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Conserved domains on  [gi|1917984019|ref|NP_001375228|]
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ubiquitin carboxyl-terminal hydrolase 25 isoform 4 [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 ...
 547-827 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: 534.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 547 HEDKSPETVLQSAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 626
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 627 QAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHY 706
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 707 RRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTD 786
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1917984019 787 FLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 827
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 37-434 1.15e-99

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: 308.72  E-value: 1.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  37 SQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNGFKDLHECL 116
Cdd:cd02665    20 SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 117 EAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnreitrikre 196
Cdd:cd02665   100 EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ-------------------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 197 EIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlpstteqqgal 276
Cdd:cd02665   158 IIQ----------------------------------------------------------------------------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 277 sselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqesisrihrti 356
Cdd:cd02665       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917984019 357 elmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASAYCLMYI 434
Cdd:cd02665   161 ----------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
 
Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
 547-827 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: 534.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 547 HEDKSPETVLQSAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 626
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 627 QAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHY 706
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 707 RRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTD 786
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1917984019 787 FLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 827
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 37-434 1.15e-99

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: 308.72  E-value: 1.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  37 SQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNGFKDLHECL 116
Cdd:cd02665    20 SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 117 EAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnreitrikre 196
Cdd:cd02665   100 EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ-------------------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 197 EIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlpstteqqgal 276
Cdd:cd02665   158 IIQ----------------------------------------------------------------------------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 277 sselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqesisrihrti 356
Cdd:cd02665       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917984019 357 elmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASAYCLMYI 434
Cdd:cd02665   161 ----------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
2-204 2.26e-15

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 77.87  E-value: 2.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019   2 RELRYLF-ALLVGTKRKYVDPSRAVEILKDAFKS-NDSQQQDVSEFTHKLLDWLEDAFQMKAEEEtdeekPKNPMVELFY 79
Cdd:pfam00443  49 CALRDLFkALQKNSKSSSVSPKMFKKSLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  80 GRF------LAVGVlEGKKFEnTEMFGQYPLQVNG----FKDLHECLEAAMIE---GEIESLHSENSGKSGQ---EHWFT 143
Cdd:pfam00443 124 GQLksrlkcLSCGE-VSETFE-PFSDLSLPIPGDSaelkTASLQICFLQFSKLeelDDEEKYYCDKCGCKQDaikQLKIS 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917984019 144 ELPPVLTFELSRFEFNQAlgRPEKIHNKLEFPQVLYLDRYMhrnreiTRIKREEIKRLKDY 204
Cdd:pfam00443 202 RLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL------AEELKPKTNNLQDY 254
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 370-486 3.52e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 63.74  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  370 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGG--------------YRNASAYCLMYI- 434
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1917984019  435 NDKAQFLIQEefnketgqplVGIETLPPDLRDFVEEDNQRFE-KELEEWDAQL 486
Cdd:COG5077    511 KSMLDDLLNP----------VAAVDIPPHVEEVLSEEIDKTEvRCKEIDEIHL 553
 
Name Accession Description Interval E-value
USP25_C cd20486
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ...
 547-827 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: 534.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 547 HEDKSPETVLQSAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVA 626
Cdd:cd20486     1 HEDKGPEAVLQSAIKLEYARLVKLAQEDTPPENDYRLQHVVVYFIQNQAPKKIIERTLLEQFADRNLSFDERCHNIMKVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 627 QAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHY 706
Cdd:cd20486    81 QAKLEMIKPDEVNMEEYERWHQDYRKFRETTMYLLIGLELFQKKSYVEALLYLIYAYQYNKELLSKGPYRGHDEELISHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 707 RRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTD 786
Cdd:cd20486   161 RRECLLKLNEQAAALFESGDDREVNNGLIIMNELIVPCLPLLLVDEMEEKDIVAVEDMRNRWCSYLGQEMEPNLQEKLTD 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1917984019 787 FLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 827
Cdd:cd20486   241 FLPKLLDCSTEIKSFHDPPKLPSYSTHELCERFARIMLSLS 281
USP25_USP28_C-like cd20485
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ...
 556-827 1.02e-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: 334.26  E-value: 1.02e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 556 LQSAIKLEYARLVKLAQEDTP--PETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLsfDERCHNIMKVAQAKLEMI 633
Cdd:cd20485     1 LTEAIDEELDRLKSLARTLPSslPEEDPRLQHIVVYLIANKAPKNVIERALLEQFADCRL--DERYSRLKKLAQEKLEEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 634 KPEEVNLEEY-EEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSK-GLYRGHDEELISHYRRECL 711
Cdd:cd20485    79 SIKSDDIEKEyELWHEKYHQFRKVVFHFVLGVELYHQEKYEEALPYFVHAYLLNSKLLAKgPPGKGLDEKLLAHYRRKCL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 712 LKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEmEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTDFLPKL 791
Cdd:cd20485   159 LKLNEQAASLFESGDDEDVSEGLTIMNELIVPCLSLLSASS-SEEDLAAVEEIRNKWCSYLGQDLDEDKQEKLQDFLSKL 237

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1917984019 792 LDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLS 827
Cdd:cd20485   238 LDPSSEIRSIKEPPAVRPNSLSDLCERYTAVMNSVS 273
USP28_C cd20487
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ...
 556-829 3.17e-107

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: 330.65  E-value: 3.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 556 LQSAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVAQAKLEMIKP 635
Cdd:cd20487     1 LIKAFHEEYSRLYQLSKEEPTPQNDPRLQHVLVYFFQNEAPKRVIERTLLEQFADKNLSYDERSISIMKVARAKLRLIGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 636 EEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHYRRECLLKLN 715
Cdd:cd20487    81 DDMDMEEYKKWHEDYSLFRKVSVYLLTGLELYQNGKYQEALTYLVYAYQSNTTLLKKGEKRGVEESLIALYRRKCLLELN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 716 EQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTDFLPKLLDCS 795
Cdd:cd20487   161 DKAASLFESGEESGVAEGISIMNELIIPCMHLIINNDISKEDLDAIEVMRNHWCSYLGQDIDDTLQLKLGEFLPRLLDCS 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1917984019 796 MEIKSFHEPPKLPSYSTHELCERFARIMLSLSRT 829
Cdd:cd20487   241 TEVIVLKEPPKIRPNSPHDLCSRFAAVMESIHGT 274
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 37-434 1.15e-99

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: 308.72  E-value: 1.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  37 SQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNGFKDLHECL 116
Cdd:cd02665    20 SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 117 EAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnreitrikre 196
Cdd:cd02665   100 EAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ-------------------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 197 EIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlpstteqqgal 276
Cdd:cd02665   158 IIQ----------------------------------------------------------------------------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 277 sselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqesisrihrti 356
Cdd:cd02665       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917984019 357 elmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASAYCLMYI 434
Cdd:cd02665   161 ----------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSAYCLMYI 228
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 37-434 5.93e-27

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: 110.65  E-value: 5.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  37 SQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENT----EMFGQYPLQVNGF--K 110
Cdd:cd02257    20 SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVstepELFLSLPLPVKGLpqV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 111 DLHECLEAAMIEGEIE---SLHSENSGKSG--QEHWFTELPPVLTFELSRFEFNQAlGRPEKIHNKLEFPQVLYLDRYMh 185
Cdd:cd02257   100 SLEDCLEKFFKEEILEgdnCYKCEKKKKQEatKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYL- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 186 rnreitrikreeikrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqt 265
Cdd:cd02257       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 266 lpstteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdl 345
Cdd:cd02257       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 346 qesisrihrTIELMYSDKSMIQVPYRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDsfgGYR 424
Cdd:cd02257   178 ---------SEGEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF---GSL 245

                         410
                  ....*....|
gi 1917984019 425 NASAYCLMYI 434
Cdd:cd02257   246 SSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 3-189 3.97e-16

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 80.54  E-value: 3.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019   3 ELRYLFALLVGTKRKYVDPSRAVeilkDAFKSNDSQQQDVSEFTHKLLDWLEDAFQmkaeeETDEEKPKNPMVELFYGRF 82
Cdd:cd02668    56 QLQLIFAQLQFGNRSVVDPSGFV----KALGLDTGQQQDAQEFSKLFLSLLEAKLS-----KSKNPDLKNIVQDLFRGEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  83 LAVGVLE--GKKFENTEMFGQYPLQVNGFKDLHECLEAAMIEgeiESLHSEN--SGKSGQEH-------WFTELPPVLTF 151
Cdd:cd02668   127 SYVTQCSkcGRESSLPSKFYELELQLKGHKTLEECIDEFLKE---EQLTGDNqyFCESCNSKtdatrriRLTTLPPTLNF 203

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1917984019 152 ELSRFEFNQALGRPEKIHNKLEFPQVLYLDRYMHRNRE 189
Cdd:cd02668   204 QLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESDE 241
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
2-204 2.26e-15

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 77.87  E-value: 2.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019   2 RELRYLF-ALLVGTKRKYVDPSRAVEILKDAFKS-NDSQQQDVSEFTHKLLDWLEDAFQMKAEEEtdeekPKNPMVELFY 79
Cdd:pfam00443  49 CALRDLFkALQKNSKSSSVSPKMFKKSLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  80 GRF------LAVGVlEGKKFEnTEMFGQYPLQVNG----FKDLHECLEAAMIE---GEIESLHSENSGKSGQ---EHWFT 143
Cdd:pfam00443 124 GQLksrlkcLSCGE-VSETFE-PFSDLSLPIPGDSaelkTASLQICFLQFSKLeelDDEEKYYCDKCGCKQDaikQLKIS 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917984019 144 ELPPVLTFELSRFEFNQAlgRPEKIHNKLEFPQVLYLDRYMhrnreiTRIKREEIKRLKDY 204
Cdd:pfam00443 202 RLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLELDLSRYL------AEELKPKTNNLQDY 254
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 331-434 9.21e-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: 76.38  E-value: 9.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 331 LHRWRTEIEND-TRDLQESISRIHRTIELMYSDksMIQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTK 409
Cdd:cd02666   243 LIREAIQSESSlVRQAQNELAELKHEIEKQFDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTV 320

                          90       100
                  ....*....|....*....|....*
gi 1917984019 410 SSWEELVRDSFGGyrNASAYCLMYI 434
Cdd:cd02666   321 VPASEVFLFTLGN--TATPYFLVYV 343
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-435 2.62e-14

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: 74.99  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 370 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGY--------------RNASAYCLMYIN 435
Cdd:cd02659   252 YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEetqktydsgprafkRTTNAYMLFYER 331
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 370-486 3.52e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 63.74  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  370 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGG--------------YRNASAYCLMYI- 434
Cdd:COG5077    431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1917984019  435 NDKAQFLIQEefnketgqplVGIETLPPDLRDFVEEDNQRFE-KELEEWDAQL 486
Cdd:COG5077    511 KSMLDDLLNP----------VAAVDIPPHVEEVLSEEIDKTEvRCKEIDEIHL 553
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-434 1.09e-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: 1.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917984019 370 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 434
Cdd:cd02674   174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV--------SSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-434 2.41e-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: 53.53  E-value: 2.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917984019 370 YRLHAVLVHEGQANAGHYWAYIFDHRESrWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 434
Cdd:cd02660   273 YDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEVLK--------SQAYLLFYH 328
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
370-414 3.56e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 49.42  E-value: 3.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1917984019 370 YRLHAVLVHEGQANAGHYWAYIfdHRESRWMKYNDIAVTKSSWEE 414
Cdd:COG5533   225 YDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEE 267
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-433 1.16e-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: 48.10  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917984019 370 YRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSfGGYRNASAYCLMY 433
Cdd:cd02657   241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 35-201 3.32e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 46.61  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  35 NDSQQQDVSEFTHKLLDWLedafqmkaeeetdeekpkNPMVELFYGRFLAVGV--LEGKKFENT-EMFGQYPLQV----N 107
Cdd:cd02667    47 KGYQQQDSHELLRYLLDGL------------------RTFIDSIFGGELTSTImcESCGTVSLVyEPFLDLSLPRsdeiK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 108 GFKDLHECL----EAAMIEGEIEsLHSENSGKSGQEHWFTELPPVLTFELSRFeFNQALGRPEKIHNKLEFPQVLYLDRY 183
Cdd:cd02667   109 SECSIESCLkqftEVEILEGNNK-FACENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSFPEILDLAPF 186

                         170
                  ....*....|....*...
gi 1917984019 184 MHRNREITRIKREEIKRL 201
Cdd:cd02667   187 CDPKCNSSEDKSSVLYRL 204
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 344-433 9.93e-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: 45.18  E-value: 9.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 344 DLQESISRIHRTIELMYSDKS----------MIQVPYRLHAVLVHEG-QANAGHYWAYIFD------------------- 393
Cdd:cd02664   207 VLSLPVRVESKSSESPLEKKEeesgddgelvTRQVHYRLYAVVVHSGySSESGHYFTYARDqtdadstgqecpepkdaee 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1917984019 394 -HRESRWMKYNDIAVTKSSWEElVRDSFGGYRNASAYCLMY 433
Cdd:cd02664   287 nDESKNWYLFNDSRVTFSSFES-VQNVTSRFPKDTPYILFY 326
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 361-434 1.16e-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: 44.96  E-value: 1.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917984019 361 SDKSMIQVPYRLHAVLVHEG-QANAGHYWAYIFDHREsRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 434
Cdd:cd02661   239 SQPNDGPLKYKLYAVLVHSGfSPHSGHYYCYVKSSNG-KWYNMDDSKVSPVSIETVL--------SQKAYILFYI 304
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
357-434 6.76e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.33  E-value: 6.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917984019 357 ELMYSDKSMIqvpYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 434
Cdd:COG5560   754 EYMVDDPRLI---YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT--------SSAYVLFYR 820
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-179 6.97e-04

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.97  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  38 QQQDVSEFTHKLLDWLEDafqmkaeeetdeeKPKNPmvelFYGRF------LAVGVLEGKKFENtemFGQYPLQVNGFKD 111
Cdd:cd02662    33 EQQDAHELFQVLLETLEQ-------------LLKFP----FDGLLasrivcLQCGESSKVRYES---FTMLSLPVPNQSS 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917984019 112 LHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFN---QALGRPEKIHNKLEFPQVLY 179
Cdd:cd02662    93 GSGTTLEHCLDDFLSTEIIDDYKCDRCQTVIVRLPQILCIHLSRSVFDgrgTSTKNSCKVSFPERLPKVLY 163
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 103-181 2.08e-03

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 41.20  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 103 PLQVNGFKDLHECLEAAMIEGEIESLHSENSG-KSGQEHW----FTELPPVLTFELSRFEFNQAlGRPEKIHNKLEFPqv 177
Cdd:cd02660   169 ESGVSGTPTLSDCLDRFTRPEKLGDFAYKCSGcGSTQEATkqlsIKKLPPVLCFQLKRFEHSLN-KTSRKIDTYVQFP-- 245


                  ....
gi 1917984019 178 LYLD 181
Cdd:cd02660   246 LELN 249
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-184 2.29e-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: 41.11  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  38 QQQDVSEFTHKLLDWLEDA--FQMKAEEETDEE-KPKNPMVELFYGRFLA-VGVLEGKKFENT-EMFGQYPLQVNGFKDL 112
Cdd:cd02661    85 RQEDAHEFLRYLLDAMQKAclDRFKKLKAVDPSsQETTLVQQIFGGYLRSqVKCLNCKHVSNTyDPFLDLSLDIKGADSL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 113 HECLEAAMiegEIESLHSEN-------SGKSGQEHWFT--ELPPVLTFELSRFEFNQAlgrpEKIHNKLEFPQVLYLDRY 183
Cdd:cd02661   165 EDALEQFT---KPEQLDGENkykcercKKKVKASKQLTihRAPNVLTIHLKRFSNFRG----GKINKQISFPETLDLSPY 237


                  .
gi 1917984019 184 M 184
Cdd:cd02661   238 M 238
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 39-186 3.14e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 41.39  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019   39 QQDVSEFTHKLLDWLEDafQMKaeeetdEEKPKNPMVELFYGRFLAVGVLEGKKFEN--TEMFGQYPLQVNGFKDLHECL 116
Cdd:COG5077    273 QHDIQEFNRVLQDNLEK--SMR------GTVVENALNGIFVGKMKSYIKCVNVNYESarVEDFWDIQLNVKGMKNLQESF 344

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917984019  117 EAAMiegEIESLHSENSgKSGQEH---------WFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQVLYLDRYMHR 186
Cdd:COG5077    345 RRYI---QVETLDGDNR-YNAEKHglqdakkgvIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 4-180 7.69e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 39.22  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019   4 LRYLFALLVGTKRKY--VDPSRAVEILKDAFKS-NDSQQQDVSEFTHKLL----DWLEDAFQMKAEEETDEEKPKNPMV- 75
Cdd:cd02663    27 LKDLFESISEQKKRTgvISPKKFITRLKRENELfDNYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNNNNNAEPQp 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019  76 ----ELFYG------RFLAVGVLEGKKfentEMFGQYPLQVNGFKDLHECLEAAmieGEIESLHSEN-----SGKSGQEH 140
Cdd:cd02663   107 twvhEIFQGiltnetRCLTCETVSSRD----ETFLDLSIDVEQNTSITSCLRQF---SATETLCGRNkfycdECCSLQEA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1917984019 141 W----FTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQVLYL 180
Cdd:cd02663   180 EkrmkIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRL 223
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-433 8.40e-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: 38.91  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917984019 370 YRLHAVLVHEGQANAGHYWAYIFDHR---------------------ESRWMKYNDIAVTKSSWEELVRdsfggyrnASA 428
Cdd:cd02667   202 YRLYGVVEHSGTMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLK--------SEA 273


                  ....*
gi 1917984019 429 YCLMY 433
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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