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Conserved domains on  [gi|109148508|ref|NP_060140|]
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ubiquitin thioesterase OTUB1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTUB1 cd22763
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ...
 47-270 3.20e-161

Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS.


:

Pssm-ID: 438600  Cd Length: 224  Bit Score: 446.25  E-value: 3.20e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  47 LVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLV 126
Cdd:cd22763    1 LVSEKEDLSVLEKEYAEDDPIYQAKIKDLKKKYSYIRRTRPDGNCFYRAFGFAYLESLLDDPEELQRFKEVAAKSKDELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 127 SQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQ 206
Cdd:cd22763   81 SLGFPSFTIEDFHDTFMEVLEKVEKGTSVEELLEIFNDQGTSDYLVVYLRLLTSGYLQKEADFFQNFIEGGRSVKEFCSQ 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148508 207 EVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILY 270
Cdd:cd22763  161 EVEPMYKESDHIHIIALTSALGVSVRVEYMDRGEGGTVNPHDFPEGSEPRIHLLYRPGHYDILY 224
 
Name Accession Description Interval E-value
OTUB1 cd22763
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ...
 47-270 3.20e-161

Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS.


Pssm-ID: 438600  Cd Length: 224  Bit Score: 446.25  E-value: 3.20e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  47 LVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLV 126
Cdd:cd22763    1 LVSEKEDLSVLEKEYAEDDPIYQAKIKDLKKKYSYIRRTRPDGNCFYRAFGFAYLESLLDDPEELQRFKEVAAKSKDELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 127 SQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQ 206
Cdd:cd22763   81 SLGFPSFTIEDFHDTFMEVLEKVEKGTSVEELLEIFNDQGTSDYLVVYLRLLTSGYLQKEADFFQNFIEGGRSVKEFCSQ 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148508 207 EVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILY 270
Cdd:cd22763  161 EVEPMYKESDHIHIIALTSALGVSVRVEYMDRGEGGTVNPHDFPEGSEPRIHLLYRPGHYDILY 224
Peptidase_C65 pfam10275
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ...
 40-271 2.41e-120

Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly specific ubiquitin iso-peptidase that removes ubiquitin from proteins. The modification of cellular proteins by ubiquitin (Ub) is an important event that underlies protein stability and function in eukaryote being a dynamic and reversible process. Otubain carries several key conserved domains: (i) the OTU (ovarian tumour domain) in which there is an active cysteine protease triad (ii) a nuclear localization signal, (iii) a Ub interaction motif (UIM)-like motif phi-xx-A-xxxs-xx-Ac (where phi indicates an aromatic amino acid, x indicates any amino acid and Ac indicates an acidic amino acid), (iv) a Ub-associated (UBA)-like domain and (v) the LxxLL motif.


Pssm-ID: 431191 [Multi-domain]  Cd Length: 240  Bit Score: 343.49  E-value: 2.41e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508   40 EIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSA 119
Cdd:pfam10275   1 EEEAQGPLVSEKGPLSALEKEYAKADPIYLQKIQDLSEKYSGIRRTRGDGNCFYRAFGFSYLELLLESKDEIDRFKARVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  120 KSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEK--QTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGG 197
Cdd:pfam10275  81 SLKEALVALGFDEDTFEDFCDAFLELLKKVEDgvSTSESELLQAFNDQETSDYIVYFLRLLTSAYLKTHADEYEPFIDGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  198 RTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRG-EGGTTNPHIFP-----EGSEPKVYLLYRPGHYDILYK 271
Cdd:pfam10275 161 GTVEEFCQQEVEPMNKEADHLQIIALAEALGVPVRVEYLDRSaEGNTVNHHDFPgeddtEEQAPFITLLYRPGHYDILYK 240
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
 50-270 1.28e-03

Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 39.47  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  50 ERLELSVLYKEYAEDdNIYQQKIKDLHKKYSY-IRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKaVSAKSKEDLVS- 127
Cdd:COG5539   11 ETAMESLTEKQRFEL-KDLQTKITRIMKQLTFgRPPQRLNGKCLDLSYALSQKDEVEIEKAPKLRAE-TNEADQEDSLTp 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 128 -QGFTEFTIEDFHNTFMDLIEQVEKQTSVADLlASFNDQSTS----DYLVVYLRLLTSGYLQRESKFFEHFIEGgRTVKE 202
Cdd:COG5539   89 lQNIPELGISSFEKSVSQQSINVLEDMPGQDD-NSRLFQAERyslrDASVAKLREVVSLEVLSNPDLYNPAILE-IDVIA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109148508 203 FCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEgsepKVYLLYRPGHYDILY 270
Cdd:COG5539  167 YATWIVKPDSQGDGCIEIAIISDQLPVRIHVVDVDKDSEDRYNSHPYVQ----RISILFTGIHFDEET 230
 
Name Accession Description Interval E-value
OTUB1 cd22763
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ...
 47-270 3.20e-161

Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS.


Pssm-ID: 438600  Cd Length: 224  Bit Score: 446.25  E-value: 3.20e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  47 LVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLV 126
Cdd:cd22763    1 LVSEKEDLSVLEKEYAEDDPIYQAKIKDLKKKYSYIRRTRPDGNCFYRAFGFAYLESLLDDPEELQRFKEVAAKSKDELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 127 SQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQ 206
Cdd:cd22763   81 SLGFPSFTIEDFHDTFMEVLEKVEKGTSVEELLEIFNDQGTSDYLVVYLRLLTSGYLQKEADFFQNFIEGGRSVKEFCSQ 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148508 207 EVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILY 270
Cdd:cd22763  161 EVEPMYKESDHIHIIALTSALGVSVRVEYMDRGEGGTVNPHDFPEGSEPRIHLLYRPGHYDILY 224
Peptidase_C65 pfam10275
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ...
 40-271 2.41e-120

Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly specific ubiquitin iso-peptidase that removes ubiquitin from proteins. The modification of cellular proteins by ubiquitin (Ub) is an important event that underlies protein stability and function in eukaryote being a dynamic and reversible process. Otubain carries several key conserved domains: (i) the OTU (ovarian tumour domain) in which there is an active cysteine protease triad (ii) a nuclear localization signal, (iii) a Ub interaction motif (UIM)-like motif phi-xx-A-xxxs-xx-Ac (where phi indicates an aromatic amino acid, x indicates any amino acid and Ac indicates an acidic amino acid), (iv) a Ub-associated (UBA)-like domain and (v) the LxxLL motif.


Pssm-ID: 431191 [Multi-domain]  Cd Length: 240  Bit Score: 343.49  E-value: 2.41e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508   40 EIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSA 119
Cdd:pfam10275   1 EEEAQGPLVSEKGPLSALEKEYAKADPIYLQKIQDLSEKYSGIRRTRGDGNCFYRAFGFSYLELLLESKDEIDRFKARVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  120 KSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEK--QTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGG 197
Cdd:pfam10275  81 SLKEALVALGFDEDTFEDFCDAFLELLKKVEDgvSTSESELLQAFNDQETSDYIVYFLRLLTSAYLKTHADEYEPFIDGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  198 RTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRG-EGGTTNPHIFP-----EGSEPKVYLLYRPGHYDILYK 271
Cdd:pfam10275 161 GTVEEFCQQEVEPMNKEADHLQIIALAEALGVPVRVEYLDRSaEGNTVNHHDFPgeddtEEQAPFITLLYRPGHYDILYK 240
OTUB2 cd22764
Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, ...
 47-270 1.25e-102

Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, or ubiquitin-specific-processing protease OTUB2. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that mediates the deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. OTUB2 plays a role in DNA double-strand break (DSB) response (DDR); it enhances RNF8-mediated ubiquitination in an early phase of the DDR and promotes faster DSB repair but suppresses homologous recombination. It also functions as a cancer stemness and metastasis-promoting factor that deubiquitinates and activates the transcriptional regulators YAP/TAZ, which play important roles in development, physiology, and tumorigenesis and are negatively controlled by the Hippo pathway. OTUB2 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS.


Pssm-ID: 438601  Cd Length: 222  Bit Score: 298.14  E-value: 1.25e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  47 LVSERLELSVLYKEYAEDDnIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLV 126
Cdd:cd22764    1 LISEKCDISSLLPEHPENP-IYQRKLKDLSKRYASIRKTRGDGNCFYRALAFAYLESLLGNSREIQKFKETVLQSKNELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 127 SQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQ 206
Cdd:cd22764   80 AAGFEEHRFRNLFNTFVSVVELVEADGSGSSLLKAFNDQTTSDSIVQYLRLLTSAFLQNRADFFQHFVEEGMNIKDFCTQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148508 207 EVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEgGTTNPHIFPEGSEPKVYLLYRPGHYDILY 270
Cdd:cd22764  160 EVEPMAMECDHIQITALSQALGIPLQVEYVDEMD-TALNHHIFPEGAEPSVYLLYKTSHYNILY 222
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
 47-270 4.61e-95

Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 (also called ubiquitin thioesterase OTUB1 or OTU domain-containing ubiquitin aldehyde-binding protein 1), otubain-2 (also called ubiquitin thioesterase OTUB2 or OTU domain-containing ubiquitin aldehyde-binding protein 2), and similar proteins. They function as deubiquitylases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12). OTUB1 can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates, while OTUB2 mediates the deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. The otubain subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Members of this subfamily are classified as family C65 cysteine proteases by MEROPS.


Pssm-ID: 438586 [Multi-domain]  Cd Length: 232  Bit Score: 279.22  E-value: 4.61e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  47 LVSERLELSVLYKEYaEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLD--DSKELQRFKAVSAKSKED 124
Cdd:cd22749    1 LVGEKEPLSALAEEY-AGNPIFLQKIKELKKKYSGFRRVRGDGNCFYRAFAFSYLELLLKnqDPAELERLLARLESLKNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 125 LVSQGFTEFTIEDFHNTFMDLIEQVEK----QTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTV 200
Cdd:cd22749   80 LEALGFEELVFEDFYEEFLELLKKLRNskerELTEEELLELFNDEETSNYIVVFLRLLTSAYLKTNADDYEPFLFEGMSV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109148508 201 KEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEG---SEPKVYLLYRPGHYDILY 270
Cdd:cd22749  160 EEFCEREVEPMGKEADHLQITALANALGVPVRVEYLDRSAGGEVNFHEFPPEdsdSLPVITLLYRPGHYDILY 232
AtOTU1-like cd22765
Arabidopsis thaliana Deubiquitinating enzyme OTU1 and similar plant proteins; This group ...
 46-270 5.22e-76

Arabidopsis thaliana Deubiquitinating enzyme OTU1 and similar plant proteins; This group contains plant otibain-like proteins including Oryza sativa Japonica group otubain-like deubiquitinase and Arabidopsis thaliana deubiquitinating enzyme OTU1 (AtOTU1), also called OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1 or OTU domain-containing protein 1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that mediates the deubiquitination of protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. AtOTU1 shows a preference for Met-1 and 'Lys-48' over 'Lys-63'-linked ubiquitin tetramers as substrates. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS.


Pssm-ID: 438602  Cd Length: 247  Bit Score: 231.48  E-value: 5.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  46 PLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLD--DSKELQRFKAVSAKSKE 123
Cdd:cd22765    1 PYVGDKEPLSALAAEYQSGSPVFVAKIESLGETYGAIRRTRGDGNCFFRSFMFGYLEHLLEtqDGAEVRRVLKRIEQCKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 124 DLVSQGFTEFTIEDFHNTFMDLIEQV----EKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEG--G 197
Cdd:cd22765   81 KLVDLGYQELVFEDAMEILVEQLESIgqgdEESISIETLLENMRDDMVSNYVVMFLRFVTSAEIQRRADFFEPFIMGlsN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 198 RTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDR--------GEGGTT-NPHIF-----PEGSEPKVYLLYRP 263
Cdd:cd22765  161 MTVEQFCRRSVEPMGEESDHVHIVALTDALQVPIRVVYLDRsscdgaggGAGGVEvNHHDFvpegcPAAGRPRVHLLYRP 240


                 ....*..
gi 109148508 264 GHYDILY 270
Cdd:cd22765  241 GHYDILY 247
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 154-269 2.17e-08

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 51.67  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 154 SVADLLasFNDQSTsdylVVYLRLLTSGYLQRESKFFE----HFIEGGRTVKEFCQQevepMCKES---DHIHIIALAQA 226
Cdd:cd22744   15 ALAHAL--YGDQES----HRELRQEVVDYLRENPDLYEpaelADEDDGEDFDEYLQR----MRKPGtwgGELELQALANA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 109148508 227 LSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYR-PGHYDIL 269
Cdd:cd22744   85 LNVPIVVYSEDGGFLPVSVFGPGPGPSGRPIHLLYTgGNHYDAL 128
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 81-267 3.78e-04

OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar proteins; Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. DUBs catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. OTU7 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438608 [Multi-domain]  Cd Length: 124  Bit Score: 39.46  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  81 YIRKTRPDGNCFYRAFgfshleallddskelqrfkavsakskedlvsqgfteftiedfhntfmdlieqvekqtsvADLLa 160
Cdd:cd22771    3 RIRDVEGDGNCLFRAL-----------------------------------------------------------ADQL- 22

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 161 sFNDQStsdyLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQevepMCKES---DHIHIIALAQALSVSIQVeYMD 237
Cdd:cd22771   23 -YGDEE----RHAELRKKVVDYMEAHEEDFEPFFEDDETFEDYVSR----MREDGtwgGNLELQAASLVYRVNIVV-HQL 92

                        170       180       190
                 ....*....|....*....|....*....|.
gi 109148508 238 rGEGGTTNPHiFPEGSEPKVYLLYRPG-HYD 267
Cdd:cd22771   93 -GQPRWEIEN-FPDKGARTIHLSYHDGeHYN 121
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 169-267 1.25e-03

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 37.82  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  169 DYLVVYLRLLTSGYLQRESKFFEHFIEGGRTvkeFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEggttnphi 248
Cdd:pfam02338  24 KMLVQELRETLAEYMREHKEEFEPFLEDDET---GDIIEIEQTGAWGGEIEIFALAHILRRPIIVYKSEGGE-------- 92

                          90
                  ....*....|....*....
gi 109148508  249 fpEGSEPKVYLLYRPGHYD 267
Cdd:pfam02338  93 --ELGGLKEYGIYLPLGWD 109
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
 50-270 1.28e-03

Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 39.47  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508  50 ERLELSVLYKEYAEDdNIYQQKIKDLHKKYSY-IRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKaVSAKSKEDLVS- 127
Cdd:COG5539   11 ETAMESLTEKQRFEL-KDLQTKITRIMKQLTFgRPPQRLNGKCLDLSYALSQKDEVEIEKAPKLRAE-TNEADQEDSLTp 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148508 128 -QGFTEFTIEDFHNTFMDLIEQVEKQTSVADLlASFNDQSTS----DYLVVYLRLLTSGYLQRESKFFEHFIEGgRTVKE 202
Cdd:COG5539   89 lQNIPELGISSFEKSVSQQSINVLEDMPGQDD-NSRLFQAERyslrDASVAKLREVVSLEVLSNPDLYNPAILE-IDVIA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109148508 203 FCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEgsepKVYLLYRPGHYDILY 270
Cdd:COG5539  167 YATWIVKPDSQGDGCIEIAIISDQLPVRIHVVDVDKDSEDRYNSHPYVQ----RISILFTGIHFDEET 230
 
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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