ID A0A1S2XDP8_CICAR Unreviewed; 218 AA.
AC A0A1S2XDP8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histone H2B, gonadal {ECO:0000313|RefSeq:XP_004487735.1};
GN Name=LOC101499426 {ECO:0000313|RefSeq:XP_004487735.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004487735.1};
RN [1] {ECO:0000313|RefSeq:XP_004487735.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004487735.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00002001}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H2B family.
CC {ECO:0000256|ARBA:ARBA00006846}.
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DR RefSeq; XP_004487735.1; XM_004487678.3.
DR AlphaFoldDB; A0A1S2XDP8; -.
DR STRING; 3827.A0A1S2XDP8; -.
DR PaxDb; 3827-XP_004487735-1; -.
DR GeneID; 101499426; -.
DR KEGG; cam:101499426; -.
DR eggNOG; KOG1744; Eukaryota.
DR OrthoDB; 471986at2759; -.
DR Proteomes; UP000087171; Chromosome Ca1.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; HISTONE H2B; 1.
DR PANTHER; PTHR23428:SF238; HISTONE H2B.2; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000087171}.
FT DOMAIN 79..191
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 56..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 24539 MW; 50D5DEFE9F89F7D4 CRC64;
MAPKRAKVVV RSTRKVVEES VQVSVVSSEK RLTRGSKDVQ IDRHVGSTLK QEHVKNIPVQ
EVTPQPKEDT IASTNTVTTE DKTKQENTPN EATMEPKEQE KKVKYKEGND SSKEIRKKKR
GRRKREGYQR YVYRVLKQVH PDMGISSQAM TILNNLMNDM FERLADEAAK LNTYTGHMTL
SSREIQGAVK LVLPGELGKH AIAEGAKAVT NYISSYAA
//
