OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  163 GDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLK 242
Cdd:cd22769    1 GDRAFLIEPEHIDIVGYGRDRSGSLSYLHDTLEEIKKANDNEERLIPIHADGDGHCLVHAVSRALVGRELFWHALRENLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  243 QHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFL 322
Cdd:cd22769   81 QHFKENLDQYKALFQDFIDDSEWPDIIAECDPDFVPPEGEPLGLRNIHIFGLANVLKRPIILLDSLSGMQSSGDYSAIFL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 70778826  323 PGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVG 359
Cdd:cd22769  161 PGLVPPEKCRGKDGLLNKPICIAWSSSGRNHFIPLVG 197

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70778826  774 KKIRITTNDGRQSMVTLKPSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIE 848
Cdd:cd17059    1 MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGDTLIVE 75

OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  163 GDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLK 242
Cdd:cd22769    1 GDRAFLIEPEHIDIVGYGRDRSGSLSYLHDTLEEIKKANDNEERLIPIHADGDGHCLVHAVSRALVGRELFWHALRENLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  243 QHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFL 322
Cdd:cd22769   81 QHFKENLDQYKALFQDFIDDSEWPDIIAECDPDFVPPEGEPLGLRNIHIFGLANVLKRPIILLDSLSGMQSSGDYSAIFL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 70778826  323 PGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVG 359
Cdd:cd22769  161 PGLVPPEKCRGKDGLLNKPICIAWSSSGRNHFIPLVG 197

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70778826  774 KKIRITTNDGRQSMVTLKPSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIE 848
Cdd:cd17059    1 MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGDTLIVE 75

OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  163 GDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLK 242
Cdd:cd22769    1 GDRAFLIEPEHIDIVGYGRDRSGSLSYLHDTLEEIKKANDNEERLIPIHADGDGHCLVHAVSRALVGRELFWHALRENLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  243 QHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFL 322
Cdd:cd22769   81 QHFKENLDQYKALFQDFIDDSEWPDIIAECDPDFVPPEGEPLGLRNIHIFGLANVLKRPIILLDSLSGMQSSGDYSAIFL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 70778826  323 PGLIPAEKCTGRDGHLNKPICIAWSSSGRNHYIPLVG 359
Cdd:cd22769  161 PGLVPPEKCRGKDGLLNKPICIAWSSSGRNHFIPLVG 197

OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins classified as family C64 cysteine protease by MEROPS, such as tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3), ZRANB1, OTU domain-containing protein 7A (OTUD7A), and OTUD7B. It also includes VCIP135. These proteins are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that mediates the deubiquitination of protein substrates. TNFAIP3 also contains ubiquitin ligase activity. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. OTUD7A has been identified as a critical gene for brain function, while OTUD7B functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. This group belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  188 LYLHDTLEDIKRAN--KSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQ-----QHLARYQALFHDF- 259
Cdd:cd22750    1 RDLKDDLESEKVINwcRGVSRLVPLHTRGDGNCLLHAVSLALWGVEDRDLLLRSALHETLQndqerRFRARWRRQQLKSg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  260 ----------IDAAEWEDIINECDPLFVpPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSG------DYSATFLP 323
Cdd:cd22750   81 qelglsldeeALQAEWEEILKAAETPTV-PAGPGSYLEEIHIFVLANVLRRPIIVLADDSARSLEGsalqdnGMSGIYLP 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 70778826  324 GLIPAEKCtgrdghLNKPICIAWSSsgrNHYIPLV 358
Cdd:cd22750  160 LLWPPSEC------SRSPLALGYSN---GHFSPLV 185

OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. 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 C64 cysteine protease by MEROPS.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  193 TLEDIKRANKSQEC--LIPVHVDGDGHCLVHAVSRALVG--------RELFWHALRE----NLKQHFQ-QHLARYQALFH 257
Cdd:cd22766   36 TLEEAKKLNWCREVrkLVPLKTTGDGNCLLHAVSLYMWGvqdtdlvlRKALYEALVEtdtrNFKLRWQrERLKSQEFVGT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  258 DFID-----AAEWEDIINECDPLFVPPEGVPL--GLRNIHIFGLANVLHRPIILL--DSLSGMRSSG----DYSATFLPG 324
Cdd:cd22766  116 GLRYdtrewEEEWDNVVKMASPESKPAAGGLPynSLEEIHIFVLANILRRPIIVIadDMLRSLEGSSlaplNFGGIYLPL 195

                        170       180       190
                 ....*....|....*....|....*....|....
gi 70778826  325 LIPAEKCtgrdghLNKPICIAWSSsgrNHYIPLV 358
Cdd:cd22766  196 HWPPQEC------YKYPIVLGYDS---QHFTPLV 220

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826    214 GDGHCLVHAVSRAL-----VGRELFWHALRENLKQHFQQHLAryqaLFHDFIDAAEWEDIINECDPlfvppeGVPLGlrN 288
Cdd:pfam02338    2 GDGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKE----EFEPFLEDDETGDIIEIEQT------GAWGG--E 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70778826    289 IHIFGLANVLHRPIILLDSLSGMRSSGdysatflpgliPAEKCTGRDGHLNKPICIAWSS---SGRNHY 354
Cdd:pfam02338   70 IEIFALAHILRRPIIVYKSEGGEELGG-----------LKEYGIYLPLGWDPSLCLVYPRhlyYLGGHY 127

OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; This subfamily consists of OTU domain-containing protein 7A (OTUD7A), OTUD7B, and similar proteins. OTUD7A and OTUD7B are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that specifically target Lys11-linked polyubiquitin. OTUD7A, also called zinc finger protein Cezanne 2, has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. OTUD7B, also called zinc finger protein Cezanne, functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7 proteins belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. They are classified as family C64 cysteine proteases by MEROPS.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  193 TLEDIKRAN---KSQEC--LIPVHVDGDGHCLVHAVSRALVG---RELFW----------HALRENLKQH--FQQHLARY 252
Cdd:cd22768    6 SLEQAGRLNwwaKDGGCqrLLPLATTGDGNCLLHAASLGMWGfhdRLLTLrkalyetltsSAAKEALKRRwrWQQTQVNK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  253 QAlfhDFIDAA-----EWEDIIN--------ECDPLFVPPEGVPLG---------LRNIHIFGLANVLHRPII------L 304
Cdd:cd22768   86 EA---GLVYSEeewerEWKSLLKlasteprsQPSPSSGSELEEVIEnssdptyesLEEIHVFVLAHVLRRPIIvvadtmL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  305 LDslsgmrSSGDYSA--TF----LPGLIPAEKCtgrdgHLNkPICIAWSSSgrnHYIPLV 358
Cdd:cd22768  163 RD------SNGEPLApiPFggiyLPLECPPSEC-----HRS-PLVLAYDAA---HFSALV 207

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  207 LIPVHVDGDGHCLVHAVSRALVGRELFWHA--LRENLKQHFQQHLARYQ-ALFHDFIDAAEWEDIINE-------CDplf 276
Cdd:cd22758    6 FEIRDVPGDGNCFFHAVSDQLYGNGIEHSHkeLRQQAVNYLRENPELYDgFFLSEFDEEESWEEYLNRmskdgtwGD--- 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 70778826  277 vppegvplglrNIHIFGLANVLHRPIILLDSLSGMR 312
Cdd:cd22758   83 -----------HIILQAAANLFNVRIVIISSDGSDE 107

OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is also called TRAF-binding domain-containing protein, Trabid, or zinc finger Ran-binding domain-containing protein 1. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin; it also cleaves 'Lys-63'-linked chains with less efficiency. ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. Drosophila Trabid interacts with TGF-beta Activating Kinase 1 (TAK1), which triggers both immunity and apoptosis, resulting in reduced immune signaling output and K63-linked ubiquitination. ZRANB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. ZRANB1 does not contain the conserved aspartate, and uses cysteine and histidine as a catalytic dyad. It is classified as a family C64 cysteine protease by MEROPS.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  216 GHCLVHAVSRALVG---RELFWH-ALRENLK-------QHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPeGVPL 284
Cdd:cd22767   37 GDCLLDSVLQATWGvfdRDNVLRrALADSLHdcahwfySRWKEYESWQAQSLGYSLEEEQWQKDWAFLLSLASQP-GASL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778826  285 glRNIHIFGLANVLHRPIILL----------DSLSGMRSSGDYsatfLPGLIPAEKCTgrdghlNKPICIAWSssgRNHY 354
Cdd:cd22767  116 --EQTHIFALAHILRRPIIVYgvkyvksfrgETLGYARFQGVY----LPLLWEQSFCW------KSPIALGYT---RGHF 180

                 ....*
gi 70778826  355 IPLVG 359
Cdd:cd22767  181 SALVP 185

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 70778826  776 IRITTNDGRQSmVTLKPSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPP------QAGmekepvpLQHGDRI 845
Cdd:cd17055    3 LRVRSRDGTER-VEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGPDLLTAKssatlsQLG-------LKHGDMV 70

OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70778826  210 VHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFhdFIDAAEWEDIINE 271
Cdd:cd22755    4 IKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLL--RSDYESVEEYLEK 63