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Database: UniProt
Entry: A0A100ISR2_ASPNG
LinkDB: A0A100ISR2_ASPNG
Original site: A0A100ISR2_ASPNG 
ID   A0A100ISR2_ASPNG        Unreviewed;       138 AA.
AC   A0A100ISR2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   ORFNames=ABL_09276 {ECO:0000313|EMBL:GAQ46615.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ46615.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- FUNCTION: Variant histone H2A which can replace H2A in some
CC       nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting
CC       DNA accessibility to the cellular machineries which require DNA as a
CC       template. Histones thereby play a central role in transcription
CC       regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and nucleosome
CC       remodeling. This variant is enriched at promoters, it may keep them in
CC       a repressed state until the appropriate activation signal is received.
CC       Near telomeres, it may counteract gene silencing caused by the spread
CC       of heterochromatin proteins. Required for the RNA polymerase II and
CC       SPT15/TBP recruitment to the target genes. Involved in chromosome
CC       stability. {ECO:0000256|ARBA:ARBA00037526}.
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. H2A or its variant H2A.Z forms a heterodimer with H2B. H2A.Z
CC       associates with the VPS72/SWC2 subunit of the SWR1 chromatin remodeling
CC       complex. Interacts also with RBP1/DNA-directed RNA polymerase II
CC       largest subunit. {ECO:0000256|ARBA:ARBA00038542}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU003767}.
CC   -!- SIMILARITY: Belongs to the histone H2A family.
CC       {ECO:0000256|ARBA:ARBA00010691, 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:GAQ46615.1}.
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DR   EMBL; BCMY01000022; GAQ46615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100ISR2; -.
DR   PaxDb; 5061-CADANGAP00012412; -.
DR   VEuPathDB; FungiDB:An16g01810; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1091879; -.
DR   VEuPathDB; FungiDB:ATCC64974_72920; -.
DR   VEuPathDB; FungiDB:M747DRAFT_223025; -.
DR   OMA; ARTQNNM; -.
DR   Proteomes; UP000068243; 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:SF7; HISTONE H2A.V; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Chromosome {ECO:0000256|RuleBase:RU003767};
KW   DNA-binding {ECO:0000256|RuleBase:RU003767};
KW   Nucleosome core {ECO:0000256|RuleBase:RU003767};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003767}.
FT   DOMAIN          21..99
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          101..133
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  14823 MW;  52730E6EC06753F0 CRC64;
     MPGGKGKSIG GKAGSKDSAG KSQKSHSAKA GLQFPCGRVK RFLKNNTQNK MRVGAKAAVY
     VTAVLEYLTA EVLELAGNAA KDLKVKRITP RHLQLAIRGD EELDTLIRAT IAFGGVLPRI
     NRALLLKVEQ KKKSKTEA
//
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