Species | Cyberlindnera fabianii | |||||||||||
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Lineage | Ascomycota; Saccharomycetes; ; Phaffomycetaceae; Cyberlindnera; Cyberlindnera fabianii | |||||||||||
CAZyme ID | ONH68623.1 | |||||||||||
CAZy Family | GT3 | |||||||||||
CAZyme Description | Cell surface mannoprotein MP65 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH17 | 491 | 730 | 2.9e-17 | 0.9228295819935691 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
227625 | Scw11 | 5.16e-68 | 476 | 729 | 44 | 301 | Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism]. |
341098 | ING_Pho23p_like | 8.30e-38 | 45 | 133 | 1 | 89 | Inhibitor of growth (ING) domain of yeast Pho23p and similar proteins. This family is composed of Saccharomyces cerevisiae transcriptional regulatory protein PHO23 (Pho23p), Schizosaccharomyces pombe chromatin modification-related protein png2 (also called ING1 homolog 2), and similar proteins. Pho23p is part of Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Pho23p inhibits p53-dependent transcription. The related mammalian ING proteins act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain that binds unmodified H3 tails, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3). Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail. |
404028 | ING | 8.24e-15 | 37 | 137 | 1 | 100 | Inhibitor of growth proteins N-terminal histone-binding. Histones undergo numerous post-translational modifications, including acetylation and methylation, at residues which are then probable docking sites for various chromatin remodelling complexes. Inhibitor of growth proteins (INGs) specifically bind to residues that have been thus modified. INGs carry a well-characterized C-terminal PHD-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3), as well as this N-terminal domain that binds unmodified H3 tails. Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail. |
366033 | Glyco_hydro_17 | 4.40e-04 | 602 | 729 | 152 | 297 | Glycosyl hydrolases family 17. |
341089 | ING | 4.65e-04 | 48 | 118 | 4 | 73 | Inhibitor of growth (ING) domain family. The Inhibitor of growth (ING) family includes a group of tumor suppressors, ING1-5, which act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation, and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain that binds unmodified H3 tails, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain, which binds lysine 4-tri-methylated histone H3 (H3K4me3). Although these two regions can bind histones independently, together they increase the apparent association of the ING domain for the H3 tail. The ING family also includes three yeast orthologs, chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays a critical role in intra-S-phase DNA damage response. Pho23p is part of Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.40e-275 | 330 | 731 | 63 | 464 | |
6.34e-82 | 479 | 731 | 142 | 390 | |
8.68e-81 | 476 | 731 | 115 | 366 | |
1.11e-80 | 476 | 731 | 123 | 374 | |
2.54e-80 | 476 | 731 | 151 | 402 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.97e-74 | 476 | 728 | 135 | 385 | Probable family 17 glucosidase SCW10 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SCW10 PE=1 SV=1 |
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4.93e-74 | 470 | 728 | 126 | 382 | Probable family 17 glucosidase SCW4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SCW4 PE=1 SV=1 |
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1.63e-70 | 476 | 729 | 125 | 376 | Cell surface mannoprotein MP65 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MP65 PE=1 SV=3 |
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8.71e-37 | 474 | 730 | 305 | 562 | Probable beta-glucosidase btgE OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=btgE PE=3 SV=2 |
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8.71e-37 | 474 | 730 | 305 | 562 | Probable beta-glucosidase btgE OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=btgE PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000041 | 0.000000 |
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