ID A0A093FLN4_TYTAL Unreviewed; 373 AA.
AC A0A093FLN4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
GN ORFNames=N341_06348 {ECO:0000313|EMBL:KFV55216.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV55216.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV55216.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV55216.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. {ECO:0000256|PIRNR:PIRNR037942}.
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. {ECO:0000256|PIRNR:PIRNR037942}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037942}.
CC Chromosome {ECO:0000256|PIRNR:PIRNR037942}.
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DR EMBL; KK392009; KFV55216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FLN4; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IEA:UniProtKB-UniRule.
DR CDD; cd00074; H2A; 1.
DR CDD; cd02904; Macro_H2A-like; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR InterPro; IPR021171; Core_histone_macro-H2A.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035796; Macro_H2A.
DR PANTHER; PTHR23430:SF37; CORE HISTONE MACRO-H2A.2; 1.
DR PANTHER; PTHR23430; HISTONE H2A; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR Pfam; PF01661; Macro; 1.
DR PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037942}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037942};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW ECO:0000256|PIRNR:PIRNR037942}; Nucleus {ECO:0000256|PIRNR:PIRNR037942};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..371
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 116..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
SQ SEQUENCE 373 AA; 40449 MW; 4DED703517A810BF CRC64;
MSGRSGKKKM SKLSRSSRAG VIFPVGRMMR YLKKGTYKYR IGVGAPVYMA AVIEYLAAEI
LELAGNAARD NKKGRIAPRH ILLAVANDEE LNQLLKGVTI ASGGVLPRIQ PELLAKKRGA
KGKSETILSP TPEKKGRKSM VNKKSGKKAK STKARTPKKN KQKDNEKEGA SNSTSEDGPG
DGFTILSSKS LVPGQKLSLT QSDISHIGSM KVEGIVHPTT AEIDLKEEIG EALLHAEKTD
LDIVTVKELR KSQGPLEVAE AALTQSSGLA AKFVIHCHIP QWGSDKCEEQ LEETIKNCLT
AAEDKKLKSV AFPPFPSGRN CFPKQTAAQV TLRAISTHFD GSSSSSLKNI YFLLFDSESI
GIYVQEMAKL DTK
//
