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Database: UniProt
Entry: A0A444G437_ENSVE
LinkDB: A0A444G437_ENSVE
Original site: A0A444G437_ENSVE 
ID   A0A444G437_ENSVE        Unreviewed;       143 AA.
AC   A0A444G437;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   ORFNames=B296_00017737 {ECO:0000313|EMBL:RRT83415.1}, GW17_00005823
GN   {ECO:0000313|EMBL:RWW29644.1};
OS   Ensete ventricosum (Abyssinian banana) (Musa ensete).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Ensete.
OX   NCBI_TaxID=4639 {ECO:0000313|EMBL:RWW29644.1, ECO:0000313|Proteomes:UP000288739};
RN   [1] {ECO:0000313|EMBL:RRT83415.1, ECO:0000313|Proteomes:UP000287651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.3390/agronomy4010013;
RA   Harrison J., Moore K.A., Paszkiewicz K., Jones T., Grant M., Ambacheew D.,
RA   Muzemil S., Studholme D.J.;
RT   "A Draft Genome Sequence for Ensete ventricosum, the Drought-Tolerant Tree
RT   Against Hunger.";
RL   Agronomy (Basel) 4:13-33(2014).
RN   [2] {ECO:0000313|EMBL:RWW29644.1, ECO:0000313|Proteomes:UP000288739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Bedadit {ECO:0000313|Proteomes:UP000288739};
RC   TISSUE=Leaf {ECO:0000313|EMBL:RWW29644.1};
RX   PubMed=29896517; DOI=10.1016/j.dib.2018.03.026;
RA   Yemataw Z., Muzemil S., Ambachew D., Tripathi L., Tesfaye K., Chala A.,
RA   Farbos A., O'Neill P., Moore K., Grant M., Studholme D.J.;
RT   "Genome sequence data from 17 accessions of Ensete ventricosum, a staple
RT   food crop for millions in Ethiopia.";
RL   Data Brief 18:285-293(2018).
RN   [3] {ECO:0000313|EMBL:RRT83415.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Harrison J., Moore K.A., Paszkiewicz K., Jones T., Grant M., Ambacheew D.,
RA   Muzemil S., Studholme D.;
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC       limiting DNA accessibility to the cellular machineries which require
CC       DNA as a template. Histones thereby play a central role in
CC       transcription regulation, DNA repair, DNA replication and chromosomal
CC       stability. DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code, and
CC       nucleosome remodeling. Required for checkpoint-mediated arrest of cell
CC       cycle progression in response to low doses of ionizing radiation and
CC       for efficient repair of DNA double strand breaks (DSBs) specifically
CC       when modified by C-terminal phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00037463}.
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: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, 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:RWW29644.1}.
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DR   EMBL; AMZH03000498; RRT83415.1; -; Genomic_DNA.
DR   EMBL; JTFG03000363; RWW29644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444G437; -.
DR   Proteomes; UP000287651; Unassembled WGS sequence.
DR   Proteomes; UP000288739; 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   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; HISTONE H2A; 1.
DR   PANTHER; PTHR23430:SF366; HISTONE H2AXA-RELATED; 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.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU003767};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003767};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU003767};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288739}.
FT   DOMAIN          8..97
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          100..133
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   143 AA;  14855 MW;  F923E9E4A3E2137B CRC64;
     MSSAAPAKGG RGKAKSSKSV SRSHKAGLQF PVGRIARFLK AGKYAERVGA GAPVYLAAVL
     EYLAAEVGDP VLELAGNAAR DNKKNRIVPR HIQLAVRNDE ELSKLLGTVT IASGGVLPNI
     HQTLLPSKAG KGKGDIGSAS QEF
//
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