GenomeNet

Database: UniProt
Entry: A3LXD4_PICST
LinkDB: A3LXD4_PICST
Original site: A3LXD4_PICST 
ID   A3LXD4_PICST            Unreviewed;       103 AA.
AC   A3LXD4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Histone H4 {ECO:0000256|RuleBase:RU000528};
GN   ORFNames=PICST_61679 {ECO:0000313|EMBL:ABN67787.1}, PICST_90470
GN   {ECO:0000313|EMBL:ABN67529.1};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN67787.1, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN67787.1, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258}, and CBS 6054
RC   {ECO:0000313|EMBL:ABN67787.1};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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|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|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}.
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; CP000500; ABN67529.1; -; Genomic_DNA.
DR   EMBL; CP000500; ABN67787.1; -; Genomic_DNA.
DR   RefSeq; XP_001385558.1; XM_001385521.1.
DR   RefSeq; XP_001385816.1; XM_001385779.1.
DR   AlphaFoldDB; A3LXD4; -.
DR   STRING; 322104.A3LXD4; -.
DR   GeneID; 4839780; -.
DR   GeneID; 4839841; -.
DR   KEGG; pic:PICST_61679; -.
DR   KEGG; pic:PICST_90470; -.
DR   eggNOG; KOG3467; Eukaryota.
DR   HOGENOM; CLU_109117_2_3_1; -.
DR   InParanoid; A3LXD4; -.
DR   OMA; QKEHING; -.
DR   OrthoDB; 2782612at2759; -.
DR   Proteomes; UP000002258; Chromosome 6.
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; IPR019809; Histone_H4_CS.
DR   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   PANTHER; PTHR10484; HISTONE H4; 1.
DR   PANTHER; PTHR10484:SF0; HISTONE H4; 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.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU000528};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000528};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU000528};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   DOMAIN          28..93
FT                   /note="TATA box binding protein associated factor (TAF)
FT                   histone-like fold"
FT                   /evidence="ECO:0000259|SMART:SM00803"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   103 AA;  11421 MW;  17D36066FE62D99B CRC64;
     MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISAL IYEEVRVVLK
     SFLENVIRDA VTYTEHAKRK TVTSLDVVYA LKRQGRTLYG FGG
//
DBGET integrated database retrieval system