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Conserved domains on  [gi|545688657|ref|NP_001269971|]
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ubiquitin carboxyl-terminal hydrolase 25 isoform USP25b [Homo sapiens]

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 ...
800-1080 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: 544.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  800 YDRCGPEAGFFKAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 879
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  880 QAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHY 959
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  960 RRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTD 1039
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 545688657 1040 FLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 1080
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-655 5.07e-104

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: 325.67  E-value: 5.07e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 249
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLF------------------------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNG 329
Cdd:cd02665    20 --------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  330 FKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnr 409
Cdd:cd02665    92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ------------ 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  410 eitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlps 489
Cdd:cd02665   158 --------IIQ--------------------------------------------------------------------- 160
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  490 tteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqes 569
Cdd:cd02665       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  570 isrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASA 649
Cdd:cd02665   161 ------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSA 222

                  ....*.
gi 545688657  650 YCLMYI 655
Cdd:cd02665   223 YCLMYI 228
UBA_UBP25 cd14354
UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; ...
15-60 2.36e-24

UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels.


:

Pssm-ID: 270539  Cd Length: 46  Bit Score: 96.70  E-value: 2.36e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 545688657   15 KHQQTFLNQLREITGINDTQILQQALKDSNGNLELAVAFLTAKNAK 60
Cdd:cd14354     1 KHQQTFLNQLREITGINDVQVLQQALKDSNGNLELAVAFLTAKNAK 46
 
Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
800-1080 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: 544.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  800 YDRCGPEAGFFKAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 879
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  880 QAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHY 959
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  960 RRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTD 1039
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 545688657 1040 FLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 1080
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-655 5.07e-104

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: 325.67  E-value: 5.07e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 249
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLF------------------------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNG 329
Cdd:cd02665    20 --------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  330 FKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnr 409
Cdd:cd02665    92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ------------ 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  410 eitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlps 489
Cdd:cd02665   158 --------IIQ--------------------------------------------------------------------- 160
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  490 tteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqes 569
Cdd:cd02665       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  570 isrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASA 649
Cdd:cd02665   161 ------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSA 222

                  ....*.
gi 545688657  650 YCLMYI 655
Cdd:cd02665   223 YCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
169-425 2.97e-30

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.17  E-value: 2.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657   169 VGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSnaqdlpRNQKEHRNLPFMRELRYLF-ALLVGTKRKYVDPSRAVE 247
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLS------EDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657   248 ILKDAFKS-NDSQQQDVSEFTHKLLDWLEDAFQMKAEEEtdeekPKNPMVELFYGRF------LAVGVlEGKKFEnTEMF 320
Cdd:pfam00443   75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFRGQLksrlkcLSCGE-VSETFE-PFSD 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657   321 GQYPLQVNG----FKDLHECLEAAMIE---GEIESLHSENSGKSGQ---EHWFTELPPVLTFELSRFEFNQAlgRPEKIH 390
Cdd:pfam00443  148 LSLPIPGDSaelkTASLQICFLQFSKLeelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLN 225
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 545688657   391 NKLEFPQVLYLDRYMhrnreiTRIKREEIKRLKDY 425
Cdd:pfam00443  226 TEVEFPLELDLSRYL------AEELKPKTNNLQDY 254
UBA_UBP25 cd14354
UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; ...
15-60 2.36e-24

UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels.


Pssm-ID: 270539  Cd Length: 46  Bit Score: 96.70  E-value: 2.36e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 545688657   15 KHQQTFLNQLREITGINDTQILQQALKDSNGNLELAVAFLTAKNAK 60
Cdd:cd14354     1 KHQQTFLNQLREITGINDVQVLQQALKDSNGNLELAVAFLTAKNAK 46
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
148-407 9.49e-13

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 72.98  E-value: 9.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  148 PTEVWRDSRNPYDRKRQdKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVlnYKPPSNAQDlPRN------QKEHRNLPF 221
Cdd:COG5077   174 PTGVLWHSFLNYNSKKE-TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTDHPR-GRDsvalalQRLFYNLQT 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  222 MRElrylfallvgtkrkyvdPSRAVEILKD-AFKSNDS-QQQDVSEFTHKLLDWLEDafQMKaeeetdEEKPKNPMVELF 299
Cdd:COG5077   250 GEE-----------------PVDTTELTRSfGWDSDDSfMQHDIQEFNRVLQDNLEK--SMR------GTVVENALNGIF 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  300 YGRFLAVGVLEGKKFEN--TEMFGQYPLQVNGFKDLHECLEAAMiegEIESLHSENSgKSGQEH---------WFTELPP 368
Cdd:COG5077   305 VGKMKSYIKCVNVNYESarVEDFWDIQLNVKGMKNLQESFRRYI---QVETLDGDNR-YNAEKHglqdakkgvIFESLPP 380
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 545688657  369 VLTFELSRFEFNQALGRPEKIHNKLEFPQVLYLDRYMHR 407
Cdd:COG5077   381 VLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419
 
Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
800-1080 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: 544.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  800 YDRCGPEAGFFKAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 879
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  880 QAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHY 959
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  960 RRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTD 1039
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 545688657 1040 FLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 1080
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
811-1080 3.90e-108

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: 338.50  E-value: 3.90e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  811 KAIKLEYARLVKLAQEDTP--PETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLsfDERCHNIMKVAQAKLEMIKP 888
Cdd:cd20485     3 EAIDEELDRLKSLARTLPSslPEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEELSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  889 EEVNLEEY-EEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSK-GLYRGHDEELISHYRRECLLK 966
Cdd:cd20485    81 KSDDIEKEyELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKgPPGKGLDEKLLAHYRRKCLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  967 LNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEmEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTDFLPKLLD 1046
Cdd:cd20485   161 LNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSASS-SEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKLLD 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 545688657 1047 CSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 1080
Cdd:cd20485   240 PSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
811-1082 1.30e-106

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: 334.50  E-value: 1.30e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  811 KAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVAQAKLEMIKPEE 890
Cdd:cd20487     3 KAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGPDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  891 VNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHYRRECLLKLNEQ 970
Cdd:cd20487    83 MDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELNDK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  971 AAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTDFLPKLLDCSME 1050
Cdd:cd20487   163 AASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCSTE 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 545688657 1051 IKSFHEPPKLPSYSTHELCERFARIMLSLSRT 1082
Cdd:cd20487   243 VIVLKEPPKIRPNSPHDLCSRFAAVMESIHGT 274
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-655 5.07e-104

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: 325.67  E-value: 5.07e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 249
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLF------------------------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNG 329
Cdd:cd02665    20 --------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  330 FKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnr 409
Cdd:cd02665    92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ------------ 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  410 eitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlps 489
Cdd:cd02665   158 --------IIQ--------------------------------------------------------------------- 160
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  490 tteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqes 569
Cdd:cd02665       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  570 isrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASA 649
Cdd:cd02665   161 ------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSA 222

                  ....*.
gi 545688657  650 YCLMYI 655
Cdd:cd02665   223 YCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
169-425 2.97e-30

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.17  E-value: 2.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657   169 VGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSnaqdlpRNQKEHRNLPFMRELRYLF-ALLVGTKRKYVDPSRAVE 247
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLS------EDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657   248 ILKDAFKS-NDSQQQDVSEFTHKLLDWLEDAFQMKAEEEtdeekPKNPMVELFYGRF------LAVGVlEGKKFEnTEMF 320
Cdd:pfam00443   75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFRGQLksrlkcLSCGE-VSETFE-PFSD 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657   321 GQYPLQVNG----FKDLHECLEAAMIE---GEIESLHSENSGKSGQ---EHWFTELPPVLTFELSRFEFNQAlgRPEKIH 390
Cdd:pfam00443  148 LSLPIPGDSaelkTASLQICFLQFSKLeelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLN 225
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 545688657   391 NKLEFPQVLYLDRYMhrnreiTRIKREEIKRLKDY 425
Cdd:pfam00443  226 TEVEFPLELDLSRYL------AEELKPKTNNLQDY 254
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
170-655 1.16e-29

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: 118.74  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 249
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENT----EMFGQYPL 325
Cdd:cd02257    20 --------SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVstepELFLSLPL 91
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  326 QVNGF--KDLHECLEAAMIEGEIE---SLHSENSGKSG--QEHWFTELPPVLTFELSRFEFNQAlGRPEKIHNKLEFPQV 398
Cdd:cd02257    92 PVKGLpqVSLEDCLEKFFKEEILEgdnCYKCEKKKKQEatKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  399 LYLDRYMhrnreitrikreeikrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidasspp 478
Cdd:cd02257   171 LDLSPYL------------------------------------------------------------------------- 177
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  479 sgsipsqtlpstteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrte 558
Cdd:cd02257       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  559 iendtrdlqesisrihrTIELMYSDKSMIQVPYRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELV 637
Cdd:cd02257   178 -----------------SEGEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVL 240
                         490
                  ....*....|....*...
gi 545688657  638 RDsfgGYRNASAYCLMYI 655
Cdd:cd02257   241 EF---GSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-410 4.62e-26

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: 110.20  E-value: 4.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNA-QDLPRNQKEHRNLPFMRELRYLFALLVGTKRKYVDPSRAVei 248
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  249 lkDAFKSNDSQQQDVSEFTHKLLDWLEDAFQmkaeeETDEEKPKNPMVELFYGRFLAVGVLE--GKKFENTEMFGQYPLQ 326
Cdd:cd02668    79 --KALGLDTGQQQDAQEFSKLFLSLLEAKLS-----KSKNPDLKNIVQDLFRGEYSYVTQCSkcGRESSLPSKFYELELQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  327 VNGFKDLHECLEAAMIEgeiESLHSEN--SGKSGQEH-------WFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQ 397
Cdd:cd02668   152 LKGHKTLEECIDEFLKE---EQLTGDNqyFCESCNSKtdatrriRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPE 228
                         250
                  ....*....|...
gi 545688657  398 VLYLDRYMHRNRE 410
Cdd:cd02668   229 ILDMGEYLAESDE 241
UBA_UBP25 cd14354
UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; ...
15-60 2.36e-24

UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels.


Pssm-ID: 270539  Cd Length: 46  Bit Score: 96.70  E-value: 2.36e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 545688657   15 KHQQTFLNQLREITGINDTQILQQALKDSNGNLELAVAFLTAKNAK 60
Cdd:cd14354     1 KHQQTFLNQLREITGINDVQVLQQALKDSNGNLELAVAFLTAKNAK 46
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
169-656 3.01e-23

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: 102.34  E-value: 3.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  169 VGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDlprnqKEHRNLPFMRelryLFALLVGTKRKYVDPSRAVEI 248
Cdd:cd02659     3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDD-----NKSVPLALQR----LFLFLQLSESPVKTTELTDKT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  249 LKDAFKSNDS-QQQDVSEFTHKLLDWLEDafQMKAEEEtdeekpKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQV 327
Cdd:cd02659    74 RSFGWDSLNTfEQHDVQEFFRVLFDKLEE--KLKGTGQ------EGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  328 N--GFKDLHECLEAaMIEGEI----ESLHSENSGKSGQEH---WFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQV 398
Cdd:cd02659   146 AvkGKKNLEESLDA-YVQGETlegdNKYFCEKCGKKVDAEkgvCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  399 LYLDRYMHRNREitriKREEIKRLKDYltvlqqrlERYLsygsgpkrfplvdvlqyalefasskpvctspvddidasspp 478
Cdd:cd02659   225 LDMEPYTEKGLA----KKEGDSEKKDS--------ESYI----------------------------------------- 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  479 sgsipsqtlpstteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrte 558
Cdd:cd02659       --------------------------------------------------------------------------------
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  559 iendtrdlqesisrihrtielmysdksmiqvpYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVR 638
Cdd:cd02659   252 --------------------------------YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEE 299
                         490       500       510
                  ....*....|....*....|....*....|..
gi 545688657  639 DSFGGY--------------RNASAYCLMYIN 656
Cdd:cd02659   300 ECFGGEetqktydsgprafkRTTNAYMLFYER 331
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
168-655 9.14e-20

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: 92.17  E-value: 9.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  168 PVGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPP--SNAQDLP----------RNQKEHRNLPFMRELRYLFALLVGT 235
Cdd:cd02666     1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaELASDYPterriggrevSRSELQRSNQFVYELRSLFNDLIHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  236 KRKYVDPSRAVEILkdAFKsndsqQQDVSEFTHKLLdwledaFQMKAEEETDEEKPKNPMVELFygrflavgvlegkkfe 315
Cdd:cd02666    81 NTRSVTPSKELAYL--ALR-----QQDVTECIDNVL------FQLEVALEPISNAFAGPDTEDD---------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  316 ntemfgqyPLQVNGFKDLHECLEAAMIEGEIESlhSENSGKSGQEHWFTELPPVltfelsrfefnqalGRPEKIHNKLEF 395
Cdd:cd02666   132 --------KEQSDLIKRLFSGKTKQQLVPESMG--NQPSVRTKTERFLSLLVDV--------------GKKGREIVVLLE 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  396 PQVLY--LDRYMHRnreitrikreeikrlkDYLTVLQQRLErylsygsgpkrfplvdvlqyalEFASSKPVCTSPVDDID 473
Cdd:cd02666   188 PKDLYdaLDRYFDY----------------DSLTKLPQRSQ----------------------VQAQLAQPLQRELISMD 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  474 assppsgsipsqtlpsTTEQqgalsselpstsPSSVAAISSrsvihkpftqsrippdlpmhpAPRHITEEELSVLEsclh 553
Cdd:cd02666   230 ----------------RYEL------------PSSIDDIDE---------------------LIREAIQSESSLVR---- 256
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  554 rwrtEIENDTRDLQESISRIhrtielmYSDksMIQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSW 633
Cdd:cd02666   257 ----QAQNELAELKHEIEKQ-------FDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPA 323
                         490       500
                  ....*....|....*....|..
gi 545688657  634 EELVRDSFGGyrNASAYCLMYI 655
Cdd:cd02666   324 SEVFLFTLGN--TATPYFLVYV 343
UBA_UBP25_like cd14276
UBA domain found in ubiquitin carboxyl-terminal hydrolase UBP25, UBP28, and similar proteins; ...
19-56 2.01e-14

UBA domain found in ubiquitin carboxyl-terminal hydrolase UBP25, UBP28, and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels. UBP28, also called deubiquitinating enzyme 28, ubiquitin thioesterase 28, or ubiquitin-specific-processing protease 28, is also an ubiquitin-specific protease belonging to the DUB family. UBP28 can form a ternary complex with nucleoplasmic Fbw7alpha, an F-box protein that is part of an SCF-type ubiquitin ligase, and MYC, a transcription factor encoded by MYC proto-oncogene. UBP28 is required for the stability of MYC, and this stabilization is necessary for tumour-cell proliferation. Besides, UBP28 plays a critical role in the regulation of the Chk2-p53-PUMA pathway. It specifically interacts with 53BP1 and is essential to stabilize Chk2 and 53BP1 in response to DNA damage.


Pssm-ID: 270462  Cd Length: 38  Bit Score: 67.83  E-value: 2.01e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 545688657   19 TFLNQLREITGINDTQILQQALKDSNGNLELAVAFLTA 56
Cdd:cd14276     1 QLINQLKEITGIQDPQILQQALEASNGDLTQAVSLLTE 38
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-401 3.98e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 71.75  E-value: 3.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDlprnqkehrnLPFMRELRYLFALLVGTKRKYVDPSRAV--E 247
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDS----------QSVMKKLQLLQAHLMHTQRRAEAPPDYFleA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  248 ILKDAFksNDSQQQDVSEFTHKLLDWLedafqmkaeeetdeekpkNPMVELFYGRFLAVGVL---EGKKFENTEMFGQYP 324
Cdd:cd02664    71 SRPPWF--TPGSQQDCSEYLRYLLDRL------------------HTLIEKMFGGKLSTTIRclnCNSTSARTERFRDLD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  325 LQVNGFKDLHECLEAAmiegeiESLHSEN-----SGKSGQ----EHWFTELPPVLTFELSRFEFNQALGRPEKIHNKLEF 395
Cdd:cd02664   131 LSFPSVQDLLNYFLSP------EKLTGDNqyyceKCASLQdaekEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSI 204

                  ....*.
gi 545688657  396 PQVLYL 401
Cdd:cd02664   205 NEVLSL 210
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
148-407 9.49e-13

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 72.98  E-value: 9.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  148 PTEVWRDSRNPYDRKRQdKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVlnYKPPSNAQDlPRN------QKEHRNLPF 221
Cdd:COG5077   174 PTGVLWHSFLNYNSKKE-TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTDHPR-GRDsvalalQRLFYNLQT 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  222 MRElrylfallvgtkrkyvdPSRAVEILKD-AFKSNDS-QQQDVSEFTHKLLDWLEDafQMKaeeetdEEKPKNPMVELF 299
Cdd:COG5077   250 GEE-----------------PVDTTELTRSfGWDSDDSfMQHDIQEFNRVLQDNLEK--SMR------GTVVENALNGIF 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  300 YGRFLAVGVLEGKKFEN--TEMFGQYPLQVNGFKDLHECLEAAMiegEIESLHSENSgKSGQEH---------WFTELPP 368
Cdd:COG5077   305 VGKMKSYIKCVNVNYESarVEDFWDIQLNVKGMKNLQESFRRYI---QVETLDGDNR-YNAEKHglqdakkgvIFESLPP 380
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 545688657  369 VLTFELSRFEFNQALGRPEKIHNKLEFPQVLYLDRYMHR 407
Cdd:COG5077   381 VLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-399 3.82e-11

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: 65.43  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPpsnaqdlPRNQKEHRNLPFMRELRYLFALLvGTKRKYVDPSRAVEIL 249
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP-------ARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 KDAF-----KSNDSQ--QQDVSE--------FTHKLL------DWLEDAFQMKAEE---ETDEEKPKNPMVELFYgrFLa 305
Cdd:cd02657    73 RMAFpqfaeKQNQGGyaQQDAEEcwsqllsvLSQKLPgagskgSFIDQLFGIELETkmkCTESPDEEEVSTESEY--KL- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  306 vgvlegkkfeNTEMFGQypLQVNGfkdLHECLEAAMiEGEIEsLHSENSGKSGQ---EHWFTELPPVLTFELSRFEFNQA 382
Cdd:cd02657   150 ----------QCHISIT--TEVNY---LQDGLKKGL-EEEIE-KHSPTLGRDAIytkTSRISRLPKYLTVQFVRFFWKRD 212
                         250
                  ....*....|....*..
gi 545688657  383 LGRPEKIHNKLEFPQVL 399
Cdd:cd02657   213 IQKKAKILRKVKFPFEL 229
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
168-405 7.55e-10

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 61.52  E-value: 7.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  168 PVGLKNVGNTCWFSAVIQSlfnllefrrlvLNYKPPSnAQDLPR----NQKEHRNLPFMRELRYLFALLVGTKRKYVDPS 243
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQC-----------LTHTPPL-ANYLLSrehsKDCCNEGFCMMCALEAHVERALASSGPGSAPR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  244 RAVEILKdAFKSN--DSQQQDVSEFTHKLLDWLEDA--FQMKAEEETDEE-KPKNPMVELFYGRFLA-VGVLEGKKFENT 317
Cdd:cd02661    69 IFSSNLK-QISKHfrIGRQEDAHEFLRYLLDAMQKAclDRFKKLKAVDPSsQETTLVQQIFGGYLRSqVKCLNCKHVSNT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  318 -EMFGQYPLQVNGFKDLHECLEAAMiegEIESLHSEN-------SGKSGQEHWFT--ELPPVLTFELSRFEFNQAlgrpE 387
Cdd:cd02661   148 yDPFLDLSLDIKGADSLEDALEQFT---KPEQLDGENkykcercKKKVKASKQLTihRAPNVLTIHLKRFSNFRG----G 220
                         250
                  ....*....|....*...
gi 545688657  388 KIHNKLEFPQVLYLDRYM 405
Cdd:cd02661   221 KINKQISFPETLDLSPYM 238
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-422 8.66e-10

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 60.86  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFnLLEFRRLVLNYKPpsnaqdlprnqkehrnlpfmrelRYLFAllvgtkrkyvdpsravEIL 249
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSETP-----------------------KELFS----------------QVC 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 KDAFKSNDSQQQDVSEFTHKLLDWLedafqmkaeeetdeekpkNPMVELFYGRFLAVGV--LEGKKFENT-EMFGQYPLQ 326
Cdd:cd02667    41 RKAPQFKGYQQQDSHELLRYLLDGL------------------RTFIDSIFGGELTSTImcESCGTVSLVyEPFLDLSLP 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  327 V----NGFKDLHECL----EAAMIEGEIEsLHSENSGKSGQEHWFTELPPVLTFELSRFeFNQALGRPEKIHNKLEFPQV 398
Cdd:cd02667   103 RsdeiKSECSIESCLkqftEVEILEGNNK-FACENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSFPEI 180
                         250       260
                  ....*....|....*....|....
gi 545688657  399 LYLDRYMHRNREITRIKREEIKRL 422
Cdd:cd02667   181 LDLAPFCDPKCNSSEDKSSVLYRL 204
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
591-655 1.30e-08

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 56.53  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545688657  591 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 655
Cdd:cd02674   174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV--------SSSAYILFYE 230
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
170-394 2.14e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.73  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSL-FNLLEFRRLVL-NYKPPSNAQDLPRNQKEHRNLpfmRELRYLFALLVGTKRkyvdpsrave 247
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDdLSKELKVLKNVIRKPEPDLNQ---EEALKLFTALWSSKE---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  248 iLKDAFKSNDSQQQDVSEFTHKLLDWLEdaFQMKAEEETDEEKPKNPMVELFYGRFLAVGV--LEGKKFENTEMFGQYPL 325
Cdd:COG5533    68 -HKVGWIPPMGSQEDAHELLGKLLDELK--LDLVNSFTIRIFKTTKDKKKTSTGDWFDIIIelPDQTWVNNLKTLQEFID 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  326 QVNGFKDlheclEAAMI-EGEIESLHSENsgKSGQEHWFTELPPVLTFELSRFEFNqalGRPEKIHNKLE 394
Cdd:COG5533   145 NMEELVD-----DETGVkAKENEELEVQA--KQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD 204
UBA_UBP28 cd14355
UBA domain found in ubiquitin carboxyl-terminal hydrolase 28 (UBP28) and similar proteins; ...
21-60 2.16e-08

UBA domain found in ubiquitin carboxyl-terminal hydrolase 28 (UBP28) and similar proteins; UBP28, also called deubiquitinating enzyme 28, ubiquitin thioesterase 28, or ubiquitin-specific-processing protease 28, is an ubiquitin-specific protease that belongs to the deubiquitinating enzyme (DUB) family which specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. UBP28 can form a ternary complex with nucleoplasmic Fbw7alpha, an F-box protein that is part of an SCF-type ubiquitin ligase, and MYC, a transcription factor encoded by MYC proto-oncogene. UBP28 is required for the stability of MYC, and this stabilization is necessary for tumour-cell proliferation. Besides, UBP28 plays a critical role in the regulation of the Chk2-p53-PUMA pathway. It specifically interacts with 53BP1 and is essential to stabilize Chk2 and 53BP1 in response to DNA damage.


Pssm-ID: 270540  Cd Length: 42  Bit Score: 51.01  E-value: 2.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 545688657   21 LNQLREITGINDTQILQQALKDSNGNLELAVAFLTAKNAK 60
Cdd:cd14355     3 LNQLREITGIQDPDFLHEALKAANGNLTQAVGVLTEERDK 42
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
591-655 2.62e-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: 2.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545688657  591 YRLHAVLVHEGQANAGHYWAYIFDHRESrWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 655
Cdd:cd02660   273 YDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEVLK--------SQAYLLFYH 328
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-399 5.70e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 52.71  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQ-DLPRNQKEHRnlpfMRELRYlfALLVGtkrKYVDPSRAVE- 247
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvVDPANDLNCQ----LIKLAD--GLLSG---RYSKPASLKSe 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  248 -------ILKDAFKS---------NDSQQQDVSEFTHKLLDWLEDAFQMKAEeetdeekpKNPmVELFygRFLAVGVLEG 311
Cdd:cd02658    72 ndpyqvgIKPSMFKAligkghpefSTMRQQDALEFLLHLIDKLDRESFKNLG--------LNP-NDLF--KFMIEDRLEC 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  312 KKFE--NTEMFGQYPLQVNGFKD----------------LHECLEAAMIEGEIESLHSENSGKSG--QEHWFTELPPVLT 371
Cdd:cd02658   141 LSCKkvKYTSELSEILSLPVPKDeatekeegelvyepvpLEDCLKAYFAPETIEDFCSTCKEKTTatKTTGFKTFPDYLV 220
                         250       260
                  ....*....|....*....|....*...
gi 545688657  372 FELSRFEFNQAlGRPEKIHNKLEFPQVL 399
Cdd:cd02658   221 INMKRFQLLEN-WVPKKLDVPIDVPEEL 247
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
591-635 5.07e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 49.42  E-value: 5.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 545688657  591 YRLHAVLVHEGQANAGHYWAYIfdHRESRWMKYNDIAVTKSSWEE 635
Cdd:COG5533   225 YDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEE 267
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-402 5.71e-06

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 49.68  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNykppsnaqdlprnQKEHRNLPFMR-------ELRYLFALLVGTKRKyvDP 242
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLS-------------DRHSCTCLSCSpnsclscAMDEIFQEFYYSGDR--SP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  243 SRAVEILKDAFKSNDS----QQQDVSEFTHKLLDwledafQMKAEEETDEEKPKNPMV------ELFYGRFLAVGVLEGK 312
Cdd:cd02660    67 YGPINLLYLSWKHSRNlagySQQDAHEFFQFLLD------QLHTHYGGDKNEANDESHcnciihQTFSGSLQSSVTCQRC 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  313 KFENT-----------------EMFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSENSG-KSGQEHW----FTELPPVL 370
Cdd:cd02660   141 GGVSTtvdpfldlsldipnkstPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFAYKCSGcGSTQEATkqlsIKKLPPVL 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 545688657  371 TFELSRFEFNQAlGRPEKIHNKLEFPqvLYLD 402
Cdd:cd02660   221 CFQLKRFEHSLN-KTSRKIDTYVQFP--LELN 249
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-401 6.39e-06

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 49.23  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNLlefrrlvlnykppsnaqdlprnqkehrNLpfMRELRYLFALLVGTKRKY--VDPSRAVE 247
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFE---------------------------NL--LTCLKDLFESISEQKKRTgvISPKKFIT 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  248 ILKDAFKS-NDSQQQDVSEFTHKLL----DWLEDAFQMKAEEETDEEKPKNPMV-----ELFYG------RFLAVGVLEG 311
Cdd:cd02663    52 RLKRENELfDNYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNNNNNAEPQptwvhEIFQGiltnetRCLTCETVSS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  312 KKfentEMFGQYPLQVNGFKDLHECLEAAmieGEIESLHSEN-----SGKSGQEHW----FTELPPVLTFELSRFEFNQA 382
Cdd:cd02663   132 RD----ETFLDLSIDVEQNTSITSCLRQF---SATETLCGRNkfycdECCSLQEAEkrmkIKKLPKILALHLKRFKYDEQ 204
                         250
                  ....*....|....*....
gi 545688657  383 LGRPEKIHNKLEFPQVLYL 401
Cdd:cd02663   205 LNRYIKLFYRVVFPLELRL 223
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
591-654 1.38e-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 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: 48.48  E-value: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545688657  591 YRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSfGGYRNASAYCLMY 654
Cdd:cd02657   241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
582-655 1.28e-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: 45.34  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545688657  582 SDKSMIQVPYRLHAVLVHEG-QANAGHYWAYIFDHREsRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 655
Cdd:cd02661   239 SQPNDGPLKYKLYAVLVHSGfSPHSGHYYCYVKSSNG-KWYNMDDSKVSPVSIETVL--------SQKAYILFYI 304
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
259-400 5.60e-04

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 42.74  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  259 QQQDVSEFTHKLLDWLEDafqmkaeeetdeeKPKNPmvelFYGRF------LAVGVLEGKKFENtemFGQYPLQVNGFKD 332
Cdd:cd02662    33 EQQDAHELFQVLLETLEQ-------------LLKFP----FDGLLasrivcLQCGESSKVRYES---FTMLSLPVPNQSS 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545688657  333 LHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFN---QALGRPEKIHNKLEFPQVLY 400
Cdd:cd02662    93 GSGTTLEHCLDDFLSTEIIDDYKCDRCQTVIVRLPQILCIHLSRSVFDgrgTSTKNSCKVSFPERLPKVLY 163
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
578-655 6.40e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.72  E-value: 6.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545688657  578 ELMYSDKSMIqvpYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 655
Cdd:COG5560   754 EYMVDDPRLI---YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT--------SSAYVLFYR 820
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
170-396 2.47e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 40.73  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  170 GLKNVGNTCWFSAVIQSLFNllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 249
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  250 kdafksndsQQQDVSEFTHKLLDWLE----DAF--QMKAEEETDEEKPKNPMVELFYgrFLAVGVLEGKKFENTEMfgqy 323
Cdd:cd02674    21 ---------DQQDAQEFLLFLLDGLHsiivDLFqgQLKSRLTCLTCGKTSTTFEPFT--YLSLPIPSGSGDAPKVT---- 85
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  324 plqvngfkdLHECLEaamiegeiESLHSENSGKSGQEHW--------------FTELPPVLTFELSRFEFNQalGRPEKI 389
Cdd:cd02674    86 ---------LEDCLR--------LFTKEETLDGDNAWKCpkckkkrkatkkltISRLPKVLIIHLKRFSFSR--GSTRKL 146

                  ....*..
gi 545688657  390 HNKLEFP 396
Cdd:cd02674   147 TTPVTFP 153
UBA_like_SF cd00194
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
24-52 6.71e-03

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


Pssm-ID: 270455  Cd Length: 28  Bit Score: 35.08  E-value: 6.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 545688657   24 LREITGiNDTQILQQALKDSNGNLELAVA 52
Cdd:cd00194     1 LVDITG-ASQEEAQQALEACGGNLNIAAN 28
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
591-654 7.59e-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: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688657  591 YRLHAVLVHEGQANAGHYWAYIFDHR---------------------ESRWMKYNDIAVTKSSWEELVRdsfggyrnASA 649
Cdd:cd02667   202 YRLYGVVEHSGTMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLK--------SEA 273

                  ....*
gi 545688657  650 YCLMY 654
Cdd:cd02667   274 YLLFY 278
 
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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