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Database: UniProt
Entry: W4KMU5_HETIT
LinkDB: W4KMU5_HETIT
Original site: W4KMU5_HETIT 
ID   W4KMU5_HETIT            Unreviewed;       103 AA.
AC   W4KMU5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Histone H4 {ECO:0000256|RuleBase:RU000528};
GN   ORFNames=HETIRDRAFT_468325 {ECO:0000313|EMBL:ETW86700.1},
GN   HETIRDRAFT_478720 {ECO:0000313|EMBL:ETW79305.1};
OS   Heterobasidion irregulare (strain TC 32-1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Bondarzewiaceae; Heterobasidion;
OC   Heterobasidion annosum species complex.
OX   NCBI_TaxID=747525 {ECO:0000313|EMBL:ETW86700.1, ECO:0000313|Proteomes:UP000030671};
RN   [1] {ECO:0000313|EMBL:ETW86700.1, ECO:0000313|Proteomes:UP000030671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC 32-1 {ECO:0000313|EMBL:ETW86700.1,
RC   ECO:0000313|Proteomes:UP000030671};
RX   PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA   Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA   Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA   van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA   Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA   Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA   Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E., Lombard V.,
RA   Lucas S., Lunden K., Morin E., Murat C., Park J., Raffaello T., Rouze P.,
RA   Salamov A., Schmutz J., Solheim H., Stahlberg J., Velez H., de Vries R.P.,
RA   Wiebenga A., Woodward S., Yakovlev I., Garbelotto M., Martin F.,
RA   Grigoriev I.V., Stenlid J.;
RT   "Insight into trade-off between wood decay and parasitism from the genome
RT   of a fungal forest pathogen.";
RL   New Phytol. 194:1001-1013(2012).
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|RuleBase:RU000528}.
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. {ECO:0000256|RuleBase:RU000528}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the histone H4 family.
CC       {ECO:0000256|ARBA:ARBA00006564, ECO:0000256|RuleBase:RU000528}.
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DR   EMBL; KI925461; ETW79305.1; -; Genomic_DNA.
DR   EMBL; KI925454; ETW86700.1; -; Genomic_DNA.
DR   RefSeq; XP_009540698.1; XM_009542403.1.
DR   RefSeq; XP_009549550.1; XM_009551255.1.
DR   SMR; W4KMU5; -.
DR   STRING; 747525.W4KMU5; -.
DR   GeneID; 20677224; -.
DR   GeneID; 20677837; -.
DR   KEGG; hir:HETIRDRAFT_468325; -.
DR   KEGG; hir:HETIRDRAFT_478720; -.
DR   eggNOG; KOG3467; Eukaryota.
DR   HOGENOM; CLU_109117_2_3_1; -.
DR   OrthoDB; 2782612at2759; -.
DR   Proteomes; UP000030671; 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   CDD; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR035425; CENP-T/H4_C.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   PANTHER; PTHR10484; HISTONE H4; 1.
DR   PANTHER; PTHR10484:SF0; HISTONE H4; 1.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU000528};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000528};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU000528};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030671}.
FT   DOMAIN          39..96
FT                   /note="CENP-T/Histone H4 histone fold"
FT                   /evidence="ECO:0000259|Pfam:PF15511"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   103 AA;  11366 MW;  AC48D0028C50C948 CRC64;
     MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     IFLENVIRDS VTYTEHAKRK TVTALDVVYA LKRSGRTLYG FGA
//
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