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 1204894017 242 RAKGLEVKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQAL 321
Cdd:cd22796     1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1204894017 322 SEMYNRPIHIYSYST-EPINIFHGSYNTDTPPIRLSYHHGNHYNSLVD 368
Cdd:cd22796    81 SEIYNRPIEVYSYSNgEPINIFHGSYEGDDPPIRLSYHDGNHYNSIID 128

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 1204894017 242 RAKGLEVKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQAL 321
Cdd:cd22796     1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1204894017 322 SEMYNRPIHIYSYST-EPINIFHGSYNTDTPPIRLSYHHGNHYNSLVD 368
Cdd:cd22796    81 SEIYNRPIEVYSYSNgEPINIFHGSYEGDDPPIRLSYHDGNHYNSIID 128

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 1204894017 242 RAKGLEVKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQAL 321
Cdd:cd22796     1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1204894017 322 SEMYNRPIHIYSYST-EPINIFHGSYNTDTPPIRLSYHHGNHYNSLVD 368
Cdd:cd22796    81 SEIYNRPIEVYSYSNgEPINIFHGSYEGDDPPIRLSYHDGNHYNSIID 128

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 1204894017 245 GLEVKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEG--FTSYCKRKRRDKVYGNNAEIQALS 322
Cdd:cd22771     1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDDetFEDYVSRMREDGTWGGNLELQAAS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1204894017 323 EMYNRPIHIYSYSTEPINIFHgSYNTDTPPIRLSYHHGNHYNS 365
Cdd:cd22771    81 LVYRVNIVVHQLGQPRWEIEN-FPDKGARTIHLSYHDGEHYNS 122

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 1204894017 242 RAKGLEVKRMLEDGNCLFRAVADQV-----YGDSEAYDLIRQMCIDYMEQERDHFSQFIT---------EGFTSYCKRKR 307
Cdd:cd22748     2 KPLGLRIKEIPPDGHCLYRAIADQLklrggSEEPYSYKELRKLAADYMRAHRDDFLPFLTnddgdlmteEEFEEYCDKIE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1204894017 308 RDKVYGNNAEIQALSEMYNRPIHIYSYSTEPINIfhGSYNTDTPPIRLSYHH-----GNHYNSLV 367
Cdd:cd22748    82 NTAEWGGQLELRALSKALKRPIHVYQAGSPPLVI--GEEFDSGEPLRLSYHRhayglGEHYNSVV 144

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 1204894017 245 GLEVKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQALSEM 324
Cdd:cd22753     9 GLYRKHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLLELEALSLL 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1204894017 325 YNRPIHIYS-YSTEPINIFHGSYNTdtpPIRLSYHHGNHYNSLVD 368
Cdd:cd22753    89 YKVDFIVYSiPDQPPSNITNNGYPK---KIMLCYSGGNHYDSVYS 130

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 1204894017 242 RAKGLEVKRMLEDGNCLFRAVADQVYgDSEAYDL-IRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQA 320
Cdd:cd22794     6 RSLGLYRKQIAKDGSCLFRAVAEQVF-HTQSRHLeVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQVEISA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1204894017 321 LSEMYNRPIHIY-SYSTEPINIfhgSYNTDTPPIRLSYHHGNHYNS 365
Cdd:cd22794    85 LSLMYKRDFIIYqEPGKPPSNV---TENGFPDKILLCFSNGNHYDS 127

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 1204894017 239 DIRRAKGLEVKRMLEDGNCLFRAVADQ--VYGDSEAYDLIRQMCIDYMEQERDHFSQFIT----------EGFTSYCKRK 306
Cdd:cd22761     3 KILKERGLKIHEIPSDGDCLYNAIAHQlsLRGIETSVEELRKQTADYMRENKDDFLPFLTnpdtgdplteEEFEKYCDDV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1204894017 307 RRDKVYGNNAEIQALSEMYNRPIHIYSYSTEPINIfhGSYNTDTPPIRLSYHH-----GNHYNSLV 367
Cdd:cd22761    83 ENTGAWGGQLELRALSHVLKRPIEVIQAEGPPIII--GEEFKSGKPLILTYHRhayglGEHYNSVE 146

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 1204894017 254 DGNCLFRAVADQVYGDSEA-----YDLIRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQALSEMYNRP 328
Cdd:pfam02338   3 DGNCLYRSISHQLWGVHDVlrkmlVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1204894017 329 IHIYsYSTEPINI----FHGSYNTDT--PPIRLSYH-----HGNHY 363
Cdd:pfam02338  83 IIVY-KSEGGEELgglkEYGIYLPLGwdPSLCLVYPrhlyyLGGHY 127

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, 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. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 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 1204894017 245 GLEVKRMLEDGNCLFRAVADQ---VYGDSEAYDL--IRQMCIDYMEQERDHFSQFI---------TEGFTSYCKRKRRDK 310
Cdd:cd22797     9 GLAIKEIKADGHCLYRAVEDQlqlRGGGAPAPDYqqLRELAADYMRAHPDDFLPFLededeggdgDEAFEAYCREVESTA 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1204894017 311 VYGNNAEIQALSEMYNRPIHIYSySTEPINIFHGSYNTDTPPIRLSYH-H----GNHYNSLV 367
Cdd:cd22797    89 AWGGQLELGALAHALRRHIKVYS-AGMPDVEMGEEYAGTGPPLRLCYHrHafglGEHYNSVV 149

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 1204894017 245 GLEVKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEG--FTSYCKRKRRDKVYGNNAEIQALS 322
Cdd:cd22770    13 GLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDDvpFDKHVANLSKPGTYAGNDAIVAFA 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1204894017 323 EMYNRPIHIYSYSTEPINIfHGSYNTDTPPIRLSYHHGNHYNSLvdpRRL 372
Cdd:cd22770    93 RLHQVNVVIHQLNAPLWQI-RGTEKSSSRELHISYHNGDHYSSV---RKL 138

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204894017 254 DGNCLFRAVA------------DQVYGDSEAyDLIRQMCIDYMEQERDHFSQFITEGFTSYCKRKRRDKVYGNNAEIQAL 321
Cdd:cd22760    10 DGRCLFRAVAhgeclargkaapDEERERELA-DELRTRAADELVKRREETEWFIEGDFDEYVARMRRPGVWGGEPELLML 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1204894017 322 SEMYNRPIHIYSYSTE-----PINIFHGSYNTDTpPIRLSYHHGNHYNSLV 367
Cdd:cd22760    89 SHVLQRPITVYMADEGeggliSIAEYGQEYGKGN-PIRVLFHGFGHYEALL 138

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; Deubiquitinating enzyme OTU3, also called OTU domain-containing protein 3, 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. OTU3 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU3 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 1204894017 246 LEVKRMLEDGNCLFRAVAD--------QVYGDSEAYDL--IR-----QMCIDymEQERDHFSQFIT-----EGFTSYCKR 305
Cdd:cd22759     3 YTVVRVKGDGRCMFRALVKglaankgiFLSGREEEQEAdeLRlavaeALCRS--EERRRDYEEALIaitveGSLDRYCRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204894017 306 KRRDKVYGNNAEIQALSEMYNRPIHIY-------------------SYSTEpiniFHGSYNTDTP--PIRLSYHHGNHYN 364
Cdd:cd22759    81 IQRPDFWGGESELLVLSKMLKQPIIVYipeseaknggwgsgfipiqKYGEE----FAKGTKGRKGrkPVRLLYSGSNHYD 156

                  ...
gi 1204894017 365 SLV 367
Cdd:cd22759   157 LLI 159

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 1204894017 248 VKRMLEDGNCLFRAVADQVYGDSEAYDLIRQMCIDYMEQERDHFSQFITEG----FTS---YCKRKRRDKVYGNNAEIQA 320
Cdd:cd22757     3 VIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSegnnYKSaeeYRADMSKPGTYGTLCELVA 82

                          90
                  ....*....|..
gi 1204894017 321 LSEMYNRPIHIY 332
Cdd:cd22757    83 AAELYPFHFEVY 94

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) 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. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204894017 246 LEVKRMLEDGNCLFRAVADQVYGD--SEAYDLiRQMCIDYMEQERDHFsqfiTEGF-----TSYCKRKRRDKVYGNNAEI 318
Cdd:cd22745     3 LVRRVVPDDNSCLFTSISYLLEGGllDSAPEL-REIVADAILSDPDTY----NEAIlgkppDEYCAWILKPDSWGGAIEL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1204894017 319 QALSEMYNrpIHIYSYSTEPINIFHgsYNTDTPP---IRLSYhHGNHYNSLV 367
Cdd:cd22745    78 SILSKHFG--VEICVVDVQTGRVDR--FGEDKGYskrIFLLY-SGIHYDALA 124