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Conserved domains on  [gi|25144248|ref|NP_491765|]
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Ubiquitin carboxyl-terminal hydrolase [Caenorhabditis elegans]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 1004990)

ubiquitin carboxyl-terminal hydrolase family protein may be a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-786 5.79e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 321.96  E-value: 5.79e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALVTVDSFQTRYGEqgLETLVNCPLDKLHNDFNAQFSKVVRAMLSGDYSSEM------DPTNNH 393
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDD--LENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPAslksenDPYQVG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 394 IKPLQFKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAENSR-TEVIDPTDSFKFKAINRFEDRGTRRVRYTDQEEMLIRL 472
Cdd:cd02658  79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFkNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 473 PISGDLLRPIP-DTENRYSVDMKAAIHAYFDVQKIDDYISPiTGEPKGATNTISMKTFPDYLFFQVSKFAYNVDGTQKKL 551
Cdd:cd02658 159 PVPKDEATEKEeGELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 552 dmeleieeeldlsgyrghgkleheialpdeeptaprttpDIPASVrfvagelmlmgfcenacyraayysngnveiasnwl 631
Cdd:cd02658 238 ---------------------------------------DVPIDV----------------------------------- 243
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 632 mehmddsdindlfvipsgtpsargevdpnlvasivemgfsnhqakyalkqvptvaeavewlfanMDSIpvesaavglssd 711
Cdd:cd02658 244 ----------------------------------------------------------------PEEL------------ 247
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 712 apepsvtesatqktfkdGGEKYKLIGMISHMGSRPDSGHYVAHMLK----EGKWVLFNDEKVALSQDPP--KKLAYVYLY 785
Cdd:cd02658 248 -----------------GPGKYELIAFISHKGTSVHSGHYVAHIKKeidgEGKWVLFNDEKVVASQDPPemKKLGYIYFY 310

                .
gi 25144248 786 K 786
Cdd:cd02658 311 Q 311
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
185-266 3.64e-17

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 76.15  E-value: 3.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   185 CEVegCGLNDNLWLNLTDGAVRCGRSQflsdgkktngNGHMQDYFDSTRFPLVVKLGTISsnlelidVYSYDEDDAVIDP 264
Cdd:pfam02148   1 CSL--CGNTSNLWLCLTCGHVGCGRYQ----------NSHALEHYEETGHPLAVNLSTLT-------VYCYPCDDYVHDP 61

                  ..
gi 25144248   265 NL 266
Cdd:pfam02148  62 SL 63
zf-UBP_var super family cl39301
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
19-78 1.75e-14

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


The actual alignment was detected with superfamily member pfam17807:

Pssm-ID: 407678  Cd Length: 64  Bit Score: 68.39  E-value: 1.75e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248    19 PTFDQKIFKDQCAYCFKDPHGKDGLYISLKNYHAFCREHAEIYGTTSGNTLFVQFESTKK 78
Cdd:pfam17807   4 PSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFCKKHAQLHFERTGHPVYLNIKRTKK 63
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
597-634 1.76e-12

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


:

Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 62.26  E-value: 1.76e-12
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 597 RFVAGELMLMGFCENACYRAAYYS-NGNVEIASNWLMEH 634
Cdd:cd14296   1 EEAVSQLMSMGFSENAAKRALYYTgNSSVEAAMNWLFEH 39
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
660-695 1.34e-11

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


:

Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 59.62  E-value: 1.34e-11
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 660 NLVASIVEMGFSNHQAKYALKQV--PTVAEAVEWLFAN 695
Cdd:cd14327   1 EAVAQLVEMGFSRERAEEALRAVgtNSVELAMEWLFTN 38
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-786 5.79e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 321.96  E-value: 5.79e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALVTVDSFQTRYGEqgLETLVNCPLDKLHNDFNAQFSKVVRAMLSGDYSSEM------DPTNNH 393
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDD--LENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPAslksenDPYQVG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 394 IKPLQFKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAENSR-TEVIDPTDSFKFKAINRFEDRGTRRVRYTDQEEMLIRL 472
Cdd:cd02658  79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFkNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 473 PISGDLLRPIP-DTENRYSVDMKAAIHAYFDVQKIDDYISPiTGEPKGATNTISMKTFPDYLFFQVSKFAYNVDGTQKKL 551
Cdd:cd02658 159 PVPKDEATEKEeGELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 552 dmeleieeeldlsgyrghgkleheialpdeeptaprttpDIPASVrfvagelmlmgfcenacyraayysngnveiasnwl 631
Cdd:cd02658 238 ---------------------------------------DVPIDV----------------------------------- 243
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 632 mehmddsdindlfvipsgtpsargevdpnlvasivemgfsnhqakyalkqvptvaeavewlfanMDSIpvesaavglssd 711
Cdd:cd02658 244 ----------------------------------------------------------------PEEL------------ 247
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 712 apepsvtesatqktfkdGGEKYKLIGMISHMGSRPDSGHYVAHMLK----EGKWVLFNDEKVALSQDPP--KKLAYVYLY 785
Cdd:cd02658 248 -----------------GPGKYELIAFISHKGTSVHSGHYVAHIKKeidgEGKWVLFNDEKVVASQDPPemKKLGYIYFY 310

                .
gi 25144248 786 K 786
Cdd:cd02658 311 Q 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
319-785 6.49e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 166.46  E-value: 6.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   319 TGLVNTGSSCYMNSVLQALVTVDSFQtRYGEQGLETLVNCPLDKLHNdFNAQFSKVVRAMLSGDYSSemdptnnHIKPLQ 398
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKNSKSS-------SVSPKM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   399 FKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAEN-----SRTEVIDPTDSFKFKAINRFEDRGTRRVRYTDQEEMLIRLP 473
Cdd:pfam00443  72 FKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDlngnhSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   474 ISGDLLRPIPDTENrysvDMKAAIHAYFDVQKIDDYISPITGEPKGATNTISMKTFPDYLFFQVSKFAYNVDGTQKkldm 553
Cdd:pfam00443 152 IPGDSAELKTASLQ----ICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEK---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   554 eleieeeldlsgyrghgkleheialpdeeptaprttpdipasvrfvagelmlmgfcenacyraayysngnveiasnwlme 633
Cdd:pfam00443     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   634 hmddsdINDLFVIPsgtpsargevdpnlvasivemgfsnhqakyalkqvptvaeavewLFANMDSIpvesaavglssdap 713
Cdd:pfam00443 224 ------LNTEVEFP--------------------------------------------LELDLSRY-------------- 239
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25144248   714 epsVTESATQKTfkDGGEKYKLIGMISHMGSrPDSGHYVAHMLK--EGKWVLFNDEKVALSQ---DPPKKLAYVYLY 785
Cdd:pfam00443 240 ---LAEELKPKT--NNLQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTEVDeetAVLSSSAYILFY 310
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
185-266 3.64e-17

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 76.15  E-value: 3.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   185 CEVegCGLNDNLWLNLTDGAVRCGRSQflsdgkktngNGHMQDYFDSTRFPLVVKLGTISsnlelidVYSYDEDDAVIDP 264
Cdd:pfam02148   1 CSL--CGNTSNLWLCLTCGHVGCGRYQ----------NSHALEHYEETGHPLAVNLSTLT-------VYCYPCDDYVHDP 61

                  ..
gi 25144248   265 NL 266
Cdd:pfam02148  62 SL 63
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
19-78 1.75e-14

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


Pssm-ID: 407678  Cd Length: 64  Bit Score: 68.39  E-value: 1.75e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248    19 PTFDQKIFKDQCAYCFKDPHGKDGLYISLKNYHAFCREHAEIYGTTSGNTLFVQFESTKK 78
Cdd:pfam17807   4 PSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFCKKHAQLHFERTGHPVYLNIKRTKK 63
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
184-245 5.50e-14

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 66.62  E-value: 5.50e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25144248    184 TCEVegCGLNDNLWLNLTDGAVRCGRSQflsdgkktngNGHMQDYFDSTRFPLVVKLGTISS 245
Cdd:smart00290   1 RCSV--CGTIENLWLCLTCGQVGCGRYQ----------NGHALEHFEETGHPLVVKLGTQRV 50
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
597-634 1.76e-12

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 62.26  E-value: 1.76e-12
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 597 RFVAGELMLMGFCENACYRAAYYS-NGNVEIASNWLMEH 634
Cdd:cd14296   1 EEAVSQLMSMGFSENAAKRALYYTgNSSVEAAMNWLFEH 39
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
660-695 1.34e-11

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 59.62  E-value: 1.34e-11
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 660 NLVASIVEMGFSNHQAKYALKQV--PTVAEAVEWLFAN 695
Cdd:cd14327   1 EAVAQLVEMGFSRERAEEALRAVgtNSVELAMEWLFTN 38
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
602-631 1.16e-07

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 48.21  E-value: 1.16e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 25144248   602 ELMLMGFCENACYRAAYYSNGNVEIASNWL 631
Cdd:pfam00627   8 RLVEMGFDREQVREALRATGNNVERAAEYL 37
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
317-431 1.31e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 55.27  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 317 GYTGLVNTGSSCYMNSVLQALVTVDSFQTRYGEQGLETLVN--CPLdKLHNDFNAQFSKVVRAMLSGDYSSemdptnnhI 394
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINeeNPL-GMHGSVASAYADLIKQLYDGNLHA--------F 334
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 25144248 395 KPLQFKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAE 431
Cdd:COG5560 335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHE 371
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
602-632 2.58e-07

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 47.48  E-value: 2.58e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 25144248    602 ELMLMGFCENACYRAAYYSNGNVEIASNWLM 632
Cdd:smart00165   7 QLLEMGFSREEALKALRAANGNVERAAEYLL 37
 
Name Accession Description Interval E-value
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-786 5.79e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 321.96  E-value: 5.79e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALVTVDSFQTRYGEqgLETLVNCPLDKLHNDFNAQFSKVVRAMLSGDYSSEM------DPTNNH 393
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDD--LENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPAslksenDPYQVG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 394 IKPLQFKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAENSR-TEVIDPTDSFKFKAINRFEDRGTRRVRYTDQEEMLIRL 472
Cdd:cd02658  79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFkNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 473 PISGDLLRPIP-DTENRYSVDMKAAIHAYFDVQKIDDYISPiTGEPKGATNTISMKTFPDYLFFQVSKFAYNVDGTQKKL 551
Cdd:cd02658 159 PVPKDEATEKEeGELVYEPVPLEDCLKAYFAPETIEDFCST-CKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPKKL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 552 dmeleieeeldlsgyrghgkleheialpdeeptaprttpDIPASVrfvagelmlmgfcenacyraayysngnveiasnwl 631
Cdd:cd02658 238 ---------------------------------------DVPIDV----------------------------------- 243
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 632 mehmddsdindlfvipsgtpsargevdpnlvasivemgfsnhqakyalkqvptvaeavewlfanMDSIpvesaavglssd 711
Cdd:cd02658 244 ----------------------------------------------------------------PEEL------------ 247
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 712 apepsvtesatqktfkdGGEKYKLIGMISHMGSRPDSGHYVAHMLK----EGKWVLFNDEKVALSQDPP--KKLAYVYLY 785
Cdd:cd02658 248 -----------------GPGKYELIAFISHKGTSVHSGHYVAHIKKeidgEGKWVLFNDEKVVASQDPPemKKLGYIYFY 310

                .
gi 25144248 786 K 786
Cdd:cd02658 311 Q 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
319-785 6.49e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 166.46  E-value: 6.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   319 TGLVNTGSSCYMNSVLQALVTVDSFQtRYGEQGLETLVNCPLDKLHNdFNAQFSKVVRAMLSGDYSSemdptnnHIKPLQ 398
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKNSKSS-------SVSPKM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   399 FKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAEN-----SRTEVIDPTDSFKFKAINRFEDRGTRRVRYTDQEEMLIRLP 473
Cdd:pfam00443  72 FKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDlngnhSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   474 ISGDLLRPIPDTENrysvDMKAAIHAYFDVQKIDDYISPITGEPKGATNTISMKTFPDYLFFQVSKFAYNVDGTQKkldm 553
Cdd:pfam00443 152 IPGDSAELKTASLQ----ICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEK---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   554 eleieeeldlsgyrghgkleheialpdeeptaprttpdipasvrfvagelmlmgfcenacyraayysngnveiasnwlme 633
Cdd:pfam00443     --------------------------------------------------------------------------------
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   634 hmddsdINDLFVIPsgtpsargevdpnlvasivemgfsnhqakyalkqvptvaeavewLFANMDSIpvesaavglssdap 713
Cdd:pfam00443 224 ------LNTEVEFP--------------------------------------------LELDLSRY-------------- 239
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25144248   714 epsVTESATQKTfkDGGEKYKLIGMISHMGSrPDSGHYVAHMLK--EGKWVLFNDEKVALSQ---DPPKKLAYVYLY 785
Cdd:pfam00443 240 ---LAEELKPKT--NNLQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTEVDeetAVLSSSAYILFY 310
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
185-266 3.64e-17

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 76.15  E-value: 3.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248   185 CEVegCGLNDNLWLNLTDGAVRCGRSQflsdgkktngNGHMQDYFDSTRFPLVVKLGTISsnlelidVYSYDEDDAVIDP 264
Cdd:pfam02148   1 CSL--CGNTSNLWLCLTCGHVGCGRYQ----------NSHALEHYEETGHPLAVNLSTLT-------VYCYPCDDYVHDP 61

                  ..
gi 25144248   265 NL 266
Cdd:pfam02148  62 SL 63
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
320-786 7.23e-17

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: 80.99  E-value: 7.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALvtvdsfqtrygeqgletlvncpldklhndfnaqfskvvramlsgdyssemdptnnhikplqf 399
Cdd:cd02257   1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 400 krvaagnhrdfsTSKQQDVEEYIRFLFEKI----------AENSRTEVIDPTDSFKFKAINRFEDRGTRRVRYTDQEEML 469
Cdd:cd02257  19 ------------FSEQQDAHEFLLFLLDKLheelkksskrTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELF 86
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 470 IRLPIsgdllrPIPDTENrysVDMKAAIHAYFDVQKIDDYISPI--TGEPKGATNTISMKTFPDYLFFQVSKFAYNVDGT 547
Cdd:cd02257  87 LSLPL------PVKGLPQ---VSLEDCLEKFFKEEILEGDNCYKceKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGT 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 548 QKKldmeleieeeldlsgyrghgkleheialpdeeptaprttpdipasvrfvagelmlmgfcenacyraayysngnveia 627
Cdd:cd02257 158 KEK----------------------------------------------------------------------------- 160
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 628 snwLMEHMDDSDINDLFvipsgtpsargevdpnlvasivemgfsnhqakyalkqvptvaeavewlfanmdsipvesaavg 707
Cdd:cd02257 161 ---LNTKVSFPLELDLS--------------------------------------------------------------- 174
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 708 lssdapePSVTESATQKTFKDGGEKYKLIGMISHMGSRPDSGHYVAHMLK--EGKWVLFNDEKV-------ALSQDPPKK 778
Cdd:cd02257 175 -------PYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDpsDGKWYKFNDDKVtevseeeVLEFGSLSS 247

                ....*...
gi 25144248 779 LAYVYLYK 786
Cdd:cd02257 248 SAYILFYE 255
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
19-78 1.75e-14

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


Pssm-ID: 407678  Cd Length: 64  Bit Score: 68.39  E-value: 1.75e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248    19 PTFDQKIFKDQCAYCFKDPHGKDGLYISLKNYHAFCREHAEIYGTTSGNTLFVQFESTKK 78
Cdd:pfam17807   4 PSASDRVYKDECIFCFDTPESEGGLFVCLKCFLGFCKKHAQLHFERTGHPVYLNIKRTKK 63
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
184-245 5.50e-14

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 66.62  E-value: 5.50e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25144248    184 TCEVegCGLNDNLWLNLTDGAVRCGRSQflsdgkktngNGHMQDYFDSTRFPLVVKLGTISS 245
Cdd:smart00290   1 RCSV--CGTIENLWLCLTCGQVGCGRYQ----------NGHALEHFEETGHPLVVKLGTQRV 50
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
597-634 1.76e-12

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 62.26  E-value: 1.76e-12
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 597 RFVAGELMLMGFCENACYRAAYYS-NGNVEIASNWLMEH 634
Cdd:cd14296   1 EEAVSQLMSMGFSENAAKRALYYTgNSSVEAAMNWLFEH 39
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
602-639 3.64e-12

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5. It has similar domain architecture, but functions differently from USP5 in cellular deubiquitination processes. It exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin in a non-activation manner. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270480 [Multi-domain]  Cd Length: 44  Bit Score: 61.17  E-value: 3.64e-12
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 602 ELMLMGFCENACYRAAYYSNGN-VEIASNWLMEHMDDSD 639
Cdd:cd14294   6 QLAEMGFPLEACRKAVYHTNNSgLEAAMNWIMEHMDDPD 44
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
660-695 1.34e-11

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 59.62  E-value: 1.34e-11
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 660 NLVASIVEMGFSNHQAKYALKQV--PTVAEAVEWLFAN 695
Cdd:cd14327   1 EAVAQLVEMGFSRERAEEALRAVgtNSVELAMEWLFTN 38
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
603-641 8.28e-10

UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270568 [Multi-domain]  Cd Length: 47  Bit Score: 54.72  E-value: 8.28e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 25144248 603 LMLMGFCENACYRAAYYS-NGNVEIASNWLMEHMDDSDIN 641
Cdd:cd14385   8 LLGMGFPEVRCKKALLATgNSDAEAAMNWLFEHMDDPDID 47
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
733-786 2.20e-08

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 56.57  E-value: 2.20e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25144248 733 YKLIGMISHMGSRPDSGHYVAHMLKE--GKWVLFNDEKVAL-SQDPPKKL--------AYVYLYK 786
Cdd:cd02657 241 YELVAVITHQGRSADSGHYVAWVRRKndGKWIKFDDDKVSEvTEEDILKLsgggdwhiAYILLYK 305
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
602-631 1.16e-07

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 48.21  E-value: 1.16e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 25144248   602 ELMLMGFCENACYRAAYYSNGNVEIASNWL 631
Cdd:pfam00627   8 RLVEMGFDREQVREALRATGNNVERAAEYL 37
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
317-431 1.31e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 55.27  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 317 GYTGLVNTGSSCYMNSVLQALVTVDSFQTRYGEQGLETLVN--CPLdKLHNDFNAQFSKVVRAMLSGDYSSemdptnnhI 394
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINeeNPL-GMHGSVASAYADLIKQLYDGNLHA--------F 334
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 25144248 395 KPLQFKRVAAGNHRDFSTSKQQDVEEYIRFLFEKIAE 431
Cdd:COG5560 335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHE 371
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
602-632 2.58e-07

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 47.48  E-value: 2.58e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 25144248    602 ELMLMGFCENACYRAAYYSNGNVEIASNWLM 632
Cdd:smart00165   7 QLLEMGFSREEALKALRAANGNVERAAEYLL 37
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
727-779 3.49e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 52.81  E-value: 3.49e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25144248 727 KDGGEKYKLIGMISHMGSRPDSGHYVAHMLKE--GKWVLFNDEKValSQDPPKKL 779
Cdd:cd02668 240 DEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEqtGEWYKFNDEDV--EEMPGKPL 292
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
599-639 3.31e-06

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA1 domain.


Pssm-ID: 270566 [Multi-domain]  Cd Length: 49  Bit Score: 44.66  E-value: 3.31e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 25144248 599 VAGELMLMGFCENACYRAAYYS-NGNVEIASNWLMEHMDDSD 639
Cdd:cd14383   6 VIIQLVEMGFPMDACRKAVYYTgNSGAEAAMNWVMSHMDDPD 47
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
602-635 3.86e-06

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 43.97  E-value: 3.86e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 25144248 602 ELMLMGFCENACYRAAYYSNGNVEIASNWLMEHM 635
Cdd:cd14306   3 KLMELGFPEEDCIRALRACGGNVEEAANWLLENA 36
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
659-696 1.03e-05

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 42.85  E-value: 1.03e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 659 PNLVASIVEMGFSNHQAKYALKQVP-TVAEAVEWLFANM 696
Cdd:cd14297   1 EDLVKQLVDMGFTEAQARKALRKTNnNVERAVDWLFEGP 39
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
602-640 1.26e-05

UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins.


Pssm-ID: 270476 [Multi-domain]  Cd Length: 49  Bit Score: 42.81  E-value: 1.26e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 25144248 602 ELMLMGFCENACYRAAYYS-NGNVEIASNWLMEHMDDSDI 640
Cdd:cd14290   9 ELEAMGFPRARAVRALHHTgNTSVEAAVNWIVEHENDPDI 48
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
733-788 1.71e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 47.49  E-value: 1.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25144248 733 YKLIGMISHMGSRpDSGHYVAHMLKEGKWVLFNDEKVAL-----SQDPPKKLAYVYLYKRI 788
Cdd:COG5533 225 YDLVGFVLHQGSL-EGGHYIAYVKKGGKWEKANDSDVTPvseeeAINEKAKNAYLYFYERI 284
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
602-639 2.24e-05

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 42.36  E-value: 2.24e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 602 ELMLMGFCENACYRAAYY-SNGNVEIASNWLMEHMDDSD 639
Cdd:cd14295   7 QLMEMGFPKVRAEKALFFtQNKGLEEAMEWLEEHSEDAD 45
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
732-786 3.33e-05

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 46.53  E-value: 3.33e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25144248 732 KYKLIGMISHMGSRPDSGHYVAHMLKEGKWVLFNDEKVALSQD----------PPKKLAYVYLYK 786
Cdd:cd02663 236 LYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDEnaveeffgdsPNQATAYVLFYQ 300
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
657-697 3.35e-05

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 41.55  E-value: 3.35e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 25144248 657 VDPNLVASIVEMGFSNHQAKYALKQVPTVAE-AVEWLFANMD 697
Cdd:cd14386   1 VPEEAVAMLVSMGFTRDQAIKALKATDNNVErAADWIFSHPD 42
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
319-428 3.67e-05

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 46.50  E-value: 3.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 319 TGLVNTGSSCYMNSVLQALVtvdsfQTRYgeqgletLVN-CPLDKLHNDFNAQFSKVVRAM--------LSGDYSSEMDP 389
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLT-----HTPP-------LANyLLSREHSKDCCNEGFCMMCALeahveralASSGPGSAPRI 69
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 25144248 390 TNNHIKplQFKrvaagnhRDFSTSKQQDVEEYIRFLFEK 428
Cdd:cd02661  70 FSSNLK--QIS-------KHFRIGRQEDAHEFLRYLLDA 99
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
317-434 7.19e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 45.71  E-value: 7.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 317 GYTGLVNTGSSCYMNSVLQALVtvdsfqtrygeqgletlvncpldklhndFNAQFSKVVRAMLSGDYSsemDPTNNHIKP 396
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLY----------------------------MTPEFRNAVYSIPPTEDD---DDNKSVPLA 49
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25144248 397 LQ-------FKRVAAGNHRDFSTSK-----------QQDVEEYIRFLFEKIAENSR 434
Cdd:cd02659  50 LQrlflflqLSESPVKTTELTDKTRsfgwdslntfeQHDVQEFFRVLFDKLEEKLK 105
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
728-785 1.03e-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: 1.03e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25144248 728 DGGEKYKLIGMISHMGSRPDSGHYVAHmLKE--GKWVLFNDEKVA-------LSQDppkklAYVYLY 785
Cdd:cd02661 243 DGPLKYKLYAVLVHSGFSPHSGHYYCY-VKSsnGKWYNMDDSKVSpvsietvLSQK-----AYILFY 303
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-429 1.40e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 44.79  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALVTVDSF--QTRYGEQGLETLVNCPLDKLHNDFNAqfskvvrAMLSGDYSSemdptnnhikPL 397
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFrrQVLSLNLPRLGDSQSVMKKLQLLQAH-------LMHTQRRAE----------AP 63
                        90       100       110
                ....*....|....*....|....*....|..
gi 25144248 398 QFKRVAAGNHRDFSTSKQQDVEEYIRFLFEKI 429
Cdd:cd02664  64 PDYFLEASRPPWFTPGSQQDCSEYLRYLLDRL 95
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-433 1.76e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 44.29  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALV---------TVDSFQTRYGEQGLETLVNCPLDKLHNDFNAQFSKVVRAMLSGDYSSEMDPT 390
Cdd:cd02660   2 GLINLGATCFMNVILQALLhnpllrnyfLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 25144248 391 NnhikplqfkrvaagnhrdFSTSKQQDVEEYIRFLFEKIAENS 433
Cdd:cd02660  82 N------------------LAGYSQQDAHEFFQFLLDQLHTHY 106
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
658-697 1.76e-04

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 39.66  E-value: 1.76e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 25144248 658 DPNLVASIVEMGFSNHQAKYALKQV--PTVAEAVEWLFANMD 697
Cdd:cd14295   1 DQELVAQLMEMGFPKVRAEKALFFTqnKGLEEAMEWLEEHSE 42
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
728-766 1.94e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 44.18  E-value: 1.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 25144248   728 DGGEKYKLIGMISHMGSRPDSGHYVAH---------MLKEGKWVLFND 766
Cdd:pfam13423 255 NEIVKYELRGVVVHIGDSGTSGHLVSFvkvadseleDPTESQWYLFND 302
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-343 2.09e-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: 43.51  E-value: 2.09e-04
                        10        20
                ....*....|....*....|....
gi 25144248 320 GLVNTGSSCYMNSVLQALVTVDSF 343
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSL 24
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-420 3.80e-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 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: 43.47  E-value: 3.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 320 GLVNTGSSCYMNSVLQALVTVDSFQTRYGE-QGLETLVNCPLDKLHNDFNAQFskvvramlsgdysSEMDPTNNHIKPL- 397
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNyNPARRGANQSSDNLTNALRDLF-------------DTMDKKQEPVPPIe 67
                        90       100       110
                ....*....|....*....|....*....|...
gi 25144248 398 ----------QFKRVAAGNHrdfstSKQQDVEE 420
Cdd:cd02657  68 flqllrmafpQFAEKQNQGG-----YAQQDAEE 95
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
698-786 4.84e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 43.25  E-value: 4.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248 698 SIPVESAAVGlSSDAPEPSVTESATQKTFKDGGEKYKLIGMISHMGSRPDSGHY------------VAHMLKE------- 758
Cdd:cd02664 209 SLPVRVESKS-SESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYftyardqtdadsTGQECPEpkdaeen 287
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 25144248 759 ---GKWVLFNDEKVALSQD---------PPKKLAYVYLYK 786
Cdd:cd02664 288 desKNWYLFNDSRVTFSSFesvqnvtsrFPKDTPYILFYE 327
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
662-697 6.17e-04

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 38.04  E-value: 6.17e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 662 VASIVEMGFSNHQAKYALKQVPT--VAEAVEWLFANMD 697
Cdd:cd14302   3 LQTLIEMGFSRNRAEKALAKTGNqgVEAAMEWLLAHED 40
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
731-769 8.11e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 42.24  E-value: 8.11e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 25144248 731 EKYKLIGMISHMGSrPDSGHYVAHmLKE---GKWVLFNDEKV 769
Cdd:cd02659 250 YIYELHGVLVHSGD-AHGGHYYSY-IKDrddGKWYKFNDDVV 289
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
732-786 8.91e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 41.50  E-value: 8.91e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25144248 732 KYKLIGMISHMGSRpDSGHYVAHMLKE--GKWVLFNDEKV--ALSQDPPKKLAYVYLYK 786
Cdd:cd02674 173 KYDLYAVVNHYGSL-NGGHYTAYCKNNetNDWYKFDDSRVtkVSESSVVSSSAYILFYE 230
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
603-637 1.11e-03

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 37.27  E-value: 1.11e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 25144248 603 LMLMGFCENACYRA-AYYSNGNVEIASNWLMEHMDD 637
Cdd:cd14302   6 LIEMGFSRNRAEKAlAKTGNQGVEAAMEWLLAHEDD 41
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
658-692 1.54e-03

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.


Pssm-ID: 270477 [Multi-domain]  Cd Length: 36  Bit Score: 36.66  E-value: 1.54e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 25144248 658 DPNLVASIVEMGFSNHQAKYALKQV-PTVAEAVEWL 692
Cdd:cd14291   1 DEDKLQQLMEMGFSEAEARLALRACnGNVERAVDYI 36
UBA_HERC2 cd14402
UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, ...
661-697 2.15e-03

UBA domain found in probable E3 ubiquitin-protein ligase HERC2 and similar proteins; HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. In addition to a ubiquitin-association (UBA) domain, HERC2 contains more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270585  Cd Length: 45  Bit Score: 36.58  E-value: 2.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 25144248 661 LVASIVEMGFSNHQAKYALKQV-------PTVAEAVEWLFANMD 697
Cdd:cd14402   2 IVQQLMEMGFPRKNVEFALKSLsgssgglPTPEALVAWLLEHPD 45
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
659-695 2.91e-03

UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270484 [Multi-domain]  Cd Length: 38  Bit Score: 35.90  E-value: 2.91e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 659 PNLVASIVEMGFSNHQAKYALKQVPTVAE-AVEWLFAN 695
Cdd:cd14298   1 DEALAQLVSMGFDPEVARKALILTNGNVErAIEWLFSN 38
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
603-637 3.22e-03

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 36.16  E-value: 3.22e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 25144248 603 LMLMGFCENACYRAAYYSNGNVEIASNWLMEHMDD 637
Cdd:cd14386   9 LVSMGFTRDQAIKALKATDNNVERAADWIFSHPDE 43
UBA1_UBP13 cd14384
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
602-639 3.41e-03

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270567  Cd Length: 49  Bit Score: 36.15  E-value: 3.41e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 602 ELMLMGFCENACYRAAYYS-NGNVEIASNWLMEHMDDSD 639
Cdd:cd14384   9 QLAEMGFPLEACRKAVYYTgNMGAEVAFNWIIAHMEEPD 47
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
603-635 3.82e-03

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 35.53  E-value: 3.82e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 25144248 603 LMLMGFCENACYRAAYYSNGNVEIASNWLMEHM 635
Cdd:cd14297   7 LVDMGFTEAQARKALRKTNNNVERAVDWLFEGP 39
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
317-439 4.09e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 40.62  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144248  317 GYTGLVNTGSSCYMNSVLQALVTVDSFqtRYGEQGLETLVNCPLDKLHNDFNAQFskvvramlsgdysSEMDPTNNHIKP 396
Cdd:COG5077  192 GYVGLRNQGATCYMNSLLQSLFFIAKF--RKDVYGIPTDHPRGRDSVALALQRLF-------------YNLQTGEEPVDT 256
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 25144248  397 LQFKRVAAGNhrDFSTSKQQDVEEYIRFLFEKIAENSRTEVID 439
Cdd:COG5077  257 TELTRSFGWD--SDDSFMQHDIQEFNRVLQDNLEKSMRGTVVE 297
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
659-695 4.16e-03

UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ubiquitin-associated (UBA) domain-containing protein encoded by a nonessential yeast gene RUP1. It can mediate the association of Rsp5 and Ubp2. The N-terminal UBA domain is responsible for antagonizing Rsp5 function, as well as bridging the Rsp5-Ubp2 interaction. No other characterized functional domains or motifs are found in RUP1p.


Pssm-ID: 270492  Cd Length: 38  Bit Score: 35.73  E-value: 4.16e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 659 PNLVASIVEMGFSNHQAKYALKQVP-TVAEAVEWLFAN 695
Cdd:cd14307   1 EEAVASLLEMGIPREVAIEALRETNgDVEAAANYIFSN 38
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
657-695 4.21e-03

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 35.45  E-value: 4.21e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 25144248 657 VDPNLVASIVEMGFSNHQAKYALKQVPTVAEAVEWLFAN 695
Cdd:cd14288   1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTH 39
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
662-696 4.56e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 35.50  E-value: 4.56e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 25144248 662 VASIVEMGFSNHQAKYALKQvpT---VAEAVEWLFANM 696
Cdd:cd14306   1 VAKLMELGFPEEDCIRALRA--CggnVEEAANWLLENA 36
UBA_Mud1_like cd14308
UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar ...
659-692 5.50e-03

UBA domain found in Schizosaccharomyces pombe UBA domain-containing protein mud1 and similar proteins; Schizosaccharomyces pombe mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1. S. cerevisiae Ddi1, also called v-SNARE-master 1 (Vsm1), belongs to a family of proteins known as the ubiquitin receptors which can bind ubiquitinated substrates and the proteasome. It is involved in the degradation of the F-box protein Ufo1, involved in the G1/S transition. It also participates in Mec1-mediated degradation of Ho endonuclease. Both S. pombe mud1 and S. cerevisiae Ddi1 contain an N-terminal ubiquitin-like (UBL) domain, an aspartyl protease-like domain, and a C-terminal ubiquitin-associated (UBA) domain. S. pombe mud1 binds to K48-linked polyubiquitin (polyUb) through UBA domain.


Pssm-ID: 270493  Cd Length: 36  Bit Score: 35.17  E-value: 5.50e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 25144248 659 PNLVASIVEMGFSNHQAKYALKQVPT-VAEAVEWL 692
Cdd:cd14308   1 PEKVRQLVDMGFTPTDAGRALKAANGdVTVAAEWL 35
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
733-769 5.68e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 39.88  E-value: 5.68e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 25144248 733 YKLIGMISHMGSRPDSGHYVAHMlkegKWVLFNDEKV 769
Cdd:cd02671 272 YRLFAVVMHSGATISSGHYTAYV----RWLLFDDSEV 304
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
320-337 7.47e-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: 38.81  E-value: 7.47e-03
                        10
                ....*....|....*...
gi 25144248 320 GLVNTGSSCYMNSVLQAL 337
Cdd:cd02674   1 GLRNLGNTCYMNSILQCL 18
 
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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