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Conserved domains on  [gi|1321526182|gb|PLW12683|]
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hypothetical protein PCANC_14441 [Puccinia coronata f. sp. avenae]

Protein Classification

OTU domain-containing protein( domain architecture ID 17784440)

OTU (ovarian tumor) domain-containing protein may function as a deubiquitinase (DUBs)/ubiquitin thiolesterase that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, or may be inactive

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
142-270 1.06e-33

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


:

Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 126.01  E-value: 1.06e-33
                          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 cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
443-567 2.53e-08

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


:

Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 53.21  E-value: 2.53e-08
                          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
PHA03247 super family cl33720
large tegument protein UL36; Provisional
624-693 1.98e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.98e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182  624 ITKPALKRTPESPATLPTTNKAPEKPQEPCQPLATPlaTEKAPEKPKQTRFAPLYPSPSPQPPTITFGPP 693
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP--QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG 2953
 
Name Accession Description Interval E-value
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
142-270 1.06e-33

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 126.01  E-value: 1.06e-33
                          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 pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
144-241 1.24e-08

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.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 53.99  E-value: 1.24e-08
                          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 cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
443-567 2.53e-08

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 53.21  E-value: 2.53e-08
                          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
PHA03247 PHA03247
large tegument protein UL36; Provisional
624-693 1.98e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.98e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182  624 ITKPALKRTPESPATLPTTNKAPEKPQEPCQPLATPlaTEKAPEKPKQTRFAPLYPSPSPQPPTITFGPP 693
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP--QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG 2953
 
Name Accession Description Interval E-value
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
142-270 1.06e-33

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 126.01  E-value: 1.06e-33
                          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_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
143-267 1.56e-24

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.


Pssm-ID: 438608 [Multi-domain]  Cd Length: 124  Bit Score: 99.55  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTrgdlegkaslhDQDIFGTFLTQSQESGFWGGDHH 222
Cdd:cd22771     7 VEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFE-----------DDETFEDYVSRMREDGTWGGNLE 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1321526182 223 LVALSCAYQIRLVVLSHEGRTYDNIPGSEQPTRTIFLWYNGANHY 267
Cdd:cd22771    76 LQAASLVYRVNIVVHQLGQPRWEIENFPDKGARTIHLSYHDGEHY 120
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
143-267 1.29e-19

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.


Pssm-ID: 438593 [Multi-domain]  Cd Length: 131  Bit Score: 85.69  E-value: 1.29e-19
                          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_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
139-267 2.82e-18

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.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 81.93  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 139 SHGFI----KGDGNCLFRAVAtwvcgDQ-------EAHQEVRGKCCKEMAQNPDKYLPFVTRgdlegkaSLHDQDIFGTF 207
Cdd:cd22758     3 ENGFEirdvPGDGNCFFHAVS-----DQlygngieHSHKELRQQAVNYLRENPELYDGFFLS-------EFDEEESWEEY 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321526182 208 LTQSQESGFWgGDHH-LVALSCAYQIRLVVLSHEGRTYDNI--PGSEQPTRTIFLWYNGANHY 267
Cdd:cd22758    71 LNRMSKDGTW-GDHIiLQAAANLFNVRIVIISSDGSDETTIiePGNSKNGRTIYLGHIGENHY 132
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
143-267 3.85e-17

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.


Pssm-ID: 438589 [Multi-domain]  Cd Length: 124  Bit Score: 78.36  E-value: 3.85e-17
                          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_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
143-270 7.84e-17

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.


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 77.69  E-value: 7.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGDlegkASLHDqdifgtFLTQSQE--SGFWGGD 220
Cdd:cd22755     6 IVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDY----ESVEE------YLEKSRMryDGTWATD 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1321526182 221 HHLVALSCAYQIRLVVLSHEGRTY------DNIPGSEQPTRTIFLWYNGANHYEII 270
Cdd:cd22755    76 VEIFAAATLLGVDIYVYSKGGYKWllysprFKLGKRNGSREAIYLKNTNGNHFEPV 131
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
133-270 2.46e-16

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.


Pssm-ID: 438590 [Multi-domain]  Cd Length: 130  Bit Score: 76.04  E-value: 2.46e-16
                          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_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
143-261 7.24e-16

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.


Pssm-ID: 438585 [Multi-domain]  Cd Length: 144  Bit Score: 75.29  E-value: 7.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVAtwvcgDQ----------EAHQEVRGKCCKEMAQNPDKYLPFVTRGDlegkASLHDQDIFGTFLTQSQ 212
Cdd:cd22748    11 IPPDGHCLYRAIA-----DQlklrggseepYSYKELRKLAADYMRAHRDDFLPFLTNDD----GDLMTEEEFEEYCDKIE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1321526182 213 ESGFWGGDHHLVALSCAYQIRLVVLSHEGRTYdNIPGSEQPTRTIFLWY 261
Cdd:cd22748    82 NTAEWGGQLELRALSKALKRPIHVYQAGSPPL-VIGEEFDSGEPLRLSY 129
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
143-270 5.26e-14

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.


Pssm-ID: 438588 [Multi-domain]  Cd Length: 134  Bit Score: 69.88  E-value: 5.26e-14
                          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_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
144-270 9.85e-14

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.


Pssm-ID: 438617 [Multi-domain]  Cd Length: 128  Bit Score: 68.61  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 144 KGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGdlegkaslhdqdiFGTFLTQSQESGFWGGDHHL 223
Cdd:cd22796    11 DGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTED-------------FTQYVKRKRRDRVFGNNLEI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1321526182 224 VALSCAYQIRLVVLSHEGRTYDNI--PGSEQPTRTIFLWYNGANHYEII 270
Cdd:cd22796    78 QAMSEIYNRPIEVYSYSNGEPINIfhGSYEGDDPPIRLSYHDGNHYNSI 126
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
143-271 1.24e-12

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.


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 65.86  E-value: 1.24e-12
                          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_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
143-261 7.99e-12

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.


Pssm-ID: 438599 [Multi-domain]  Cd Length: 142  Bit Score: 63.79  E-value: 7.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVAtwvcgDQ---------EAHQEVRGKCCKEMAQNPDKYLPFVTRGDLEgkaslhDQDIfGTFLTQSQE 213
Cdd:cd22762    12 IKPDGHCLFAAIA-----DQlqlrgseinLDYKELRKLAAEYIRKHPDDFEPFLFEETDE------LEDI-DEYCKKIEN 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1321526182 214 SGFWGGDHHLVALSCAYQIRLVVLSHEGRTYDNIPGSEQPTRTIFLWY 261
Cdd:cd22762    80 TAEWGGELELLALAKAFGVPIHVVQAEGRVIKINEEGDSDKPELWLAY 127
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
143-227 1.28e-10

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.


Pssm-ID: 438584 [Multi-domain]  Cd Length: 149  Bit Score: 60.59  E-value: 1.28e-10
                          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_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
143-227 1.79e-10

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.


Pssm-ID: 438612  Cd Length: 137  Bit Score: 59.54  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVATWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRgdlEGKASLHDqdifGTFltqsqeSGFWggdhH 222
Cdd:cd22791     6 VTGDGNCLFRAASLLLFGDESLHLELRLRTVLELVLNSEFYEAIYEA---EIKATCKP----GSY------SGIW----H 68

                  ....*
gi 1321526182 223 LVALS 227
Cdd:cd22791    69 IYALS 73
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
143-242 1.87e-10

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.


Pssm-ID: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 59.82  E-value: 1.87e-10
                          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_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
143-238 6.50e-10

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.


Pssm-ID: 438618 [Multi-domain]  Cd Length: 149  Bit Score: 58.51  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVA-----TWVCGDQEAHQEVRGKCCKEMAQNPDKYLPFVTRGDLEGKAslhdQDIFGTFLTQSQESGFW 217
Cdd:cd22797    15 IKADGHCLYRAVEdqlqlRGGGAPAPDYQQLRELAADYMRAHPDDFLPFLEDEDEGGDG----DEAFEAYCREVESTAAW 90
                          90       100
                  ....*....|....*....|.
gi 1321526182 218 GGDHHLVALSCAYQIRLVVLS 238
Cdd:cd22797    91 GGQLELGALAHALRRHIKVYS 111
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
143-236 1.39e-09

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.


Pssm-ID: 438594 [Multi-domain]  Cd Length: 128  Bit Score: 56.83  E-value: 1.39e-09
                          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_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
143-268 7.43e-09

OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar proteins; Deubiquitinating enzyme OTU3 (also called OTU domain-containing protein 3) and deubiquitinating enzyme OTU4 (also called OTU domain-containing protein 4) are deubiquitinases (DUBs) or 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. OTU3 and OTU4 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.


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 54.97  E-value: 7.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVATWVCGD------------QEAHQeVRGKCCKEMAQNPDKYlpFVTRGDLEGKaslhdqdiFGTFLTQ 210
Cdd:cd22746     7 VKGDGRCLFRAVARGLALAtggrplserrerADADA-LRKAVVEEIRKRRDEL--FEGSLVIEGD--------FDAYCQR 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321526182 211 SQESGFWGGDHHLVALSCAYQ--IRLVVLSHEGRTYDNIP--GSEQPTR-TIFLWYNGANHYE 268
Cdd:cd22746    76 MSHPDTWGGEPELLMLADVLQrpIAVYLPTPGKGGLRKIQeyGEEYLGGePIRLLYNGGNHYD 138
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
144-241 1.24e-08

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.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 53.99  E-value: 1.24e-08
                          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 cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
443-567 2.53e-08

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 53.21  E-value: 2.53e-08
                          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_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
146-271 6.41e-07

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.


Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 49.42  E-value: 6.41e-07
                          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_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
143-268 4.37e-06

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.


Pssm-ID: 438597 [Multi-domain]  Cd Length: 138  Bit Score: 46.99  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVATWVC------------GDQEAhQEVRGKCCKEMAQNPDKYLPFVtRGDlegkaslhdqdiFGTFLTQ 210
Cdd:cd22760     7 IAGDGRCLFRAVAHGEClargkaapdeerERELA-DELRTRAADELVKRREETEWFI-EGD------------FDEYVAR 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321526182 211 SQESGFWGGDHHLVALSCAYQIRLVVLSHEGRTYDNIP----GSEQPTRT-IFLWYNGANHYE 268
Cdd:cd22760    73 MRRPGVWGGEPELLMLSHVLQRPITVYMADEGEGGLISiaeyGQEYGKGNpIRVLFHGFGHYE 135
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
443-567 2.47e-05

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.


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 44.94  E-value: 2.47e-05
                          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_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
143-270 2.79e-05

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.


Pssm-ID: 438596  Cd Length: 159  Bit Score: 45.41  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 143 IKGDGNCLFRAVatwVCG--------------DQEAHQ---EVRGKCCKEmAQNPDKYLPFVTRGDLEGKaslhdqdiFG 205
Cdd:cd22759     8 VKGDGRCMFRAL---VKGlaankgiflsgreeEQEADElrlAVAEALCRS-EERRRDYEEALIAITVEGS--------LD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 206 TFLTQSQESGFWGGDHHLVALSCAYQIRLVVLSHE--------GRTYdnIP----GSE--------QPTRTIFLWYNGAN 265
Cdd:cd22759    76 RYCRRIQRPDFWGGESELLVLSKMLKQPIIVYIPEseaknggwGSGF--IPiqkyGEEfakgtkgrKGRKPVRLLYSGSN 153

                  ....*
gi 1321526182 266 HYEII 270
Cdd:cd22759   154 HYDLL 158
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
143-267 1.98e-04

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.


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 42.27  E-value: 1.98e-04
                          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
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
145-270 1.63e-03

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 38.74  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182 145 GDGNCLFRAVATwVCGdqEAHQEVRGKCCKEMAQNPDkylpfvtrgdlegkaslhdqdiFGTFLTQSQESGFWGGDHHLV 224
Cdd:cd22792     7 GDGNCFWHSLGH-FLG--LSALELKKLLRDSLFDDPE----------------------LDEELDEQLEPGVYAEDEAIA 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1321526182 225 ALSCAYQIRLVVLSHE-GRTYDNIPGSEqpTRTIFLWYNGaNHYEII 270
Cdd:cd22792    62 AAAKLFGVNICVHDPDeGVLYTFTPNES--SKSIHLLLEN-EHFEPL 105
PHA03247 PHA03247
large tegument protein UL36; Provisional
624-693 1.98e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.98e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321526182  624 ITKPALKRTPESPATLPTTNKAPEKPQEPCQPLATPlaTEKAPEKPKQTRFAPLYPSPSPQPPTITFGPP 693
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP--QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG 2953
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
439-467 2.88e-03

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.


Pssm-ID: 438594 [Multi-domain]  Cd Length: 128  Bit Score: 38.72  E-value: 2.88e-03
                          10        20
                  ....*....|....*....|....*....
gi 1321526182 439 DSSGFYHALSYWMHGHQDLHEVIRRRVVD 467
Cdd:cd22757     9 DGACLFRALSYLLYGTQSRHLEVRKEVVD 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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