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core histone macro-H2A.1 isoform 2 [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
Macro_H2A-like | cd02904 | macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ... |
177-367 | 7.53e-125 | ||||
macrodomain, macroH2A-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 are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant. : Pssm-ID: 394875 Cd Length: 188 Bit Score: 357.01 E-value: 7.53e-125
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H2A | smart00414 | Histone 2A; |
14-119 | 2.26e-63 | ||||
Histone 2A; : Pssm-ID: 197711 Cd Length: 106 Bit Score: 197.56 E-value: 2.26e-63
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COG1754 super family | cl34356 | Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; |
112-160 | 3.37e-03 | ||||
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; The actual alignment was detected with superfamily member COG1754: Pssm-ID: 441360 [Multi-domain] Cd Length: 892 Bit Score: 39.41 E-value: 3.37e-03
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Name | Accession | Description | Interval | E-value | ||||
Macro_H2A-like | cd02904 | macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ... |
177-367 | 7.53e-125 | ||||
macrodomain, macroH2A-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 are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant. Pssm-ID: 394875 Cd Length: 188 Bit Score: 357.01 E-value: 7.53e-125
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H2A | smart00414 | Histone 2A; |
14-119 | 2.26e-63 | ||||
Histone 2A; Pssm-ID: 197711 Cd Length: 106 Bit Score: 197.56 E-value: 2.26e-63
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PTZ00017 | PTZ00017 | histone H2A; Provisional |
4-126 | 2.17e-57 | ||||
histone H2A; Provisional Pssm-ID: 185399 Cd Length: 134 Bit Score: 183.02 E-value: 2.17e-57
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HFD_H2A | cd00074 | histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ... |
13-101 | 3.78e-49 | ||||
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Pssm-ID: 467020 Cd Length: 89 Bit Score: 160.39 E-value: 3.78e-49
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HTA1 | COG5262 | Histone H2A [Chromatin structure and dynamics]; |
4-128 | 8.70e-45 | ||||
Histone H2A [Chromatin structure and dynamics]; Pssm-ID: 227587 [Multi-domain] Cd Length: 132 Bit Score: 150.78 E-value: 8.70e-45
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Macro | pfam01661 | Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ... |
215-329 | 1.52e-35 | ||||
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: 125.76 E-value: 1.52e-35
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YmdB | COG2110 | O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ... |
210-367 | 3.81e-35 | ||||
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: 126.44 E-value: 3.81e-35
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PRK00431 | PRK00431 | ADP-ribose-binding protein; |
209-367 | 9.40e-34 | ||||
ADP-ribose-binding protein; Pssm-ID: 234759 Cd Length: 177 Bit Score: 123.03 E-value: 9.40e-34
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A1pp | smart00506 | Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ... |
205-329 | 5.94e-26 | ||||
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: 101.23 E-value: 5.94e-26
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Histone_H2A_C | pfam16211 | C-terminus of histone H2A; |
89-123 | 1.25e-14 | ||||
C-terminus of histone H2A; Pssm-ID: 465070 Cd Length: 35 Bit Score: 67.17 E-value: 1.25e-14
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COG1754 | COG1754 | Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; |
112-160 | 3.37e-03 | ||||
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; Pssm-ID: 441360 [Multi-domain] Cd Length: 892 Bit Score: 39.41 E-value: 3.37e-03
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Name | Accession | Description | Interval | E-value | ||||
Macro_H2A-like | cd02904 | macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ... |
177-367 | 7.53e-125 | ||||
macrodomain, macroH2A-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 are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant. Pssm-ID: 394875 Cd Length: 188 Bit Score: 357.01 E-value: 7.53e-125
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H2A | smart00414 | Histone 2A; |
14-119 | 2.26e-63 | ||||
Histone 2A; Pssm-ID: 197711 Cd Length: 106 Bit Score: 197.56 E-value: 2.26e-63
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PTZ00017 | PTZ00017 | histone H2A; Provisional |
4-126 | 2.17e-57 | ||||
histone H2A; Provisional Pssm-ID: 185399 Cd Length: 134 Bit Score: 183.02 E-value: 2.17e-57
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PLN00157 | PLN00157 | histone H2A; Provisional |
4-123 | 5.98e-54 | ||||
histone H2A; Provisional Pssm-ID: 177758 Cd Length: 132 Bit Score: 174.27 E-value: 5.98e-54
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HFD_H2A | cd00074 | histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ... |
13-101 | 3.78e-49 | ||||
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Pssm-ID: 467020 Cd Length: 89 Bit Score: 160.39 E-value: 3.78e-49
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PLN00156 | PLN00156 | histone H2AX; Provisional |
2-123 | 7.76e-48 | ||||
histone H2AX; Provisional Pssm-ID: 215080 Cd Length: 139 Bit Score: 158.98 E-value: 7.76e-48
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PLN00153 | PLN00153 | histone H2A; Provisional |
1-126 | 4.23e-45 | ||||
histone H2A; Provisional Pssm-ID: 165721 [Multi-domain] Cd Length: 129 Bit Score: 151.41 E-value: 4.23e-45
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HTA1 | COG5262 | Histone H2A [Chromatin structure and dynamics]; |
4-128 | 8.70e-45 | ||||
Histone H2A [Chromatin structure and dynamics]; Pssm-ID: 227587 [Multi-domain] Cd Length: 132 Bit Score: 150.78 E-value: 8.70e-45
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Macro | pfam01661 | Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ... |
215-329 | 1.52e-35 | ||||
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: 125.76 E-value: 1.52e-35
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YmdB | COG2110 | O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ... |
210-367 | 3.81e-35 | ||||
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: 126.44 E-value: 3.81e-35
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PRK00431 | PRK00431 | ADP-ribose-binding protein; |
209-367 | 9.40e-34 | ||||
ADP-ribose-binding protein; Pssm-ID: 234759 Cd Length: 177 Bit Score: 123.03 E-value: 9.40e-34
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Macro_SF | cd02749 | macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ... |
213-332 | 1.54e-33 | ||||
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: 120.97 E-value: 1.54e-33
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Macro_Af1521_BAL-like | cd02907 | macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ... |
205-350 | 4.75e-33 | ||||
macrodomain, Af1521-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. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain 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: 394877 [Multi-domain] Cd Length: 158 Bit Score: 120.67 E-value: 4.75e-33
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PLN00154 | PLN00154 | histone H2A; Provisional |
2-116 | 1.20e-32 | ||||
histone H2A; Provisional Pssm-ID: 177756 Cd Length: 136 Bit Score: 118.89 E-value: 1.20e-32
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PTZ00252 | PTZ00252 | histone H2A; Provisional |
4-121 | 1.87e-31 | ||||
histone H2A; Provisional Pssm-ID: 240330 Cd Length: 134 Bit Score: 115.83 E-value: 1.87e-31
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Macro_OAADPr_deacetylase | cd02908 | macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ... |
195-365 | 2.14e-29 | ||||
macrodomain, O-acetyl-ADP-ribose (OAADPr) 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. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation. Pssm-ID: 438955 Cd Length: 166 Bit Score: 111.45 E-value: 2.14e-29
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Macro_BAL-like | cd02903 | macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ... |
211-367 | 9.46e-28 | ||||
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: 107.34 E-value: 9.46e-28
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A1pp | smart00506 | Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ... |
205-329 | 5.94e-26 | ||||
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: 101.23 E-value: 5.94e-26
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PRK04143 | PRK04143 | protein-ADP-ribose hydrolase; |
194-361 | 1.97e-21 | ||||
protein-ADP-ribose hydrolase; Pssm-ID: 235225 Cd Length: 264 Bit Score: 92.35 E-value: 1.97e-21
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Macro_Ttha0132-like | cd03330 | Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ... |
205-336 | 1.21e-17 | ||||
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132; 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. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132. Pssm-ID: 394879 Cd Length: 147 Bit Score: 79.01 E-value: 1.21e-17
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Macro_GDAP2-like | cd02905 | macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ... |
206-365 | 4.40e-16 | ||||
macrodomain, GDAP2-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. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis. Pssm-ID: 394876 Cd Length: 169 Bit Score: 74.96 E-value: 4.40e-16
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PLN00155 | PLN00155 | histone H2A; Provisional |
1-56 | 6.43e-15 | ||||
histone H2A; Provisional Pssm-ID: 165723 Cd Length: 58 Bit Score: 68.58 E-value: 6.43e-15
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Histone_H2A_C | pfam16211 | C-terminus of histone H2A; |
89-123 | 1.25e-14 | ||||
C-terminus of histone H2A; Pssm-ID: 465070 Cd Length: 35 Bit Score: 67.17 E-value: 1.25e-14
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HFD_SOS1_rpt2 | cd22915 | second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ... |
22-95 | 2.16e-14 | ||||
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat. Pssm-ID: 467040 Cd Length: 75 Bit Score: 67.65 E-value: 2.16e-14
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Histone | pfam00125 | Core histone H2A/H2B/H3/H4; |
2-85 | 4.17e-12 | ||||
Core histone H2A/H2B/H3/H4; Pssm-ID: 459682 [Multi-domain] Cd Length: 126 Bit Score: 62.84 E-value: 4.17e-12
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HFD_ABTB2-like | cd22913 | histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ... |
11-91 | 2.39e-10 | ||||
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, which has implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). This subfamily also includes BTB/POZ domain-containing protein 11 (BTBD11), also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11. It is a BTB-domain-containing Kelch-like protein with unknown function. Pssm-ID: 467038 Cd Length: 105 Bit Score: 56.92 E-value: 2.39e-10
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BUR6 | COG5247 | Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription]; |
23-103 | 3.10e-05 | ||||
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription]; Pssm-ID: 227572 Cd Length: 113 Bit Score: 42.64 E-value: 3.10e-05
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COG1754 | COG1754 | Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; |
112-160 | 3.37e-03 | ||||
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; Pssm-ID: 441360 [Multi-domain] Cd Length: 892 Bit Score: 39.41 E-value: 3.37e-03
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Blast search parameters | ||||
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