H2A_PHANO
ID H2A_PHANO Reviewed; 134 AA.
AC Q0U1A1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Histone H2A;
GN Name=HTA1; ORFNames=SNOG_14611;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Core component of nucleosome which plays a central role in
CC DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC code, and nucleosome remodeling.
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.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family.
CC -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA
CC double-strand breaks (DSBs) generated by exogenous genotoxic agents and
CC by stalled replication forks. Phosphorylation is dependent on the DNA
CC damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side
CC of a detected DSB site and may mark the surrounding chromatin for
CC recruitment of proteins required for DNA damage signaling and repair.
CC Gamma-H2A is removed from the DNA prior to the strand invasion-primer
CC extension step of the repair process and subsequently dephosphorylated.
CC Dephosphorylation is necessary for efficient recovery from the DNA
CC damage checkpoint (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by ESA1 to form H2AK4ac and H2AK7ac. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-terminus
CC is not monoubiquitinated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H2AK4ac =
CC acetylated Lys-5; H2AK7ac = acetylated Lys-9; H2AS128ph =
CC phosphorylated Ser-131. {ECO:0000305}.
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DR EMBL; CH445356; EAT78151.1; -; Genomic_DNA.
DR RefSeq; XP_001804793.1; XM_001804741.1.
DR AlphaFoldDB; Q0U1A1; -.
DR SMR; Q0U1A1; -.
DR STRING; 13684.SNOT_14611; -.
DR EnsemblFungi; SNOT_14611; SNOT_14611; SNOG_14611.
DR GeneID; 5981718; -.
DR KEGG; pno:SNOG_14611; -.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_0_1; -.
DR InParanoid; Q0U1A1; -.
DR OMA; VMPYIHP; -.
DR OrthoDB; 1504122at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IEA:EnsemblFungi.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 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; PTHR23430; 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; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 3: Inferred from homology;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..134
FT /note="Histone H2A"
FT /id="PRO_0000297737"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..132
FT /note="[ST]-Q motif"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 121
FT /note="Not ubiquitinated"
FT /evidence="ECO:0000305"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 107
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 134 AA; 14136 MW; 35B522A89B04EDFA CRC64;
MTGGKSGGKA SGSKSSAQSR SSKAGLAFPV GRVHRLLRKG NYAQRVGAGA PVYLAAVLEY
LAAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL GHVTIAQGGV LPNIHQNLLP
KKTAKPGKGP SQEL
