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Conserved domains on  [gi|568997588|ref|XP_006523120|]
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ubiquitin carboxyl-terminal hydrolase 25 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
529-809 0e+00

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: 532.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 529 YDRCGPEAGFFKAIKLEYSRLVKLAQEDTPPETDYRLHHVLVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 608
Cdd:cd20486    1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 609 QAKLEMIKPEEVNLEEYEEWHADYKKFRETTMYLITGLENFQRESYIDSLLFLLCAYQNNKELLSKGPYRGHDGELISHY 688
Cdd:cd20486   81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 689 RRECLLKLNEQAAELFESGEDGDVNNGLIIMNEFIVPFLPLLLVDDMEEKDILAVEDMRNRWCSYLGQEMEANLQEKLTD 768
Cdd:cd20486  161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568997588 769 FLPKLLDCSTEIKGFHEPPKLPSYSAHELCERFARIMLSLS 809
Cdd:cd20486  241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-338 2.39e-63

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: 212.03  E-value: 2.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588   1 MFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSDNSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQv 80
Cdd:cd02665   81 TFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  81 lyldrymhrnreitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidasssa 160
Cdd:cd02665  158 -------------------IIQ---------------------------------------------------------- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 161 sgplpsqslpstteqqgpcasdlpgssspasgaalplrsvihkpftqsrippdlpmhpaprhiteeelcvlesclhrwrt 240
Cdd:cd02665      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 241 eiendtrdlqesisrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELV 320
Cdd:cd02665  161 ------------------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVE 210
                        330
                 ....*....|....*...
gi 568997588 321 RDSFGGYRNASAYCLMYI 338
Cdd:cd02665  211 RDSFGGGRNPSAYCLMYI 228
PHA03369 super family cl25753
capsid maturational protease; Provisional
91-218 3.39e-04

capsid maturational protease; Provisional


The actual alignment was detected with superfamily member PHA03369:

Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 44.22  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  91 REITRIKREEIKRLKDYLTVLQ--------QRLERYLSYGSgpKRFPLVDVLQYALEFASSKpVCTSPVDDIDASSSASG 162
Cdd:PHA03369 292 PEWKTFYEALADQLNNLYKLLRtiykhkdeTVIEQYLIEGR--KLFSTINGLKAHNEILKTA-SLTAPSRVLAAAAKVAV 368
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568997588 163 PLPSQSLPSTTEQQGPCASDLPGSSSPASGAALPLRSVIHKPFTQSRIPPDLPMHP 218
Cdd:PHA03369 369 IAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSP 424
 
Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
529-809 0e+00

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: 532.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 529 YDRCGPEAGFFKAIKLEYSRLVKLAQEDTPPETDYRLHHVLVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 608
Cdd:cd20486    1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 609 QAKLEMIKPEEVNLEEYEEWHADYKKFRETTMYLITGLENFQRESYIDSLLFLLCAYQNNKELLSKGPYRGHDGELISHY 688
Cdd:cd20486   81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 689 RRECLLKLNEQAAELFESGEDGDVNNGLIIMNEFIVPFLPLLLVDDMEEKDILAVEDMRNRWCSYLGQEMEANLQEKLTD 768
Cdd:cd20486  161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568997588 769 FLPKLLDCSTEIKGFHEPPKLPSYSAHELCERFARIMLSLS 809
Cdd:cd20486  241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-338 2.39e-63

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: 212.03  E-value: 2.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588   1 MFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSDNSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQv 80
Cdd:cd02665   81 TFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  81 lyldrymhrnreitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidasssa 160
Cdd:cd02665  158 -------------------IIQ---------------------------------------------------------- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 161 sgplpsqslpstteqqgpcasdlpgssspasgaalplrsvihkpftqsrippdlpmhpaprhiteeelcvlesclhrwrt 240
Cdd:cd02665      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 241 eiendtrdlqesisrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELV 320
Cdd:cd02665  161 ------------------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVE 210
                        330
                 ....*....|....*...
gi 568997588 321 RDSFGGYRNASAYCLMYI 338
Cdd:cd02665  211 RDSFGGGRNPSAYCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
274-337 1.55e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 69.39  E-value: 1.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568997588  274 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSfggyrnaSAYCLMY 337
Cdd:pfam00443 254 YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS-------SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
274-396 3.82e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 66.82  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  274 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGG--------------YRNASAYCLMYI- 338
Cdd:COG5077   431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568997588  339 DDKAQFLIQEefnketgqalVGMETLPPDLRDFVEEDNQRFEKELEEWDTQLAQRSLQ 396
Cdd:COG5077   511 KSMLDDLLNP----------VAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVR 558
PHA03369 PHA03369
capsid maturational protease; Provisional
91-218 3.39e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 44.22  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  91 REITRIKREEIKRLKDYLTVLQ--------QRLERYLSYGSgpKRFPLVDVLQYALEFASSKpVCTSPVDDIDASSSASG 162
Cdd:PHA03369 292 PEWKTFYEALADQLNNLYKLLRtiykhkdeTVIEQYLIEGR--KLFSTINGLKAHNEILKTA-SLTAPSRVLAAAAKVAV 368
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568997588 163 PLPSQSLPSTTEQQGPCASDLPGSSSPASGAALPLRSVIHKPFTQSRIPPDLPMHP 218
Cdd:PHA03369 369 IAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSP 424
 
Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
529-809 0e+00

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: 532.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 529 YDRCGPEAGFFKAIKLEYSRLVKLAQEDTPPETDYRLHHVLVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 608
Cdd:cd20486    1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 609 QAKLEMIKPEEVNLEEYEEWHADYKKFRETTMYLITGLENFQRESYIDSLLFLLCAYQNNKELLSKGPYRGHDGELISHY 688
Cdd:cd20486   81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 689 RRECLLKLNEQAAELFESGEDGDVNNGLIIMNEFIVPFLPLLLVDDMEEKDILAVEDMRNRWCSYLGQEMEANLQEKLTD 768
Cdd:cd20486  161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568997588 769 FLPKLLDCSTEIKGFHEPPKLPSYSAHELCERFARIMLSLS 809
Cdd:cd20486  241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
540-811 5.09e-114

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: 347.99  E-value: 5.09e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 540 KAIKLEYSRLVKLAQEDTPPETDYRLHHVLVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVAQAKLEMIKPEE 619
Cdd:cd20487    3 KAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGPDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 620 VNLEEYEEWHADYKKFRETTMYLITGLENFQRESYIDSLLFLLCAYQNNKELLSKGPYRGHDGELISHYRRECLLKLNEQ 699
Cdd:cd20487   83 MDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELNDK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 700 AAELFESGEDGDVNNGLIIMNEFIVPFLPLLLVDDMEEKDILAVEDMRNRWCSYLGQEMEANLQEKLTDFLPKLLDCSTE 779
Cdd:cd20487  163 AASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCSTE 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568997588 780 IKGFHEPPKLPSYSAHELCERFARIMLSLSRT 811
Cdd:cd20487  243 VIVLKEPPKIRPNSPHDLCSRFAAVMESIHGT 274
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
540-809 5.56e-110

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: 336.96  E-value: 5.56e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 540 KAIKLEYSRLVKLAQEDTP--PETDYRLHHVLVYFIQNQAPKKIIEKTLLEQFGDRNLsfDERCHNIMKVAQAKLEMIKP 617
Cdd:cd20485    3 EAIDEELDRLKSLARTLPSslPEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEELSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 618 EEVNLEEY-EEWHADYKKFRETTMYLITGLENFQRESYIDSLLFLLCAYQNNKELLSKGP-YRGHDGELISHYRRECLLK 695
Cdd:cd20485   81 KSDDIEKEyELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKGPpGKGLDEKLLAHYRRKCLLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 696 LNEQAAELFESGEDGDVNNGLIIMNEFIVPFLPLLLVDdMEEKDILAVEDMRNRWCSYLGQEMEANLQEKLTDFLPKLLD 775
Cdd:cd20485  161 LNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSAS-SSEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKLLD 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568997588 776 CSTEIKGFHEPPKLPSYSAHELCERFARIMLSLS 809
Cdd:cd20485  240 PSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-338 2.39e-63

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: 212.03  E-value: 2.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588   1 MFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSDNSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQv 80
Cdd:cd02665   81 TFGQYPLQVNGYGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  81 lyldrymhrnreitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidasssa 160
Cdd:cd02665  158 -------------------IIQ---------------------------------------------------------- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 161 sgplpsqslpstteqqgpcasdlpgssspasgaalplrsvihkpftqsrippdlpmhpaprhiteeelcvlesclhrwrt 240
Cdd:cd02665      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 241 eiendtrdlqesisrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELV 320
Cdd:cd02665  161 ------------------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVE 210
                        330
                 ....*....|....*...
gi 568997588 321 RDSFGGYRNASAYCLMYI 338
Cdd:cd02665  211 RDSFGGGRNPSAYCLMYI 228
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
261-338 3.15e-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: 87.92  E-value: 3.15e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568997588 261 ELMYSDKSMIQVPYRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDsfgGYRNASAYCLMYI 338
Cdd:cd02257  180 GEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF---GSLSSSAYILFYE 255
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
235-338 1.78e-15

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 78.69  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 235 LHRWRTEIEND-TRDLQESISRIHRTIELMYSDksMIQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTK 313
Cdd:cd02666  243 LIREAIQSESSlVRQAQNELAELKHEIEKQFDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTV 320
                         90       100
                 ....*....|....*....|....*
gi 568997588 314 SSWEELVRDSFGGyrNASAYCLMYI 338
Cdd:cd02666  321 VPASEVFLFTLGN--TATPYFLVYV 343
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-338 8.20e-15

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 76.53  E-value: 8.20e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568997588 274 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGY--------------RNASAYCLMYI 338
Cdd:cd02659  252 YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEetqktydsgprafkRTTNAYMLFYE 330
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
274-337 1.55e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 69.39  E-value: 1.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568997588  274 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSfggyrnaSAYCLMY 337
Cdd:pfam00443 254 YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS-------SAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
274-396 3.82e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 66.82  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  274 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGG--------------YRNASAYCLMYI- 338
Cdd:COG5077   431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568997588  339 DDKAQFLIQEefnketgqalVGMETLPPDLRDFVEEDNQRFEKELEEWDTQLAQRSLQ 396
Cdd:COG5077   511 KSMLDDLLNP----------VAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVR 558
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-338 7.82e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 56.91  E-value: 7.82e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568997588 274 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 338
Cdd:cd02674  174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV--------SSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-338 1.99e-07

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 53.92  E-value: 1.99e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568997588 274 YRLHAVLVHEGQANAGHYWAYIFDHRESrWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 338
Cdd:cd02660  273 YDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEVLK--------SQAYLLFYH 328
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
26-107 5.49e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 52.44  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588   26 GEIESLHSDNSGKSGQ---EHWFTELPPVLTFELSRFEFNQAlgRPEKIHNKLEFPQVLYLDRYMhrnreiTRIKREEIK 102
Cdd:pfam00443 178 DDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL------AEELKPKTN 249

                  ....*
gi 568997588  103 RLKDY 107
Cdd:pfam00443 250 NLQDY 254
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
274-318 1.53e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 50.57  E-value: 1.53e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568997588 274 YRLHAVLVHEGQANAGHYWAYIfdHRESRWMKYNDIAVTKSSWEE 318
Cdd:COG5533  225 YDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEE 267
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-337 6.47e-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 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: 48.87  E-value: 6.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568997588 274 YRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSfGGYRNASAYCLMY 337
Cdd:cd02657  241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-92 2.75e-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: 47.03  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588   2 FGQYPLQVNGFKDLHECLEAAMIEgeiESLHSDN--SGKSGQEH-------WFTELPPVLTFELSRFEFNQALGRPEKIH 72
Cdd:cd02668  145 FYELELQLKGHKTLEECIDEFLKE---EQLTGDNqyFCESCNSKtdatrriRLTTLPPTLNFQLLRFVFDRKTGAKKKLN 221
                         90       100
                 ....*....|....*....|
gi 568997588  73 NKLEFPQVLYLDRYMHRNRE 92
Cdd:cd02668  222 ASISFPEILDMGEYLAESDE 241
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
248-337 5.60e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 45.95  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 248 DLQESISRIHRTIELMYSDKS----------MIQVPYRLHAVLVHEG-QANAGHYWAYIFD------------------- 297
Cdd:cd02664  207 VLSLPVRVESKSSESPLEKKEeesgddgelvTRQVHYRLYAVVVHSGySSESGHYFTYARDqtdadstgqecpepkdaee 286
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568997588 298 -HRESRWMKYNDIAVTKSSWEElVRDSFGGYRNASAYCLMY 337
Cdd:cd02664  287 nDESKNWYLFNDSRVTFSSFES-VQNVTSRFPKDTPYILFY 326
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
265-338 9.86e-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: 45.34  E-value: 9.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568997588 265 SDKSMIQVPYRLHAVLVHEG-QANAGHYWAYIFDHREsRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 338
Cdd:cd02661  239 SQPNDGPLKYKLYAVLVHSGfSPHSGHYYCYVKSSNG-KWYNMDDSKVSPVSIETVL--------SQKAYILFYI 304
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-313 2.02e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 44.33  E-value: 2.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568997588 274 YRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTK 313
Cdd:cd02668  246 YELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
PHA03369 PHA03369
capsid maturational protease; Provisional
91-218 3.39e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 44.22  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  91 REITRIKREEIKRLKDYLTVLQ--------QRLERYLSYGSgpKRFPLVDVLQYALEFASSKpVCTSPVDDIDASSSASG 162
Cdd:PHA03369 292 PEWKTFYEALADQLNNLYKLLRtiykhkdeTVIEQYLIEGR--KLFSTINGLKAHNEILKTA-SLTAPSRVLAAAAKVAV 368
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568997588 163 PLPSQSLPSTTEQQGPCASDLPGSSSPASGAALPLRSVIHKPFTQSRIPPDLPMHP 218
Cdd:PHA03369 369 IAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSP 424
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
261-338 4.08e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 44.10  E-value: 4.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568997588 261 ELMYSDKSMIqvpYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 338
Cdd:COG5560  754 EYMVDDPRLI---YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT--------SSAYVLFYR 820
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
15-104 2.09e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 40.83  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588  15 LHECLEAAMIEGEIEsLHSDNSGKSGQEHWFTELPPVLTFELSRFeFNQALGRPEKIHNKLEFPQVLYLDRYMHRNREIT 94
Cdd:cd02667  117 LKQFTEVEILEGNNK-FACENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSS 194
                         90
                 ....*....|
gi 568997588  95 RIKREEIKRL 104
Cdd:cd02667  195 EDKSSVLYRL 204
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
6-84 4.34e-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: 40.05  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588   6 PLQVNGFKDLHECLEAAMIEgeiESLHSDN----SGKSGQEHW----FTELPPVLTFELSRFEFNQAlGRPEKIHNKLEF 77
Cdd:cd02660  169 ESGVSGTPTLSDCLDRFTRP---EKLGDFAykcsGCGSTQEATkqlsIKKLPPVLCFQLKRFEHSLN-KTSRKIDTYVQF 244

                 ....*..
gi 568997588  78 PqvLYLD 84
Cdd:cd02660  245 P--LELN 249
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-337 5.17e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 39.68  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997588 274 YRLHAVLVHEGQANAGHYWAYIFDHR---------------------ESRWMKYNDIAVTKSSWEELVRdsfggyrnASA 332
Cdd:cd02667  202 YRLYGVVEHSGTMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLK--------SEA 273

                 ....*
gi 568997588 333 YCLMY 337
Cdd:cd02667  274 YLLFY 278
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
47-87 6.23e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 39.57  E-value: 6.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568997588  47 ELPPVLTFELSRFEFNQAlgrpEKIHNKLEFPQVLYLDRYM 87
Cdd:cd02661  202 RAPNVLTIHLKRFSNFRG----GKINKQISFPETLDLSPYM 238
 
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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