H13_DROVI
ID H13_DROVI Reviewed; 250 AA.
AC Q94972;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Histone H1.3;
GN Name=His1.3; Synonyms=h1.3;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bochum;
RX PubMed=11029073; DOI=10.1007/s002390010090;
RA Nagel S., Grossbach U.;
RT "Histone H1 genes and histone gene clusters in the genus Drosophila.";
RL J. Mol. Evol. 51:286-298(2000).
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=9933406; DOI=10.1007/s004120050339;
RA Schienman J.E., Lozovskaya E.R., Strausbaugh L.D.;
RT "Drosophila virilis has atypical kinds and arrangements of histone
RT repeats.";
RL Chromosoma 107:529-539(1998).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; U67936; AAB07734.1; -; Genomic_DNA.
DR AlphaFoldDB; Q94972; -.
DR SMR; Q94972; -.
DR STRING; 7244.FBpp0238116; -.
DR eggNOG; KOG4012; Eukaryota.
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:UniProtKB-KW.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Nucleus.
FT CHAIN 1..250
FT /note="Histone H1.3"
FT /id="PRO_0000195965"
FT DOMAIN 44..118
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 17..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 25834 MW; D53684420BF0D9E9 CRC64;
MSDSAVATSA SPVIVQAASG EKKVSTKKAA ATPKSKKSTA APPSHPPTQQ MVDASIKNLK
ERGGSSLLAI KKYIGATYKC DAQKLAPFIK KYLKNAVANG KLIQTKGKGA SGSFKLSRSA
KKDAKPKASA VEKKTKKVNA SAAAATKRSS STSTTKKAAG AADKKLSKSA AAKKNVEKKK
ADKEKAKDAK KTGTIKAKLT TAKAKSSATK PKTPKPKTTS AKPKKVVSAT TPKKTAVKKP
KAKTASATKK