H3L_ENCCU
ID H3L_ENCCU Reviewed; 140 AA.
AC Q8SQP3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Histone H3-like protein;
GN OrderedLocusNames=ECU09_0450;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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: Mono-, di- and trimethylated to form H3K4me1/2/3. H3K4me activates
CC gene expression by regulating transcription elongation and plays a role
CC in telomere length maintenance. H3K4me enrichment correlates with
CC transcription levels, and occurs in a 5' to 3' gradient with H3K4me3
CC enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC {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; H3K14ac = acetylated Lys-15; H3K14me2 =
CC dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 =
CC monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 =
CC monomethylated Lys-24; H3K56ac = acetylated Lys-56; H3K64ac =
CC acetylated Lys-64. {ECO:0000305}.
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DR EMBL; AL590451; CAD27017.1; -; Genomic_DNA.
DR RefSeq; XP_955598.1; XM_950505.1.
DR AlphaFoldDB; Q8SQP3; -.
DR SMR; Q8SQP3; -.
DR STRING; 284813.Q8SQP3; -.
DR GeneID; 860383; -.
DR KEGG; ecu:ECU09_0450; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_0450; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q8SQP3; -.
DR OMA; SDCERRK; -.
DR OrthoDB; 1564596at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
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; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..140
FT /note="Histone H3-like protein"
FT /id="PRO_0000221361"
FT REGION 1..36
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 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 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 140 AA; 15685 MW; 1FE595B70968305F CRC64;
MSRTKQTASK ALGGKAPRKG ISAKSIPSSG CSPAMPKRTR FKAGALALKE IRKYQKSTDL
LIRKRPFQRM VRDLCKGREG VRFQASAIVA FQEAVENFLT SLMEDAYRCV LHAKRVTLMP
KDICLVYKIK YANILYAALD
