ID A0A1D2M0T2_ORCCI Unreviewed; 412 AA.
AC A0A1D2M0T2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Histone H4 {ECO:0000256|ARBA:ARBA00020836};
DE Flags: Fragment;
GN ORFNames=Ocin01_20119 {ECO:0000313|EMBL:ODM86564.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM86564.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM86564.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM86564.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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 -!- 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}.
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}.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC {ECO:0000256|ARBA:ARBA00010343}.
CC -!- SIMILARITY: Belongs to the histone H4 family.
CC {ECO:0000256|ARBA:ARBA00006564}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM86564.1}.
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DR EMBL; LJIJ01008247; ODM86564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2M0T2; -.
DR STRING; 48709.A0A1D2M0T2; -.
DR OrthoDB; 3370181at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
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; 3.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR019809; Histone_H4_CS.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR PANTHER; PTHR11426; HISTONE H3; 1.
DR PANTHER; PTHR11426:SF265; HISTONE H3.2; 1.
DR Pfam; PF00125; Histone; 2.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00427; H2B; 1.
DR SMART; SM00428; H3; 1.
DR SMART; SM00417; H4; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; Histone-fold; 3.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527}.
FT DOMAIN 339..404
FT /note="TATA box binding protein associated factor (TAF)
FT histone-like fold"
FT /evidence="ECO:0000259|SMART:SM00803"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 412
FT /evidence="ECO:0000313|EMBL:ODM86564.1"
SQ SEQUENCE 412 AA; 46689 MW; D2AFB1AC2E2DA06B CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIHWPDV SVENLAESLF NIPSEITAWT ATTAPHSQAL VQTESLLSPS KPNSFSTCHQ
RPVERLPRRQ EKPKRTFPKG DGKKRKHKRK ESYAIYIYKV LKQVHPDTGV SSKAMSIMNS
FVNDIFERIA AEASRLATTT RGPPSPLGKS KLQCVSFFPE SWPNTPSLKE PRLSPSTPPP
RPPNFSKSIN KTCIYYCEER VLERGGAKRH RKVLRDNIQG ITKPAIRRLA RRGGVKRISG
LIYEETRGVL KVFLENVIRD AVTYTEHAKR KTVTAMDVVY ALKRQQNSLR IR
//