ID A0A024UKI8_9STRA Unreviewed; 136 AA.
AC A0A024UKI8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Histone H3 {ECO:0000256|RuleBase:RU004471};
GN ORFNames=DYB32_004149 {ECO:0000313|EMBL:RHY30664.1}, DYB32_006648
GN {ECO:0000313|EMBL:RHY27642.1}, H310_02028
GN {ECO:0000313|EMBL:ETW07529.1}, H310_02964
GN {ECO:0000313|EMBL:ETW06819.1}, H310_05809
GN {ECO:0000313|EMBL:ETW02258.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW06819.1};
RN [1] {ECO:0000313|EMBL:ETW06819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW06819.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RHY27642.1, ECO:0000313|Proteomes:UP000285060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM0002 {ECO:0000313|EMBL:RHY27642.1,
RC ECO:0000313|Proteomes:UP000285060};
RA Minardi D., Oidtmann B., Van Der Giezen M., Studholme D.J.;
RT "Aphanomyces genome sequencing and annotation.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RU004471}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC {ECO:0000256|ARBA:ARBA00010343, ECO:0000256|RuleBase:RU004471}.
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DR EMBL; KI913961; ETW02258.1; -; Genomic_DNA.
DR EMBL; KI913955; ETW06819.1; -; Genomic_DNA.
DR EMBL; KI913954; ETW07529.1; -; Genomic_DNA.
DR EMBL; QUSY01000733; RHY27642.1; -; Genomic_DNA.
DR EMBL; QUSY01000287; RHY30664.1; -; Genomic_DNA.
DR RefSeq; XP_008863622.1; XM_008865400.1.
DR RefSeq; XP_008864894.1; XM_008866672.1.
DR RefSeq; XP_008868863.1; XM_008870641.1.
DR AlphaFoldDB; A0A024UKI8; -.
DR SMR; A0A024UKI8; -.
DR STRING; 157072.A0A024UKI8; -.
DR EnsemblFungi; H310_02028-t26_1; H310_02028-t26_1-p1; H310_02028.
DR EnsemblFungi; H310_02964-t26_1; H310_02964-t26_1-p1; H310_02964.
DR EnsemblFungi; H310_05809-t26_1; H310_05809-t26_1-p1; H310_05809.
DR EnsemblProtists; ETW02258; ETW02258; H310_05809.
DR EnsemblProtists; ETW06819; ETW06819; H310_02964.
DR EnsemblProtists; ETW07529; ETW07529; H310_02028.
DR GeneID; 20079078; -.
DR GeneID; 20080014; -.
DR GeneID; 20082859; -.
DR VEuPathDB; FungiDB:H310_02028; -.
DR VEuPathDB; FungiDB:H310_02964; -.
DR VEuPathDB; FungiDB:H310_05809; -.
DR eggNOG; KOG1745; Eukaryota.
DR OrthoDB; 47297at2759; -.
DR Proteomes; UP000285060; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 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:SF251; 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 Chromosome {ECO:0000256|RuleBase:RU004471};
KW DNA-binding {ECO:0000256|RuleBase:RU004471};
KW Nucleosome core {ECO:0000256|RuleBase:RU004471};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004471};
KW Reference proteome {ECO:0000313|Proteomes:UP000285060}.
FT DOMAIN 1..132
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 136 AA; 15340 MW; ED085C55D3CB5FB0 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQGSAV LALQEAAEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERS
//
