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Database: UniProt
Entry: A0A3B4XLQ0_SERLL
LinkDB: A0A3B4XLQ0_SERLL
Original site: A0A3B4XLQ0_SERLL 
ID   A0A3B4XLQ0_SERLL        Unreviewed;        95 AA.
AC   A0A3B4XLQ0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Histone H4 {ECO:0000256|RuleBase:RU000528};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000017142.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000017142.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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, ECO:0000256|RuleBase:RU000528}.
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|ARBA:ARBA00011538, ECO:0000256|RuleBase:RU000528}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the histone H4 family.
CC       {ECO:0000256|ARBA:ARBA00006564, ECO:0000256|RuleBase:RU000528}.
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DR   STRING; 1841481.ENSSLDP00000003493; -.
DR   Ensembl; ENSSLDT00000003614.1; ENSSLDP00000003493.1; ENSSLDG00000002715.1.
DR   Ensembl; ENSSLDT00000017747.1; ENSSLDP00000017142.1; ENSSLDG00000013551.1.
DR   GeneTree; ENSGT00990000203553; -.
DR   Proteomes; UP000261360; Unplaced.
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; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR035425; CENP-T/H4_C.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   PANTHER; PTHR10484; HISTONE H4; 1.
DR   PANTHER; PTHR10484:SF189; HISTONE H4 TYPE VIII; 1.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU000528};
KW   Citrullination {ECO:0000256|ARBA:ARBA00022934};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000528};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU000528};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000528}.
FT   DOMAIN          20..85
FT                   /note="TATA box binding protein associated factor (TAF)
FT                   histone-like fold"
FT                   /evidence="ECO:0000259|SMART:SM00803"
SQ   SEQUENCE   95 AA;  10670 MW;  89E8DE17A179586F CRC64;
     LAGTGKCAKR HRKVLRDNIQ GITKPAIRRL ARRGGVKRIS GLIYEETRGV LKVFLENVIR
     DAVTYTEHAK RKTVTAMDVV YALKRQGRTL YGFGG
//
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