OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs 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 300795225  51 EFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLAKPG 130
Cdd:cd22770    1 NFVSFANQLQALGLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDDVPFDKHVANLSKPG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795225 131 TFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKSSARELHIAYRYGEHYDSVRRINDNSEAP 195
Cdd:cd22770   81 TYAGNDAIVAFARLHQVNVVIHQLNAPLWQIRGTEKSSSRELHISYHNGDHYSSVRKLGDNSENP 145

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs 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 300795225  51 EFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLAKPG 130
Cdd:cd22770    1 NFVSFANQLQALGLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDDVPFDKHVANLSKPG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795225 131 TFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKSSARELHIAYRYGEHYDSVRRINDNSEAP 195
Cdd:cd22770   81 TYAGNDAIVAFARLHQVNVVIHQLNAPLWQIRGTEKSSSRELHISYHNGDHYSSVRKLGDNSENP 145

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795225  16 RRAEAERKRDERAA--RRALAKERRNRPEPGSsgceEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLE-GHSRNHL 92
Cdd:COG5539  125 FQAERYSLRDASVAklREVVSLEVLSNPDLYN----PAILEIDVIAYATWIVKPDSQGDGCIEIAIISDQLPvRIHVVDV 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795225  93 KHRQETV----DYMIRQREDFEPFVEDDI-----PFEKHVASLAKPGTFAGNDAIVAFArnHQLNVVIHQLNAPLWQIRG 163
Cdd:COG5539  201 DKDSEDRynshPYVQRISILFTGIHFDEEtlamvLWDTYVNEVLFDASDGITIEIQQLA--SLLKNPHYYTNTASPSIKC 278

                        170       180
                 ....*....|....*....|....*..
gi 300795225 164 TDKSSARELHI-AYRYGE---HYDSVR 186
Cdd:COG5539  279 NICGTGFVGEKdYYAHALatgHYNFGE 305

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs 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 300795225  51 EFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLAKPG 130
Cdd:cd22770    1 NFVSFANQLQALGLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDDVPFDKHVANLSKPG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795225 131 TFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKSSARELHIAYRYGEHYDSVRRINDNSEAP 195
Cdd:cd22770   81 TYAGNDAIVAFARLHQVNVVIHQLNAPLWQIRGTEKSSSRELHISYHNGDHYSSVRKLGDNSENP 145

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795225  63 GLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLAKPGTFAGNDAIVAFA 142
Cdd:cd22771    1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDDETFEDYVSRMREDGTWGGNLELQAAS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 300795225 143 RNHQLNVVIHQLNAPLWQIRGTDKSSARELHIAYRYGEHYDSVR 186
Cdd:cd22771   81 LVYRVNIVVHQLGQPRWEIENFPDKGARTIHLSYHDGEHYNSVR 124

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2, vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), fungal OTU domain-containing protein 2 (OTU2), and similar proteins. OTUD6A, OTUD6B, and Schizosaccharomyces pombe OTU2 are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. This subfamily belongs 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 300795225  59 LQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKH-----RQETVDYMIRQREDFEPFV-------EDDIPFEKHVASL 126
Cdd:cd22748    1 LKPLGLRIKEIPPDGHCLYRAIADQLKLRGGSEEPYsykelRKLAADYMRAHRDDFLPFLtnddgdlMTEEEFEEYCDKI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795225 127 AKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLwQIRGTDKSSARELHIAY-RY----GEHYDSVR 186
Cdd:cd22748   81 ENTAEWGGQLELRALSKALKRPIHVYQAGSPP-LVIGEEFDSGEPLRLSYhRHayglGEHYNSVV 144

OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This subfamily contains Arabidopsis thaliana deubiquitinating enzymes OTU8, OTU9, OTU10, OTU11, and OTU12, and similar proteins from plants and other eukaryotes. OTU8-OTU12 are 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 300795225  59 LQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDiPFEKHVASLAKPGTFAGNDAI 138
Cdd:cd22751    5 LDLYGLVERKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELYYEFYVPE-EYDEYLKKMSKDGEWGDELTL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300795225 139 VAFARNHQLNVVI---HQLNAPL-WQIRGTDKSSaRELHIAYRYGEHYDSVR 186
Cdd:cd22751   84 QAAADAFGVKIHVitsFEDNWFLeIEPRGLVRSK-RVLFLSYWAEVHYNSIY 134

OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, is a deubiquitinase that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. OTUD4 belongs 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 300795225  59 LQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDdiPFEKHVASLAKPGTFAGNDAI 138
Cdd:cd22794    5 LRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEG--PFEQYLKNLENPKEWAGQVEI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 300795225 139 VAFARNHQLNVVIHQ-LNAPlwQIRGTDKSSARELHIAYRYGEHYDSV 185
Cdd:cd22794   83 SALSLMYKRDFIIYQePGKP--PSNVTENGFPDKILLCFSNGNHYDSV 128

OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; This subfamily includes Schizosaccharomyces pombe and Saccharomyces cerevisiae OTU domain-containing protein 2 (OTU2) and similar proteins. S. pombe OTU2 is a ubiquitin thioesterase/hydrolase (EC 3.4.19.12) that can remove conjugated ubiquitin from protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Fungal OTU2 bbelongs 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 300795225  59 LQALGLKLREVPGDGNCLFRALGDQLEGH----SRNHLKHRQETVDYMIRQREDFEPFV----EDDIPFEKHVASLAKPG 130
Cdd:cd22762    2 LEELGLEEHDIKPDGHCLFAAIADQLQLRgseiNLDYKELRKLAAEYIRKHPDDFEPFLfeetDELEDIDEYCKKIENTA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795225 131 TFAGNDAIVAFARnhQLNVVIH--QLNAPLWQIRGTDKSSARELHIAYrY------GEHYDSVR 186
Cdd:cd22762   82 EWGGELELLALAK--AFGVPIHvvQAEGRVIKINEEGDSDKPELWLAY-YkhsyglGEHYNSLR 142

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes 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. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs 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 300795225  63 GLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDipFEKHVASLAKPGTFAGNDAIVAFA 142
Cdd:cd22796    4 GLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTED--FTQYVKRKRRDRVFGNNLEIQAMS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 300795225 143 R--NHQLNVVIHQLNAPLWQIRGTDKSSARELHIAYRYGEHYDSV 185
Cdd:cd22796   82 EiyNRPIEVYSYSNGEPINIFHGSYEGDDPPIRLSYHDGNHYNSI 126

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 300795225   70 PGDGNCLFRALGDQLEGHSRNHLKH-----RQETVDYMIRQREDFEPFVEDDipFEKHVASLAKPGTFAGndAIVAFARN 144
Cdd:pfam02338   1 PGDGNCLYRSISHQLWGVHDVLRKMlvqelRETLAEYMREHKEEFEPFLEDD--ETGDIIEIEQTGAWGG--EIEIFALA 76

                          90
                  ....*....|..
gi 300795225  145 HQLNVVIHQLNA 156
Cdd:pfam02338  77 HILRRPIIVYKS 88

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795225  64 LKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVE-DDIPFEKHVASLAKP--GTFAGNDAIVA 140
Cdd:cd22755    1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRsDYESVEEYLEKSRMRydGTWATDVEIFA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300795225 141 FArnHQLNVVIH--QLNAPLWQI-RGTDKSSARELHIAYRY-----GEHYDSV 185
Cdd:cd22755   81 AA--TLLGVDIYvySKGGYKWLLySPRFKLGKRNGSREAIYlkntnGNHFEPV 131

OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The VP80 protein is a capsid-associated structural protein that was first identified as P87 in Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV); its homologs are found only in NPV genomes. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both budded virus (BV) and occlusion-derived virus (ODV). It has also been shown to interact with the virus-triggered, nuclear F-actin cytoskeleton. P87/VP80 contains an N-terminal 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 300795225  65 KLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDD-----IPFEKHVASLAKPGTFAGNDAIV 139
Cdd:cd22757    2 RVIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSegnnyKSAEEYRADMSKPGTYGTLCELV 81

                         90
                 ....*....|....
gi 300795225 140 AFARNHQLNVVIHQ 153
Cdd:cd22757   82 AAAELYPFHFEVYR 95

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; Deubiquitinating enzyme OTU4, also called OTU domain-containing protein 4, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes 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. OTU4 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU4 belongs 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795225  69 VPGDGNCLFRAL----GDQLEGHSRNHLKHRQE-------TVDYMIRQREDFEPFVEDDipFEKHVASLAKPGTFAG 134
Cdd:cd22760    7 IAGDGRCLFRAVahgeCLARGKAAPDEERERELadelrtrAADELVKRREETEWFIEGD--FDEYVARMRRPGVWGG 81

OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU domain-containing protein that is required for the development of thoracic vertebrae in mammals. 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. Vertnin and some subfamily members do not possess the conserved catalytic residues and may not have DUB activity. VRTN gene is associated with variations in vertebral number.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795225  69 VPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPfveddiPFEKHVASLAKPGTFAGNDAIVAFA 142
Cdd:cd22791    6 VTGDGNCLFRAASLLLFGDESLHLELRLRTVLELVLNSEFYEA------IYEAEIKATCKPGSYSGIWHIYALS 73

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795225  16 RRAEAERKRDERAA--RRALAKERRNRPEPGSsgceEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLE-GHSRNHL 92
Cdd:COG5539  125 FQAERYSLRDASVAklREVVSLEVLSNPDLYN----PAILEIDVIAYATWIVKPDSQGDGCIEIAIISDQLPvRIHVVDV 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795225  93 KHRQETV----DYMIRQREDFEPFVEDDI-----PFEKHVASLAKPGTFAGNDAIVAFArnHQLNVVIHQLNAPLWQIRG 163
Cdd:COG5539  201 DKDSEDRynshPYVQRISILFTGIHFDEEtlamvLWDTYVNEVLFDASDGITIEIQQLA--SLLKNPHYYTNTASPSIKC 278

                        170       180
                 ....*....|....*....|....*..
gi 300795225 164 TDKSSARELHI-AYRYGE---HYDSVR 186
Cdd:COG5539  279 NICGTGFVGEKdYYAHALatgHYNFGE 305