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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 142 FIKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPfvtrgdlEGKASLHDQDIFGTFLTQSQESGFWGGDH 221
Cdd:cd22744     4 DVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEP-------AELADEDDGEDFDEYLQRMRKPGTWGGEL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1321526182 222 HLVALSCAYQIRLVVLSHEGRTYDNI---PGSEQPTRTIFLWYNGANHYEII 270
Cdd:cd22744    77 ELQALANALNVPIVVYSEDGGFLPVSvfgPGPGPSGRPIHLLYTGGNHYDAL 128

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182  624 ITKPALKRTPESPATLPTTNKAPEKPQEPCQPLATPlaTEKAPEKPKQTRFAPLYPSPSPQPPTITFGPP 693
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP--QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG 2953

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 142 FIKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPfvtrgdlEGKASLHDQDIFGTFLTQSQESGFWGGDH 221
Cdd:cd22744     4 DVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEP-------AELADEDDGEDFDEYLQRMRKPGTWGGEL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1321526182 222 HLVALSCAYQIRLVVLSHEGRTYDNI---PGSEQPTRTIFLWYNGANHYEII 270
Cdd:cd22744    77 ELQALANALNVPIVVYSEDGGFLPVSvfgPGPGPSGRPIHLLYTGGNHYDAL 128

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 443 FYHALSYWMHGHQDLHEVIRRRVVDGLGKiipqmKPKKKEHSILSAILNPEDPRGIVNLVS-DYTSASEgrkpgrTALLA 521
Cdd:cd22744    12 LFRALAHALYGDQESHRELRQEVVDYLRE-----NPDLYEPAELADEDDGEDFDEYLQRMRkPGTWGGE------LELQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1321526182 522 VAGLLRVHLVIVEMGRTGAAWIKCSPqgllFRGITFPTIYLFYNSN 567
Cdd:cd22744    81 LANALNVPIVVYSEDGGFLPVSVFGP----GPGPSGRPIHLLYTGG 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 142 FIKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPfvtrgdlEGKASLHDQDIFGTFLTQSQESGFWGGDH 221
Cdd:cd22744     4 DVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEP-------AELADEDDGEDFDEYLQRMRKPGTWGGEL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1321526182 222 HLVALSCAYQIRLVVLSHEGRTYDNI---PGSEQPTRTIFLWYNGANHYEII 270
Cdd:cd22744    77 ELQALANALNVPIVVYSEDGGFLPVSvfgPGPGPSGRPIHLLYTGGNHYDAL 128

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This subfamily includes bilaterial OTU domain-containing protein 3 (OTUD3), Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, and similar proteins. 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. OTU7 is a DUB that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. 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 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGDlegkaslhDQDIFGTF---LTQSQESGFWGG 219
Cdd:cd22756     5 ITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFSEAAT--------FAEDDEAFedyLARMAKDGTYGD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1321526182 220 DHHLVALSCAYQIRLVVLSHEGR---TYDNIPGSEQPTRTIFLWYNGANHY 267
Cdd:cd22756    77 NLEIVAFARAYNVDVKVYQPDPVyviSAPEDGSPGPARRVLHIAYHNWEHY 127

OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU domain-containing protein 5 (OTUD5), also called deubiquitinating enzyme A (DUBA), is a phosphorylation-dependent deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can hydrolyze 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, and may function as negative regulator of the innate immune system. It limits type I interferon production in macrophages and suppresses interleukin-17A production in T cells. OTUD5 also functions in an apoptotic signaling cascade by mediating the sequential activation of PDCD5 (programmed cell death 5) and p53 in response to genotoxic stress. In Drosophila, OTUD5/DUBA is essential for spermatogenesis. This subfamily also includes Arabidopsis thaliana OTU domain-containing protein 6, also called deubiquitinating enzyme OTU6 or otubain-like deubiquitinase 1 (OTLD1), which binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It also includes plant OTU6.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGdlegkaslhdqdiFGTFLTQSQESGFWGGDHH 222
Cdd:cd22752     7 MEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTED-------------FEEYINRKRQDGVWGNHIE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1321526182 223 LVALSCAYQIRLVVLShegrtYDNIP------GSEQPTRTIFLWYNGANHY 267
Cdd:cd22752    74 IQAMSELYNRPIEVYA-----YSTEPintfheASSSDNEPIRLSYHGNSHY 119

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 and similar proteins; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is alco called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). This subfamily also contains OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, a DUB that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. 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 1321526182 133 LDGWKISHGF----IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVtrgdlegkaslhdQDIFGTFL 208
Cdd:cd22753     1 IDEYLDSLGLyrkhIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFS-------------EISFDDYL 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1321526182 209 TQSQESGFWGGDHHLVALSCAYQIRLVVLSHEGRTYDNIPGSEQPtRTIFLWYNGANHYEII 270
Cdd:cd22753    68 ERLSDPKEWGGLLELEALSLLYKVDFIVYSIPDQPPSNITNNGYP-KKIMLCYSGGNHYDSV 128

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 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGDLEGkaslhdqdifgtFLTQSQESGFWgGDH- 221
Cdd:cd22751    15 VEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELYYEFYVPEEYDE------------YLKKMSKDGEW-GDEl 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1321526182 222 HLVALSCAYQIRLVVL-SHEGRTYDNI--PGSEQPTRTIFLWYNGANHYEII 270
Cdd:cd22751    82 TLQAAADAFGVKIHVItSFEDNWFLEIepRGLVRSKRVLFLSYWAEVHYNSI 133

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 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVtrgdlEGKaslhdqdiFGTFLTQSQESGFWGGDHH 222
Cdd:cd22794    15 IAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFI-----EGP--------FEQYLKNLENPKEWAGQVE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1321526182 223 LVALSCAYQIRLVVLSHEGRTYDNIPGSEQPTRtIFLWYNGANHYEIIW 271
Cdd:cd22794    82 ISALSLMYKRDFIIYQEPGKPPSNVTENGFPDK-ILLCFSNGNHYDSVY 129

OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU domain-containing protein 1 (OTUD1), also called DUBA-7 in humans, is a deubiquitinating enzyme/ubiquitinyl hydrolase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin; this specificity is facilitated by the C-terminal Ub-interacting motif (UIM) of OTUD1. It interacts and promotes the deubiquitination of myeloid cell leukemia 1 (MCL1), a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumorigenesis. OTUD1 also deubiquitinates IFN regulatory factor 3 (IRF3) and attenuates its function; IRF3 is critical for the transcription of type I IFNs in defensing virus and promoting inflammatory responses. Loss-of-function mutations of OTUD1 associated with multiple autoimmune diseases including systemic lupus erythematosus (SLE), rheumatoid arthritis (RA), ulcerative colitis (UC) and Hashimoto's thyroiditis (HT). OTUD1 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 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFvtrgdLEGKAslhdqdifGTFLTQSQESGFWGGDHH 222
Cdd:cd22747    26 IIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPI-----IEGDV--------GEFLIKAAQDGAWAGYPE 92

                  ....*
gi 1321526182 223 LVALS 227
Cdd:cd22747    93 LLAMG 97

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which 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 1321526182 143 IKGDGNCLFRAVATW--VCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTR---GDLEgkaslhDQDIFGTFLTQSQESGFW 217
Cdd:cd22761    15 IPSDGDCLYNAIAHQlsLRGIETSVEELRKQTADYMRENKDDFLPFLTNpdtGDPL------TEEEFEKYCDDVENTGAW 88

                          90       100
                  ....*....|....*....|....*
gi 1321526182 218 GGDHHLVALSCAYQIRLVVLSHEGR 242
Cdd:cd22761    89 GGQLELRALSHVLKRPIEVIQAEGP 113

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 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGDLEGKASLHDQdifgtFLTQSQeSGFWGGDHH 222
Cdd:cd22757     6 IPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSEGNNYKSAEEY-----RADMSK-PGTYGTLCE 79

                          90
                  ....*....|....
gi 1321526182 223 LVALSCAYQIRLVV 236
Cdd:cd22757    80 LVAAAELYPFHFEV 93

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 1321526182 144 KGDGNCLFRAVATWVCGDQEA-----HQEVRGKCCKEMAQNPDKYLPFVtrgdlegkaslhdQDIFGTFLTQSQESGFWG 218
Cdd:pfam02338   1 PGDGNCLYRSISHQLWGVHDVlrkmlVQELRETLAEYMREHKEEFEPFL-------------EDDETGDIIEIEQTGAWG 67

                          90       100
                  ....*....|....*....|...
gi 1321526182 219 GDHHLVALSCAYQIRLVVLSHEG 241
Cdd:pfam02338  68 GEIEIFALAHILRRPIIVYKSEG 90

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 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 1321526182 146 DGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVtrgdlEGKaslhdqdiFGTFLTQSQESGFWGGDHHLVA 225
Cdd:cd22795    18 DASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYV-----EGS--------FEKYLERLEDPKESAGQLEISA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1321526182 226 LSCAYQIRLVVLSHEGR--TYDNIPGSEQptrTIFLWYNGANHYEIIW 271
Cdd:cd22795    85 LSLIYNRDFILYRYPGKppTYATDNGFED---KILLCCSSNGHYDSVY 129

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 1321526182 443 FYHALSYWMHGHQDLHEVIRRRVVDglgkiipQMKPKKKEHSILSAILNPEdprgivnlVSDYTSASEGRKPGRTA---- 518
Cdd:cd22755    13 FFRALSYAITGSEKYHRKIRKAIVD-------FLEKNPDEFRNLLRSDYES--------VEEYLEKSRMRYDGTWAtdve 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1321526182 519 LLAVAGLLRVHLVIVEMGRTGaaWIKCSPQGLL-FRGITFPTIYLFYNSN 567
Cdd:cd22755    78 IFAAATLLGVDIYVYSKGGYK--WLLYSPRFKLgKRNGSREAIYLKNTNG 125

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 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVtrgdlegkaslHDQDIFGTFLTQSQESGFWGGDHH 222
Cdd:cd22770    19 IPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFV-----------EDDVPFDKHVANLSKPGTYAGNDA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1321526182 223 LVALSCAYQIRLVVlsHE-GRTYDNIPGSEQP-TRTIFLWYNGANHY 267
Cdd:cd22770    88 IVAFARLHQVNVVI--HQlNAPLWQIRGTEKSsSRELHISYHNGDHY 132

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182  624 ITKPALKRTPESPATLPTTNKAPEKPQEPCQPLATPlaTEKAPEKPKQTRFAPLYPSPSPQPPTITFGPP 693
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP--QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG 2953