GenomeNet

Database: UniProt
Entry: A0A420Y7Q0_9PEZI
LinkDB: A0A420Y7Q0_9PEZI
Original site: A0A420Y7Q0_9PEZI 
ID   A0A420Y7Q0_9PEZI        Unreviewed;       143 AA.
AC   A0A420Y7Q0;
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   Name=HTZ1 {ECO:0000313|EMBL:RKU43895.1};
GN   ORFNames=DL546_006277 {ECO:0000313|EMBL:RKU43895.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU43895.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU43895.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU43895.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RKU43895.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QVQW01000037; RKU43895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420Y7Q0; -.
DR   STRING; 177199.A0A420Y7Q0; -.
DR   Proteomes; UP000275385; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275385}.
FT   DOMAIN          17..103
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          105..137
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   143 AA;  15279 MW;  2B8D3D348687DDD8 CRC64;
     MAGGKGKSSG GKSSGGKTST AEGPKKQQSH SARAGLQFPC GRVKRFLKQN TQNKMRVGAK
     AAVYVTAVLE YLTAEVLELA GNAAKDLKVK RITPRHLQLA IRGDEELDTL IRATIAFGGV
     LPHINRALLL KVEQKKKSKA AES
//
DBGET integrated database retrieval system