ID A0A7T7IGF3_9HYPO Unreviewed; 94 AA. AC A0A7T7IGF3; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 02-OCT-2024, entry version 13. DE RecName: Full=Histone H3 {ECO:0000256|ARBA:ARBA00020835}; DE Flags: Fragment; OS Dactylonectria sp. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Dactylonectria. OX NCBI_TaxID=1925737 {ECO:0000313|EMBL:QQL06444.1}; RN [1] {ECO:0000313|EMBL:QQL06444.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RRD_53 {ECO:0000313|EMBL:QQL06444.1}; RX PubMed=33376252; RA Grunewaldt-Stocker G., Popp C., Baumann A., Fricke S., Menssen M., RA Winkelmann T., Maiss E.; RT "Observations on early fungal infections with relevance for replant disease RT in fine roots of the rose rootstock Rosa corymbifera 'Laxa'."; RL Sci. Rep. 10:0-22410(2020). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact CC DNA into chromatin, limiting DNA accessibility to the cellular CC machineries which require DNA as a template. Histones thereby play a CC central role in transcription regulation, DNA repair, DNA replication CC and chromosomal stability. DNA accessibility is regulated via a complex CC set of post-translational modifications of histones, also called CC histone code, and nucleosome remodeling. CC {ECO:0000256|ARBA:ARBA00002001}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the histone H3 family. CC {ECO:0000256|ARBA:ARBA00010343}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN961641; QQL06444.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7T7IGF3; -. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0009303; P:rRNA transcription; IEA:TreeGrafter. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR PANTHER; PTHR11426:SF268; HISTONE H3; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. PE 3: Inferred from homology; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}. FT DOMAIN 5..94 FT /note="Histone H2A/H2B/H3" FT /evidence="ECO:0000259|Pfam:PF00125" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QQL06444.1" FT NON_TER 94 FT /evidence="ECO:0000313|EMBL:QQL06444.1" SQ SEQUENCE 94 AA; 10744 MW; EC2CC19E72AD5FED CRC64; RKSAPSTGGV KKPHRYKPGT VALREIRRYQ KSTELLIRKL PFQRLVREIA QDFKSDLRFQ SSAIGALQES VESYLVSLFE DTNLCAIHAK RVTI //