ID   H3_ASPCL                Reviewed;         136 AA.
AC   A1CP80;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Histone H3;
GN   Name=hht1; ORFNames=ACLA_021650;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent
CC       H3K14ac formation and is required for transcriptional activation
CC       through TBP recruitment to the promoters (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Mono-, di- and trimethylated by the COMPASS complex to form
CC       H3K4me1/2/3. H3K4me activates gene expression by regulating
CC       transcription elongation and plays a role in telomere length
CC       maintenance. H3K4me enrichment correlates with transcription levels,
CC       and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end
CC       of genes, shifting to H3K4me2 and then H3K4me1. Methylated by set2 to
CC       form H3K36me. H3K36me represses gene expression. Methylated by dot1 to
CC       form H3K79me. H3K79me is required for association of SIR proteins with
CC       telomeric regions and for telomeric silencing. The COMPASS-mediated
CC       formation of H3K4me2/3 and the dot1-mediated formation of H3K79me
CC       require H2BK123ub1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC       H3K14ac formation by gcn5 is promoted by H3S10ph. H3K14ac can also be
CC       formed by esa1. H3K56ac formation occurs predominantly in newly
CC       synthesized H3 molecules during G1, S and G2/M of the cell cycle and
CC       may be involved in DNA repair (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H3K4me1/2/3 =
CC       mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1
CC       = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac =
CC       acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated
CC       Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24;
CC       H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28;
CC       H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac =
CC       acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37;
CC       H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3
CC       = mono-, di- and trimethylated Lys-80. {ECO:0000305}.
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; DS027059; EAW07451.1; -; Genomic_DNA.
DR   RefSeq; XP_001268877.1; XM_001268876.1.
DR   AlphaFoldDB; A1CP80; -.
DR   BMRB; A1CP80; -.
DR   SMR; A1CP80; -.
DR   STRING; 344612.A1CP80; -.
DR   EnsemblFungi; EAW07451; EAW07451; ACLA_021650.
DR   GeneID; 4701152; -.
DR   KEGG; act:ACLA_021650; -.
DR   VEuPathDB; FungiDB:ACLA_021650; -.
DR   eggNOG; KOG1745; Eukaryota.
DR   HOGENOM; CLU_078295_4_0_1; -.
DR   OMA; HFAMART; -.
DR   OrthoDB; 5482964at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..136
FT                   /note="Histone H3"
FT                   /id="PRO_0000297742"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         5
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         5
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         65
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15333 MW;  811AE1772F1DD20C CRC64;
     MARTKQTARK STGGKAPRKQ LASKAARKAA PSTGGVKKPH RYKPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK SDLRFQSSAI GALQESVEAY LVSLFEDTNL CAIHAKRVTI
     QSKDIQLARR LRGERS
//