hypothetical protein GUITHDRAFT_160203 [Guillardia theta CCMP2712]
Protein Classification
PLN00104 family protein( domain architecture ID 11476376)
PLN00104 family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
29-383 | 0e+00 | ||||||
MYST -like histone acetyltransferase; Provisional : Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 581.71 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
29-383 | 0e+00 | ||||||
MYST -like histone acetyltransferase; Provisional Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 581.71 E-value: 0e+00
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| MOZ_SAS | pfam01853 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
172-349 | 3.42e-132 | ||||||
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: 376.00 E-value: 3.42e-132
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| SAS2 | COG5027 | Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
33-380 | 1.04e-127 | ||||||
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 372.95 E-value: 1.04e-127
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| CBD_MOF_like | cd18642 | chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
9-54 | 1.24e-06 | ||||||
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: 45.50 E-value: 1.24e-06
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| CHROMO | smart00298 | Chromatin organization modifier domain; |
27-54 | 4.99e-04 | ||||||
Chromatin organization modifier domain; Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 37.96 E-value: 4.99e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
29-383 | 0e+00 | ||||||
MYST -like histone acetyltransferase; Provisional Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 581.71 E-value: 0e+00
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| PLN03238 | PLN03238 | probable histone acetyltransferase MYST; Provisional |
97-382 | 3.21e-153 | ||||||
probable histone acetyltransferase MYST; Provisional Pssm-ID: 215642 [Multi-domain] Cd Length: 290 Bit Score: 433.90 E-value: 3.21e-153
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| MOZ_SAS | pfam01853 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
172-349 | 3.42e-132 | ||||||
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: 376.00 E-value: 3.42e-132
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| SAS2 | COG5027 | Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
33-380 | 1.04e-127 | ||||||
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 372.95 E-value: 1.04e-127
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| PLN03239 | PLN03239 | histone acetyltransferase; Provisional |
34-382 | 1.27e-125 | ||||||
histone acetyltransferase; Provisional Pssm-ID: 178777 [Multi-domain] Cd Length: 351 Bit Score: 366.29 E-value: 1.27e-125
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| PTZ00064 | PTZ00064 | histone acetyltransferase; Provisional |
32-387 | 3.34e-101 | ||||||
histone acetyltransferase; Provisional Pssm-ID: 173359 [Multi-domain] Cd Length: 552 Bit Score: 310.80 E-value: 3.34e-101
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| zf-MYST | pfam17772 | MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ... |
113-167 | 3.47e-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: 99.61 E-value: 3.47e-26
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| Tudor-knot | pfam11717 | RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
25-54 | 1.38e-08 | ||||||
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: 50.67 E-value: 1.38e-08
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| CBD_MOF_like | cd18642 | chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
9-54 | 1.24e-06 | ||||||
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: 45.50 E-value: 1.24e-06
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| CBD_ESA1_like | cd18986 | chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ... |
26-54 | 1.49e-05 | ||||||
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: 42.59 E-value: 1.49e-05
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| CHROMO | smart00298 | Chromatin organization modifier domain; |
27-54 | 4.99e-04 | ||||||
Chromatin organization modifier domain; Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 37.96 E-value: 4.99e-04
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| CBD | cd18643 | chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ... |
33-54 | 1.43e-03 | ||||||
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: 36.77 E-value: 1.43e-03
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| CBD_MSL3_like | cd18983 | chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; ... |
28-54 | 1.70e-03 | ||||||
chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; This subgroup includes human male-specific lethal (MSL) complex subunit 3 (MSL3, also known as MSL3L1). The MSL3 chromodomain specifically recognizes the H4K20 monomethyl mark, in a DNA-dependent manner, and may be involved in chromosomal targeting of the MSL complex. Also included is MORF-related gene on chromosome 15 (MRG15, also known as MORF4L1) which specifically binds to Lys36-methylated histone H3 and plays a role in transcriptional regulation and in DNA repair. This subgroup also includes Arabidopsis thaliana Morf Related Gene 2 (MRG2) which acts as a H3K4me3/H3K36me3 reader involved in the regulation of Arabidopsis flowering. 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. Pssm-ID: 350846 Cd Length: 57 Bit Score: 36.27 E-value: 1.70e-03
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| CBD_MOF_like | cd18984 | chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
33-54 | 3.00e-03 | ||||||
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: 36.00 E-value: 3.00e-03
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| CBD_TIP60_like | cd18985 | chromo barrel domain of human tat-interactive protein 60, and similar proteins; ... |
29-54 | 4.94e-03 | ||||||
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: 35.25 E-value: 4.94e-03
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| NAT_SF | cd04301 | N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
235-281 | 8.51e-03 | ||||||
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included. Pssm-ID: 173926 [Multi-domain] Cd Length: 65 Bit Score: 34.56 E-value: 8.51e-03
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| CBD_RBP1_like | cd18641 | chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; ... |
29-60 | 8.97e-03 | ||||||
chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; Retinoblastoma-binding protein 1 (RBP1), also termed AT-rich interaction domain 4A, is a ubiquitously expressed nuclear protein. RBP1 is a tumor and leukemia suppressor that binds both methylated histone tails and DNA, and is involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. The chromo barrel domain of RBP1 has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. RBP1 binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation; pRB represses transcription by recruiting RBP1. 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. Pssm-ID: 350843 [Multi-domain] Cd Length: 59 Bit Score: 34.56 E-value: 8.97e-03
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| Blast search parameters | ||||
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