GenomeNet

Database: UniProt
Entry: A0A1D2M0T2_ORCCI
LinkDB: A0A1D2M0T2_ORCCI
Original site: A0A1D2M0T2_ORCCI 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system