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Conserved domains on  [gi|727346117|ref|NP_001289818|]
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ubiquitin thioesterase otulin [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_OTUL cd22799
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
 81-346 2.71e-179

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


:

Pssm-ID: 438620  Cd Length: 266  Bit Score: 497.35  E-value: 2.71e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  81 LSVAPEMDIMDYCKKEWRGNTEKAMCMRKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPE 160
Cdd:cd22799    1 LSVAPEMDILDYCKKEWRGNTQKATCMKKGYEEVSQKFTSIRRVRGDNYCALRATLFQALSQAVGLPPWLQDPELMLLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 161 KLINKYTWIKQWKLGLKFDGKSEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEEEYSLYEAMKFLMLAR 240
Cdd:cd22799   81 KLISKYNWIKQWKLGLKFDGKNEDLVDKLKEYLTLLKKKWAGLAEMRTAEERQIACDELFTNEAEEYSLYEAVKFLMLNR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 241 AIQLYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVY 320
Cdd:cd22799  161 AIELYNDKEKGKEVPFFSWLLFARDTSNNPGQLLRNHLNQVGHSGGLEQVEMFLLGYALQHTIQVYRLYKYNTEEFITVY 240

                        250       260
                 ....*....|....*....|....*.
gi 727346117 321 PTDPPKDWPMVTLIAEDDRHYNIPVR 346
Cdd:cd22799  241 PTDPPKDWPVVTLITEDDRHYNIPVR 266
 
Name Accession Description Interval E-value
OTU_OTUL cd22799
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
 81-346 2.71e-179

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438620  Cd Length: 266  Bit Score: 497.35  E-value: 2.71e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  81 LSVAPEMDIMDYCKKEWRGNTEKAMCMRKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPE 160
Cdd:cd22799    1 LSVAPEMDILDYCKKEWRGNTQKATCMKKGYEEVSQKFTSIRRVRGDNYCALRATLFQALSQAVGLPPWLQDPELMLLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 161 KLINKYTWIKQWKLGLKFDGKSEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEEEYSLYEAMKFLMLAR 240
Cdd:cd22799   81 KLISKYNWIKQWKLGLKFDGKNEDLVDKLKEYLTLLKKKWAGLAEMRTAEERQIACDELFTNEAEEYSLYEAVKFLMLNR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 241 AIQLYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVY 320
Cdd:cd22799  161 AIELYNDKEKGKEVPFFSWLLFARDTSNNPGQLLRNHLNQVGHSGGLEQVEMFLLGYALQHTIQVYRLYKYNTEEFITVY 240

                        250       260
                 ....*....|....*....|....*.
gi 727346117 321 PTDPPKDWPMVTLIAEDDRHYNIPVR 346
Cdd:cd22799  241 PTDPPKDWPVVTLITEDDRHYNIPVR 266
Peptidase_C101 pfam16218
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in ...
 81-345 7.34e-173

Peptidase family C101; This is a family of cysteine-peptidases that is conserved in vertebrates. The key residues as found in SwissProt:Q96BN8 are Asp126, Cys129, His339 and Asn341.


Pssm-ID: 465075  Cd Length: 265  Bit Score: 481.04  E-value: 7.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117   81 LSVAPEMDIMDYCKKEWRGNTEKAMCMRKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPE 160
Cdd:pfam16218   1 LSVAPEVDILDYSEREWRGNTAKAALMRKGYEEVSQKFSSLRRVRGDNYCALRATLFQILSQSTQLPSWLQDEDILMLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  161 KLINKYTWIKQWKLGLKFDGKSEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEEEYSLYEAMKFLMLAR 240
Cdd:pfam16218  81 KLQTKYNWIKQWTFPPECPYGGKNAVEKLKECLELLKTKWQEAVECKTHEERQSACDELFSGEEEEYKLYEALKFLMLNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  241 AIQLYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVY 320
Cdd:pfam16218 161 AIELYEDMEKGKEVPVFCWLLFARDTSSDPESFLMNHLNQVGDSGGLEQVEMFLLGYALEVTIQVYRLYKYNTEEFITYY 240

                         250       260
                  ....*....|....*....|....*
gi 727346117  321 PTDPPKDWPMVTLIAEDDRHYNIPV 345
Cdd:pfam16218 241 PDDHRDDWPVVTLITEDDRHYNVPV 265
 
Name Accession Description Interval E-value
OTU_OTUL cd22799
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
 81-346 2.71e-179

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438620  Cd Length: 266  Bit Score: 497.35  E-value: 2.71e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  81 LSVAPEMDIMDYCKKEWRGNTEKAMCMRKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPE 160
Cdd:cd22799    1 LSVAPEMDILDYCKKEWRGNTQKATCMKKGYEEVSQKFTSIRRVRGDNYCALRATLFQALSQAVGLPPWLQDPELMLLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 161 KLINKYTWIKQWKLGLKFDGKSEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEEEYSLYEAMKFLMLAR 240
Cdd:cd22799   81 KLISKYNWIKQWKLGLKFDGKNEDLVDKLKEYLTLLKKKWAGLAEMRTAEERQIACDELFTNEAEEYSLYEAVKFLMLNR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 241 AIQLYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVY 320
Cdd:cd22799  161 AIELYNDKEKGKEVPFFSWLLFARDTSNNPGQLLRNHLNQVGHSGGLEQVEMFLLGYALQHTIQVYRLYKYNTEEFITVY 240

                        250       260
                 ....*....|....*....|....*.
gi 727346117 321 PTDPPKDWPMVTLIAEDDRHYNIPVR 346
Cdd:cd22799  241 PTDPPKDWPVVTLITEDDRHYNIPVR 266
Peptidase_C101 pfam16218
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in ...
 81-345 7.34e-173

Peptidase family C101; This is a family of cysteine-peptidases that is conserved in vertebrates. The key residues as found in SwissProt:Q96BN8 are Asp126, Cys129, His339 and Asn341.


Pssm-ID: 465075  Cd Length: 265  Bit Score: 481.04  E-value: 7.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117   81 LSVAPEMDIMDYCKKEWRGNTEKAMCMRKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPE 160
Cdd:pfam16218   1 LSVAPEVDILDYSEREWRGNTAKAALMRKGYEEVSQKFSSLRRVRGDNYCALRATLFQILSQSTQLPSWLQDEDILMLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  161 KLINKYTWIKQWKLGLKFDGKSEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEEEYSLYEAMKFLMLAR 240
Cdd:pfam16218  81 KLQTKYNWIKQWTFPPECPYGGKNAVEKLKECLELLKTKWQEAVECKTHEERQSACDELFSGEEEEYKLYEALKFLMLNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  241 AIQLYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVY 320
Cdd:pfam16218 161 AIELYEDMEKGKEVPVFCWLLFARDTSSDPESFLMNHLNQVGDSGGLEQVEMFLLGYALEVTIQVYRLYKYNTEEFITYY 240

                         250       260
                  ....*....|....*....|....*
gi 727346117  321 PTDPPKDWPMVTLIAEDDRHYNIPV 345
Cdd:pfam16218 241 PDDHRDDWPVVTLITEDDRHYNVPV 265
OTU_OTUL-like cd22790
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin family; Otulin family includes ...
 91-345 1.21e-128

OTU (ovarian tumor) domain of ubiquitin thioesterase otulin family; Otulin family includes otulin and otulinl. Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulin and otulinl belong to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438611  Cd Length: 258  Bit Score: 368.48  E-value: 1.21e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  91 DYCKKEWRGNTEKAMCMRKGYEEVSQK--FTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELIllPEKLINKYT- 167
Cdd:cd22790    1 DYAEREWKGETPKAKTIKKGYEEIPRLlgCKYLRRIRGDNYCAIRAALFQVLSQGIPVPSKWPALEQI--PEKLLNSYGc 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 168 -WIKQWKLGLKFDGKSEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEE-EYSLYEAMKFLMLARAIQLY 245
Cdd:cd22790   79 sWLQQWSFANRLPYTGEDVLSGLRECLLTLDSQVEELESMSTEEDREDALLSLLNSDPTlDLKLMEAVKLLMLVSAIELY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 246 DDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPP 325
Cdd:cd22790  159 NRMQKGEDVPLFAWLLFARDTSSTPKDFLKNHLNPVGDTAGLEQVEMFLLGYSLGVTIRVFRPSQFGQEDFICYYPDEED 238

                        250       260
                 ....*....|....*....|
gi 727346117 326 KDWPMVTLIAEDDRHYNIPV 345
Cdd:cd22790  239 DDWPEVTLIAEDDRHYNVPV 258
OTU_OTULL cd22798
OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called ...
 88-345 2.93e-97

OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulinl belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).


Pssm-ID: 438619  Cd Length: 261  Bit Score: 289.01  E-value: 2.93e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  88 DIMDYCKKEWRGNTEKAMCMRKGYEEVSQK--FTSIRRVRGDNYCALRATLFQAMSQLAELPPWLQDLELILLPEKLINK 165
Cdd:cd22798    1 DLLEYCAREWKGETPRAKQMRKAYEELFWRhhIKYVRQVRGDNYCALRAVLFQIFSQGIPFPSWMKEQDILKLPEKLLYS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 166 Y--TWIKQWKLGL-KFDGksEDLVERIKESLALLRKKWVSLAAMEAAEARQTACDELFTNEEEEYSLYEAMKFLMLARAI 242
Cdd:cd22798   81 QgcNWIQQYSFGPeKYTG--PNVFGKLRKCVETLKTQWTEISGIKDYEKRGKMCNTLFSDEAKEYKLYEAIKFLMLYQVI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 243 QLYDDKEKGKEVPFFSVLLFARDTSNDPEQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPT 322
Cdd:cd22798  159 EVYEQMKTGQDVPNFFSLLFSRDTSSDPLSFMMNHLNSIGDTGGLEQIEMFLLGYTLEVKIKVFRLYKFNTEEFEVCYPE 238

                        250       260
                 ....*....|....*....|...
gi 727346117 323 DPPKDWPMVTLIAEDDRHYNIPV 345
Cdd:cd22798  239 EYLRDWPEISLLTEDDRHYNIPV 261
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
 107-343 4.92e-09

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: 56.19  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 107 MRKGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQLAELPPwlqdlelILLPEKLINKytwIKQWKLGLKFDGKSEDLV 186
Cdd:cd22749   21 FLQKIKELKKKYSGFRRVRGDGNCFYRAFAFSYLELLLKNQD-------PAELERLLAR---LESLKNLLEALGFEELVF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 187 ERIKESL-ALLRKkwvsLAAMEAAEARQTACDELFTNEEEEYSLyeaMKFLMLARAIQLYDDKEkgKEVPFFsvllfarD 265
Cdd:cd22749   91 EDFYEEFlELLKK----LRNSKERELTEEELLELFNDEETSNYI---VVFLRLLTSAYLKTNAD--DYEPFL-------F 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 266 TSNDPEQLLRNHLNQVGHTGglEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITV-YPTDPPKDWPMVTLIAeddR--HYN 342
Cdd:cd22749  155 EGMSVEEFCEREVEPMGKEA--DHLQITALANALGVPVRVEYLDRSAGGEVNFHeFPPEDSDSLPVITLLY---RpgHYD 229


                 .
gi 727346117 343 I 343
Cdd:cd22749  230 I 230
OTUB2 cd22764
Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, ...
 98-137 1.41e-03

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: 39.67  E-value: 1.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 727346117  98 RGNTEKAMCMRKgYEEVSQKFTSIRRVRGDNYCALRATLF 137
Cdd:cd22764   13 PEHPENPIYQRK-LKDLSKRYASIRKTRGDGNCFYRALAF 51
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 240-343 2.43e-03

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: 37.42  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117 240 RAI--QLYDDKEKGKEV-------------PFFSVLLFARDTSNDPEQLLRNhLNQVGHTGGleQVEMFLLAYAVRHTIQ 304
Cdd:cd22744   14 RALahALYGDQESHRELrqevvdylrenpdLYEPAELADEDDGEDFDEYLQR-MRKPGTWGG--ELELQALANALNVPIV 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 727346117 305 VYrlSKYNTEEFITVYPTDPPKDWPMVTLIAEDDRHYNI 343
Cdd:cd22744   91 VY--SEDGGFLPVSVFGPGPGPSGRPIHLLYTGGNHYDA 127
Peptidase_C65 pfam10275
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ...
 113-343 5.60e-03

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: 38.03  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  113 EVSQKFTSIRRVRGDNYCALRATLFqAMsqlaelppwlqdLELILLPEKLINKY-TWIKQWKLGLKFDGKSEDLVER-IK 190
Cdd:pfam10275  35 DLSEKYSGIRRTRGDGNCFYRAFGF-SY------------LELLLESKDEIDRFkARVESLKEALVALGFDEDTFEDfCD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  191 ESLALLRKkwvslaameAAEARQTACDELF----TNEEEEYSLYeamkFLMLARAIQLYDDKEkgkevpFFSVLLFARDT 266
Cdd:pfam10275 102 AFLELLKK---------VEDGVSTSESELLqafnDQETSDYIVY----FLRLLTSAYLKTHAD------EYEPFIDGGGT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727346117  267 SndpEQLLRNHLNQVGHTGglEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYpTDPPKDW-----PMVTLIAEDDrHY 341
Cdd:pfam10275 163 V---EEFCQQEVEPMNKEA--DHLQIIALAEALGVPVRVEYLDRSAEGNTVNHH-DFPGEDDteeqaPFITLLYRPG-HY 235


                  ..
gi 727346117  342 NI 343
Cdd:pfam10275 236 DI 237
 
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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