Tat interactive protein 60kDa, isoform C [Drosophila melanogaster]
Protein Classification
chromo domain-containing protein( domain architecture ID 13040247)
chromo (chromatin organization modifier) domain-containing protein may bind methylated histone tails
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PLN00104 super family | cl33410 | MYST -like histone acetyltransferase; Provisional |
255-533 | 1.45e-157 | |||||
MYST -like histone acetyltransferase; Provisional The actual alignment was detected with superfamily member PLN00104: Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 456.91 E-value: 1.45e-157
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| CBD_TIP60_like | cd18985 | chromo barrel domain of human tat-interactive protein 60, and similar proteins; ... |
27-90 | 1.42e-39 | |||||
chromo barrel domain of human tat-interactive protein 60, and similar proteins; Tat-interactive protein 60 (also known as KAT5 or HTATIP) catalyzes the acetylation of lysine side chains in various histone and nonhistone proteins, and in itself. It plays roles in multiple cellular processes including remodeling, transcription, DNA double-strand break repair, apoptosis, embryonic stem cell identity, and embryonic development. The TIP60 chromo barrel domain recognizes trimethylated lysine at site 9 of histone H3 (H3K9me3) which triggers TIP60 to acetylate and activate ataxia telangiectasia-mutated kinase, thereby promoting the DSB repair pathway. In a different study, the TIP60 chromo barrel domain was shown to bind H3K4me1, which stabilizes TIP60 recruitment to a subset of estrogen receptor alpha target genes, facilitating regulation of the associated gene transcription. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. : Pssm-ID: 350848 [Multi-domain] Cd Length: 64 Bit Score: 138.10 E-value: 1.42e-39
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| Name | Accession | Description | Interval | E-value | |||||
| PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
255-533 | 1.45e-157 | |||||
MYST -like histone acetyltransferase; Provisional Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 456.91 E-value: 1.45e-157
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| MOZ_SAS | pfam01853 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
316-500 | 2.74e-135 | |||||
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases. Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 389.48 E-value: 2.74e-135
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| SAS2 | COG5027 | Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
241-531 | 7.76e-134 | |||||
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 394.52 E-value: 7.76e-134
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| CBD_TIP60_like | cd18985 | chromo barrel domain of human tat-interactive protein 60, and similar proteins; ... |
27-90 | 1.42e-39 | |||||
chromo barrel domain of human tat-interactive protein 60, and similar proteins; Tat-interactive protein 60 (also known as KAT5 or HTATIP) catalyzes the acetylation of lysine side chains in various histone and nonhistone proteins, and in itself. It plays roles in multiple cellular processes including remodeling, transcription, DNA double-strand break repair, apoptosis, embryonic stem cell identity, and embryonic development. The TIP60 chromo barrel domain recognizes trimethylated lysine at site 9 of histone H3 (H3K9me3) which triggers TIP60 to acetylate and activate ataxia telangiectasia-mutated kinase, thereby promoting the DSB repair pathway. In a different study, the TIP60 chromo barrel domain was shown to bind H3K4me1, which stabilizes TIP60 recruitment to a subset of estrogen receptor alpha target genes, facilitating regulation of the associated gene transcription. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. Pssm-ID: 350848 [Multi-domain] Cd Length: 64 Bit Score: 138.10 E-value: 1.42e-39
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| Tudor-knot | pfam11717 | RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
23-78 | 8.05e-21 | |||||
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is required for binding to RNA. The know influences the loop conformation of the helical turn Ht2 - residues 61-6 3- that is located at the side opposite the knot in the tudor domain-chromodomain; stabilization of Ht2 is essential for RNA binding. Pssm-ID: 432022 [Multi-domain] Cd Length: 55 Bit Score: 85.72 E-value: 8.05e-21
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| CHROMO | smart00298 | Chromatin organization modifier domain; |
38-76 | 1.66e-06 | |||||
Chromatin organization modifier domain; Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 45.28 E-value: 1.66e-06
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| Name | Accession | Description | Interval | E-value | |||||
| PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
255-533 | 1.45e-157 | |||||
MYST -like histone acetyltransferase; Provisional Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 456.91 E-value: 1.45e-157
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| MOZ_SAS | pfam01853 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
316-500 | 2.74e-135 | |||||
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases. Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 389.48 E-value: 2.74e-135
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| SAS2 | COG5027 | Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
241-531 | 7.76e-134 | |||||
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 394.52 E-value: 7.76e-134
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| PLN03238 | PLN03238 | probable histone acetyltransferase MYST; Provisional |
254-533 | 1.40e-130 | |||||
probable histone acetyltransferase MYST; Provisional Pssm-ID: 215642 [Multi-domain] Cd Length: 290 Bit Score: 381.89 E-value: 1.40e-130
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| PLN03239 | PLN03239 | histone acetyltransferase; Provisional |
244-533 | 2.83e-106 | |||||
histone acetyltransferase; Provisional Pssm-ID: 178777 [Multi-domain] Cd Length: 351 Bit Score: 322.37 E-value: 2.83e-106
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| PTZ00064 | PTZ00064 | histone acetyltransferase; Provisional |
234-504 | 8.30e-98 | |||||
histone acetyltransferase; Provisional Pssm-ID: 173359 [Multi-domain] Cd Length: 552 Bit Score: 307.33 E-value: 8.30e-98
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| CBD_TIP60_like | cd18985 | chromo barrel domain of human tat-interactive protein 60, and similar proteins; ... |
27-90 | 1.42e-39 | |||||
chromo barrel domain of human tat-interactive protein 60, and similar proteins; Tat-interactive protein 60 (also known as KAT5 or HTATIP) catalyzes the acetylation of lysine side chains in various histone and nonhistone proteins, and in itself. It plays roles in multiple cellular processes including remodeling, transcription, DNA double-strand break repair, apoptosis, embryonic stem cell identity, and embryonic development. The TIP60 chromo barrel domain recognizes trimethylated lysine at site 9 of histone H3 (H3K9me3) which triggers TIP60 to acetylate and activate ataxia telangiectasia-mutated kinase, thereby promoting the DSB repair pathway. In a different study, the TIP60 chromo barrel domain was shown to bind H3K4me1, which stabilizes TIP60 recruitment to a subset of estrogen receptor alpha target genes, facilitating regulation of the associated gene transcription. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. Pssm-ID: 350848 [Multi-domain] Cd Length: 64 Bit Score: 138.10 E-value: 1.42e-39
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| zf-MYST | pfam17772 | MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ... |
257-311 | 1.60e-26 | |||||
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone acetyltransferases. Pssm-ID: 407644 [Multi-domain] Cd Length: 55 Bit Score: 101.93 E-value: 1.60e-26
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| Tudor-knot | pfam11717 | RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
23-78 | 8.05e-21 | |||||
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is required for binding to RNA. The know influences the loop conformation of the helical turn Ht2 - residues 61-6 3- that is located at the side opposite the knot in the tudor domain-chromodomain; stabilization of Ht2 is essential for RNA binding. Pssm-ID: 432022 [Multi-domain] Cd Length: 55 Bit Score: 85.72 E-value: 8.05e-21
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| CBD_MOF_like | cd18642 | chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
25-86 | 2.39e-14 | |||||
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, and Saccharomyces ESA1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. Pssm-ID: 350844 [Multi-domain] Cd Length: 67 Bit Score: 67.84 E-value: 2.39e-14
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| CBD_ESA1_like | cd18986 | chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ... |
26-85 | 7.35e-12 | |||||
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, and similar proteins; The subgroup includes the chromo barrel domain of NuA4 histone acetyltransferase (HAT) complex catalytic subunit Esa1 (also known as Tas1 and Kat5). Yeast Esa1p acetylates specific histones nonrandomly in H4, H3, and H2A. Esa1 also plays roles in cell cycle progression. In addition, its chromo barrel domain plays a role in the yeast Piccolo NuA4 complex's ability to distinguish between histones and nucleosomes; however, the chromodomain is not required for the Piccolo to bind to nucleosomes. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. Pssm-ID: 350849 [Multi-domain] Cd Length: 65 Bit Score: 60.69 E-value: 7.35e-12
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| CHROMO | smart00298 | Chromatin organization modifier domain; |
38-76 | 1.66e-06 | |||||
Chromatin organization modifier domain; Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 45.28 E-value: 1.66e-06
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| CBD_MOF_like | cd18984 | chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
37-72 | 3.00e-06 | |||||
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domain of Drosophila melanogaster males-absent on the first (MOF) protein. The histone H4 lysine 16 (H4K16)-specific acetyltransferase MOF is part of two distinct complexes involved in X chromosome dosage compensation and autosomal transcription regulation. Its chromobarrel domain is essential for H4K16 acetylation throughout the Drosophila genome and controls spreading of the male-specific lethal (MSL) complex on the X chromosome. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. Pssm-ID: 350847 [Multi-domain] Cd Length: 70 Bit Score: 44.86 E-value: 3.00e-06
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| CBD | cd18643 | chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ... |
35-77 | 3.15e-05 | |||||
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, human male-specific lethal (MSL) complex subunit 3 (MSL3), and retinoblastoma binding protein 1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The chromobarrel domains include a MOF-like subgroup which may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites. Pssm-ID: 350845 [Multi-domain] Cd Length: 61 Bit Score: 41.78 E-value: 3.15e-05
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| MBT_PHF20L1-like | cd20104 | malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ... |
35-84 | 9.59e-03 | |||||
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439094 [Multi-domain] Cd Length: 60 Bit Score: 34.91 E-value: 9.59e-03
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| Blast search parameters | ||||
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