
Cdd:pfam00443 200 ISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
228-295 1.24e-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: 50.95  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 228 RQVPYRLHAVLVHEG-QANAGHYWAYIYNQ--------------------PRQSWLKYNDISVTESSWEEVERDSYGGLR 286
Cdd:cd02664   239 RQVHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSRFPK 318

                  ....*....
gi 1622866695 287 NvSAYCLMY 295
Cdd:cd02664   319 D-TPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
232-278 1.97e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 50.19  E-value: 1.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622866695 232 YRLHAVLVHEGQANAGHYWAYIYNQPRqsWLKYNDISVTESSWEEVE 278
Cdd:COG5533   225 YDLVGFVLHQGSLEGGHYIAYVKKGGK--WEKANDSDVTPVSEEEAI 269
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
229-296 1.76e-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: 47.27  E-value: 1.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866695 229 QVPYRLHAVLVHEG-QANAGHYWAYIyNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 296
Cdd:cd02661   245 PLKYKLYAVLVHSGfSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLSQ--------KAYILFYI 304
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
232-295 4.38e-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: 46.26  E-value: 4.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622866695 232 YRLHAVLVHEGQ-ANAGHYWAYIYNQPRQSWLKYNDISVTE-----------SSWEEVERDSYGGLRNVS--AYCLMY 295
Cdd:cd02668   246 YELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEEmpgkplklgnsEDPAKPRKSEIKKGTHSSrtAYMLVY 323
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
5-51 9.35e-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: 45.10  E-value: 9.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622866695   5 TKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQIIYMDRYMYRSKE 51
Cdd:cd02668   195 TTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESDE 241
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
222-295 1.29e-04

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 44.30  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 222 YCDPLlRQVP-------YRLHAVLVHEGQANAGHYWAYIYNQPRQ---------------------SWLKYNDISVTESS 273
Cdd:cd02667   186 FCDPK-CNSSedkssvlYRLYGVVEHSGTMRSGHYVAYVKVRPPQqrlsdltkskpaadeagpgsgQWYYISDSDVREVS 264
                          90       100
                  ....*....|....*....|..
gi 1622866695 274 WEEVERdsygglrnVSAYCLMY 295
Cdd:cd02667   265 LEEVLK--------SEAYLLFY 278
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
219-296 4.35e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.72  E-value: 4.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622866695 219 EQMYCDPllrQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDsygglrnvSAYCLMYI 296
Cdd:COG5560   754 EYMVDDP---RLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTS--------SAYVLFYR 820
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
6-51 6.85e-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: 42.26  E-value: 6.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622866695   6 KLPPVLTFELSRFEFNQSlgqpEKIHNKLEFPQIIYMDRYMYRSKE 51
Cdd:cd02661   202 RAPNVLTIHLKRFSNFRG----GKINKQISFPETLDLSPYMSQPND 243
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
226-295 7.81e-04

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.58  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866695 226 LLRQVPYRLHAVLVHEGQANAGHYWAY--------------------IYNQPRQSWLKYNDISVTESSWEEVerdsyggL 285
Cdd:cd02662   157 RLPKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV-------L 229
                          90
                  ....*....|
gi 1622866695 286 RNVSAYCLMY 295
Cdd:cd02662   230 EQKSAYMLFY 239
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
6-50 1.56e-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: 41.20  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622866695   6 KLPPVLTFELSRFEFNQSlGQPEKIHNKLEFPQIIYMDRYMYRSK 50
Cdd:cd02660   215 KLPPVLCFQLKRFEHSLN-KTSRKIDTYVQFPLELNMTPYTSSSI 258
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
4-51 8.48e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 39.47  E-value: 8.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622866695    4 FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQII----YMDRYMYRSKE 51
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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