ID A0A4Q1BPW0_TREME Unreviewed; 196 AA.
AC A0A4Q1BPW0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN ORFNames=M231_02759 {ECO:0000313|EMBL:RXK39964.1};
OS Tremella mesenterica (Jelly fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Tremellaceae; Tremella.
OX NCBI_TaxID=5217 {ECO:0000313|EMBL:RXK39964.1, ECO:0000313|Proteomes:UP000289152};
RN [1] {ECO:0000313|EMBL:RXK39964.1, ECO:0000313|Proteomes:UP000289152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28783 {ECO:0000313|EMBL:RXK39964.1,
RC ECO:0000313|Proteomes:UP000289152};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:RXK39964.1}.
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DR EMBL; SDIL01000024; RXK39964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q1BPW0; -.
DR STRING; 5217.A0A4Q1BPW0; -.
DR VEuPathDB; FungiDB:TREMEDRAFT_19608; -.
DR InParanoid; A0A4Q1BPW0; -.
DR Proteomes; UP000289152; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chromosome {ECO:0000256|RuleBase:RU003767};
KW DNA-binding {ECO:0000256|RuleBase:RU003767};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleosome core {ECO:0000256|RuleBase:RU003767};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003767};
KW Reference proteome {ECO:0000313|Proteomes:UP000289152}.
FT DOMAIN 18..90
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT DOMAIN 93..123
FT /note="Histone H2A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16211"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 196 AA; 21207 MW; 9F4F69CC4E309BE1 CRC64;
MPITPSSGIK NNRMKGKNKS AKAGVTFPVN RVIRHLKNGH YSNRVGVGAG VYLAAVLEYL
TAEVLELAGN AASDNKKSRI QPRHLLLAIK NDEEIDQLLK DVTISQGGVM PAINQFLLPG
GNKRGATQGS VSTGVSVSSK SKMSTSSKRR EVKPVNESYS LEGESIFPFC FVRGVRMDHR
EIYPSVQSVG GSTETY
//
