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Database: UniProt
Entry: A0A0R3Q197_ANGCS
LinkDB: A0A0R3Q197_ANGCS
Original site: A0A0R3Q197_ANGCS 
ID   A0A0R3Q197_ANGCS        Unreviewed;       357 AA.
AC   A0A0R3Q197;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Histone H4 {ECO:0000256|ARBA:ARBA00020836};
GN   ORFNames=ACOC_LOCUS12771 {ECO:0000313|EMBL:VDM64356.1};
OS   Angiostrongylus costaricensis (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0001277001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ACOC_0001277001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM64356.1, ECO:0000313|Proteomes:UP000267027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Costa Rica {ECO:0000313|EMBL:VDM64356.1,
RC   ECO:0000313|Proteomes:UP000267027};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; UYYA01005212; VDM64356.1; -; Genomic_DNA.
DR   STRING; 334426.A0A0R3Q197; -.
DR   WBParaSite; ACOC_0001277001-mRNA-1; ACOC_0001277001-mRNA-1; ACOC_0001277001.
DR   OMA; FPRFDIT; -.
DR   Proteomes; UP000050601; Unplaced.
DR   Proteomes; UP000267027; Unassembled WGS sequence.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   CDD; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 3.
DR   InterPro; IPR035425; CENP-T/H4_C.
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   PANTHER; PTHR11426; HISTONE H3; 1.
DR   PANTHER; PTHR11426:SF274; HISTONE H3.1T; 1.
DR   Pfam; PF15511; CENP-T_C; 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   SUPFAM; SSF47113; Histone-fold; 3.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
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   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267027}.
FT   DOMAIN          41..96
FT                   /note="CENP-T/Histone H4 histone fold"
FT                   /evidence="ECO:0000259|Pfam:PF15511"
FT   DOMAIN          117..232
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          241..332
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   REGION          116..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  39721 MW;  4072ED7954C3A047 CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYCEHAKRK TVTAMDVVYA LKRQGRTLYG FAEERATISF ANNRSNMART
     KQTARKSTGG KAPRKQLATK AARKSAPATG GVKKPHRYRP GTVALREIRR YQKSTELLIR
     KLPFQRLVRE IAQDFKTDLR FQSSAVMALQ EASEAYLVGL FEDTNLCAIH AKPIMPPKPS
     AKGAKKAAKS QKASRAGDKK KKHRRKESYS VYIYRVLKQV HPDTGVSSKA MSIMNSFVND
     VFERIAAEAS RLAHYNKRST ISSREIQTAV RLILPGELAK HAVSEGTKAV TKYTSSK
//
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