H2A2_MEDTR
ID H2A2_MEDTR Reviewed; 153 AA.
AC Q2HU65;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable histone H2A.2;
GN ORFNames=MtrDRAFT_AC149210g4v1;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The international Medicago genome annotation group;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone 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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: Contains one SPKK motif which may interact with the minor
CC groove of A/T-rich DNA sites. Phosphorylation of this motif may
CC regulate DNA binding. This motif is reiterated in both termini of
CC histone H1 and in the N-terminus of sea urchin histones H2B, but its
CC presence in the C-terminus seems to be unique to plant H2A.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; AC149210; ABD32280.1; -; Genomic_DNA.
DR RefSeq; XP_003597343.1; XM_003597295.2.
DR AlphaFoldDB; Q2HU65; -.
DR SMR; Q2HU65; -.
DR STRING; 3880.AES67594; -.
DR PRIDE; Q2HU65; -.
DR EnsemblPlants; AES67594; AES67594; MTR_2g096570.
DR GeneID; 11417382; -.
DR Gramene; AES67594; AES67594; MTR_2g096570.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_1_1_1; -.
DR OMA; HAYLYSA; -.
DR OrthoDB; 1504122at2759; -.
DR ExpressionAtlas; Q2HU65; differential.
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; -; 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 Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT CHAIN 1..153
FT /note="Probable histone H2A.2"
FT /id="PRO_0000239993"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..152
FT /note="SPKK motif"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 153 AA; 16308 MW; 6BAA7B488CA7E619 CRC64;
MDASTKTKKG AGGRKGGGPR KKSVTRSIRA GLQFPVGRIG RYLKKGRYAQ RVGTGAPVYL
AAVLEYLAAE VLELAGNAAR DNKKNRIIPR HVLLAVRNDE ELGKLLAGVT IAHGGVLPNI
NPVLLPKKTE RSNTVSKEPK SPKPKAGKSP KKA