ID A0A0G4LC53_9PEZI Unreviewed; 513 AA.
AC A0A0G4LC53;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Histone H2A.Z {ECO:0000256|ARBA:ARBA00040236};
GN ORFNames=BN1708_012642 {ECO:0000313|EMBL:CRK19484.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK19484.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK19484.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK19484.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Variant histone H2A which can replace H2A in some
CC nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting
CC DNA accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC remodeling. This variant is enriched at promoters, it may keep them in
CC a repressed state until the appropriate activation signal is received.
CC Near telomeres, it may counteract gene silencing caused by the spread
CC of heterochromatin proteins. Required for the RNA polymerase II and
CC SPT15/TBP recruitment to the target genes. Involved in chromosome
CC stability. {ECO:0000256|ARBA:ARBA00037526}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H2A family.
CC {ECO:0000256|ARBA:ARBA00010691}.
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DR EMBL; CVQH01010779; CRK19484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4LC53; -.
DR STRING; 100787.A0A0G4LC53; -.
DR OrthoDB; 235643at2759; -.
DR Proteomes; UP000044602; 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; cd00074; H2A; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR PANTHER; PTHR23430; HISTONE H2A; 1.
DR PANTHER; PTHR23430:SF7; HISTONE H2A.V; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..513
FT /note="Histone H2A.Z"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002566575"
FT REPEAT 125..157
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 158..190
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 378..473
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT DOMAIN 475..507
FT /note="Histone H2A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16211"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 56631 MW; 475D5698704A3C64 CRC64;
MDPIGIAGIL IVFAQVSSRI IVSCYEYQKS VKDAPDEVSR MHDEAAGIRN VAERLVDMVA
HNGHLAIVKL FIATNVDVNA IGGRYSTAVA TAAAQDHVEI MRDTDLLQSL IQKYNSNVNS
PKLFNGSRPI HSAGSRGTVD HVRILLDGGA DVNARNNNGR TPLHWAAERG SWNVVELLLS
RGADAGIRSE EESLQTVLQD RIENPSHRRE SFGASVMEEA ILSLDLGNAI AKWREPGHNN
GWLIQPPRYL WSLPARISKS HGELWPAEPR VRSTFLWALA YLCPHQLVNK PGNFPPSPPL
HHHDHPPIHQ HHHLPTTGFE FDWRKKSVYI NHHQHRRQPF SIDHQLSIFR VKLGPFGNTE
STSNQPRIAS TMAGGKGKSG GKTSGGKAST DGGPKKQQSH SARAGLQFPC GRVKRFLKSN
TQNKMRVGAK AAVYTTAVLE YLTAEVLELA GNAAKDLKVK RITPRHLQLA IRGDEELDTL
IRATIAFGGV LPHINRALLL KVEQKKKAKQ LEA
//
