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Database: UniProt
Entry: A0A059LFM8_9CHLO
LinkDB: A0A059LFM8_9CHLO
Original site: A0A059LFM8_9CHLO 
ID   A0A059LFM8_9CHLO        Unreviewed;        96 AA.
AC   A0A059LFM8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   ORFNames=H632_c2724p0 {ECO:0000313|EMBL:KDD72925.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD72925.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD72925.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD72925.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
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:RU003767}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU003767}.
CC   -!- SIMILARITY: Belongs to the histone H2A family.
CC       {ECO:0000256|RuleBase:RU003767}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDD72925.1}.
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DR   EMBL; AYPS01002724; KDD72925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LFM8; -.
DR   STRING; 1291522.A0A059LFM8; -.
DR   OrthoDB; 1424728at2759; -.
DR   Proteomes; UP000026042; 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; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   PANTHER; PTHR23430; HISTONE H2A; 1.
DR   PANTHER; PTHR23430:SF50; HISTONE H2A; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|RuleBase:RU003767};
KW   DNA-binding {ECO:0000256|RuleBase:RU003767};
KW   Nucleosome core {ECO:0000256|RuleBase:RU003767};
KW   Nucleus {ECO:0000256|RuleBase:RU003767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026042}.
FT   DOMAIN          5..52
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          55..87
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
SQ   SEQUENCE   96 AA;  10249 MW;  F1790724ADF3B691 CRC64;
     MHVTERIGAG APVYLAAVLE YLAAEVLELS GNAARDNKKT RIVPRHIQLA VRNDEELSKL
     LAGVTIAEGG VLPNIQSVLL PQKGKKAVGS SMSQEF
//
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