ID W6ULX8_ECHGR Unreviewed; 96 AA.
AC W6ULX8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Histone H2A, embryonic {ECO:0000313|EMBL:EUB54484.1};
GN ORFNames=EGR_10652 {ECO:0000313|EMBL:EUB54484.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB54484.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB54484.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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 -!- 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:EUB54484.1}.
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DR EMBL; APAU02000247; EUB54484.1; -; Genomic_DNA.
DR AlphaFoldDB; W6ULX8; -.
DR STRING; 6210.W6ULX8; -.
DR EnsemblMetazoa; XM_024499901.1; XP_024345680.1; GeneID_36346367.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
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 Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR032454; Histone_H2A_C.
DR PANTHER; PTHR23430; HISTONE H2A; 1.
DR PANTHER; PTHR23430:SF50; HISTONE H2A; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00023269};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023269};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT DOMAIN 68..86
FT /note="Histone H2A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16211"
SQ SEQUENCE 96 AA; 10203 MW; 1DF7A97004A8742B CRC64;
MVGGRGKEGK LRTKAKTRSA RAGLQFLVGR VRHLLRRGNY AERVGGCWST GLLDCCARVP
GCRGAGVELN KLLGGVTIAQ GGVLPKKTEK LVVSKE
//
