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Database: UniProt
Entry: A0A1S2Y6N5_CICAR
LinkDB: A0A1S2Y6N5_CICAR
Original site: A0A1S2Y6N5_CICAR 
ID   A0A1S2Y6N5_CICAR        Unreviewed;       141 AA.
AC   A0A1S2Y6N5;
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-like {ECO:0000313|RefSeq:XP_004499390.1};
GN   Name=LOC101505124 {ECO:0000313|RefSeq:XP_004499390.1};
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_004499390.1};
RN   [1] {ECO:0000313|RefSeq:XP_004499390.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004499390.1};
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_004499390.1; XM_004499333.1.
DR   AlphaFoldDB; A0A1S2Y6N5; -.
DR   STRING; 3827.A0A1S2Y6N5; -.
DR   PaxDb; 3827-XP_004499390-1; -.
DR   GeneID; 101505124; -.
DR   KEGG; cam:101505124; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   OrthoDB; 973204at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca5.
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:SF386; HISTONE H2B.1-LIKE PROTEIN; 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          13..84
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   141 AA;  16215 MW;  48B772AA13C9005B CRC64;
     MADKKPTIVE KNSATVDADE EKKKKNQEKE KKWSKMIKFK KYIYRVLKQV HPDIAISSKA
     VKIINTIITN IMVKIIHQSS KYINLRRGKS KMLTVREIPA AVMEVFPPQM AQLAISAAHK
     AQTTYKVNQL TDIMDRTMSL K
//
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