O-acetyl-ADP-ribose deacetylase 1 [Microcebus murinus]
macro domain-containing protein( domain architecture ID 10121048)
macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling, such as ADP-ribose 1''-phosphate phosphatase that is involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Macro_Poa1p-like | cd02901 | macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ... |
13-143 | 7.11e-69 | |||
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation. : Pssm-ID: 394873 Cd Length: 135 Bit Score: 204.41 E-value: 7.11e-69
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Macro_Poa1p-like | cd02901 | macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ... |
13-143 | 7.11e-69 | |||
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation. Pssm-ID: 394873 Cd Length: 135 Bit Score: 204.41 E-value: 7.11e-69
|
|||||||
YmdB | COG2110 | O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ... |
14-151 | 9.38e-13 | |||
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441713 Cd Length: 168 Bit Score: 62.12 E-value: 9.38e-13
|
|||||||
A1pp | smart00506 | Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ... |
13-130 | 1.41e-10 | |||
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji). Pssm-ID: 214701 Cd Length: 133 Bit Score: 55.39 E-value: 1.41e-10
|
|||||||
tk.4 | PHA02595 | hypothetical protein; Provisional |
14-149 | 1.54e-10 | |||
hypothetical protein; Provisional Pssm-ID: 222899 Cd Length: 154 Bit Score: 55.85 E-value: 1.54e-10
|
|||||||
Macro | pfam01661 | Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ... |
40-130 | 5.69e-04 | |||
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site. Pssm-ID: 460286 Cd Length: 116 Bit Score: 37.54 E-value: 5.69e-04
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Macro_Poa1p-like | cd02901 | macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ... |
13-143 | 7.11e-69 | |||
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation. Pssm-ID: 394873 Cd Length: 135 Bit Score: 204.41 E-value: 7.11e-69
|
|||||||
Macro_SF | cd02749 | macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ... |
28-139 | 6.18e-35 | |||
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response. Pssm-ID: 394871 Cd Length: 121 Bit Score: 117.88 E-value: 6.18e-35
|
|||||||
YmdB | COG2110 | O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ... |
14-151 | 9.38e-13 | |||
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441713 Cd Length: 168 Bit Score: 62.12 E-value: 9.38e-13
|
|||||||
A1pp | smart00506 | Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ... |
13-130 | 1.41e-10 | |||
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji). Pssm-ID: 214701 Cd Length: 133 Bit Score: 55.39 E-value: 1.41e-10
|
|||||||
tk.4 | PHA02595 | hypothetical protein; Provisional |
14-149 | 1.54e-10 | |||
hypothetical protein; Provisional Pssm-ID: 222899 Cd Length: 154 Bit Score: 55.85 E-value: 1.54e-10
|
|||||||
PHA03033 | PHA03033 | hypothetical protein; Provisional |
49-139 | 9.24e-07 | |||
hypothetical protein; Provisional Pssm-ID: 165330 Cd Length: 142 Bit Score: 45.74 E-value: 9.24e-07
|
|||||||
Macro_BAL-like | cd02903 | macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ... |
9-141 | 1.12e-04 | |||
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors. Pssm-ID: 394874 Cd Length: 175 Bit Score: 40.31 E-value: 1.12e-04
|
|||||||
Macro | pfam01661 | Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ... |
40-130 | 5.69e-04 | |||
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site. Pssm-ID: 460286 Cd Length: 116 Bit Score: 37.54 E-value: 5.69e-04
|
|||||||
Blast search parameters | ||||
|