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Database: UniProt
Entry: N4W2F7_COLOR
LinkDB: N4W2F7_COLOR
Original site: N4W2F7_COLOR 
ID   N4W2F7_COLOR            Unreviewed;       141 AA.
AC   N4W2F7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   Name=hH2Az {ECO:0000313|EMBL:TDZ24966.1};
GN   ORFNames=Cob_v002115 {ECO:0000313|EMBL:TDZ24966.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ24966.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
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. {ECO:0000256|RuleBase:RU003767}.
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:TDZ24966.1}.
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DR   EMBL; AMCV02000003; TDZ24966.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4W2F7; -.
DR   STRING; 1213857.N4W2F7; -.
DR   EnsemblFungi; ENH87526; ENH87526; Cob_00463.
DR   eggNOG; KOG1757; Eukaryota.
DR   HOGENOM; CLU_062828_2_1_1; -.
DR   OrthoDB; 235643at2759; -.
DR   Proteomes; UP000014480; Unassembled WGS sequence.
DR   GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IEA:EnsemblFungi.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480}.
FT   DOMAIN          15..101
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          103..135
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
SQ   SEQUENCE   141 AA;  15100 MW;  11E793368A6E48B0 CRC64;
     MAGGKGKSGG KTSGGKATAE VPKKQQSHSA RAGLQFPCGR VKRFLKANTQ NKMRVGAKAA
     VYVTAVLEYL TAEVLELAGN AAKDLKVKRI TPRHLQLAIR GDEELDTLIR ATIAFGGVLP
     HINRALLLKV EQKKKAKALE S
//
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