ID   H1_PEA                  Reviewed;         265 AA.
AC   P08283;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Histone H1;
DE   AltName: Full=PsH1b;
DE   AltName: Full=PsH1b-40;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Marvel;
RX   PubMed=3109912; DOI=10.1111/j.1432-1033.1987.tb13490.x;
RA   Gantt S., Key J.L.;
RT   "Molecular cloning of a pea H1 histone cDNA.";
RL   Eur. J. Biochem. 166:119-125(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-265.
RC   STRAIN=cv. Little Marvel; TISSUE=Root tip;
RX   PubMed=7548832; DOI=10.1007/bf00032675;
RA   Woo H.H., Brigham L.A., Hawes M.C.;
RT   "Molecular cloning and expression of mRNAs encoding H1 histone and an H1
RT   histone-like sequences in root tips of pea (Psium sativum L.).";
RL   Plant Mol. Biol. 28:1143-1147(1995).
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; X05636; CAA29123.1; -; mRNA.
DR   EMBL; L40471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S00033; S00033.
DR   AlphaFoldDB; P08283; -.
DR   SMR; P08283; -.
DR   EnsemblPlants; Psat6g056720.1; Psat6g056720.1.cds; Psat6g056720.
DR   Gramene; Psat6g056720.1; Psat6g056720.1.cds; Psat6g056720.
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:0008168; F:methyltransferase activity; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleus.
FT   CHAIN           1..265
FT                   /note="Histone H1"
FT                   /id="PRO_0000195955"
FT   DOMAIN          61..130
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..167
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  28023 MW;  1D41049DBC224062 CRC64;
     MATEEPIVAV ETVPEPIVTE PTTITEPEVP EKEEPKAEVE KTKKAKGSKP KKASKPRNPA
     SHPTYEEMIK DAIVSLKEKN GSSQYAIAKF IEEKQKQLPA NFKKLLLQNL KKNVASGKLI
     KVKGSFKLSA AAKKPAVAKP KAKTAAKAKS VKAKPAAKPK AKAVVKPKVA SKAKAVAAKP
     KKAAAKPKTV AAKTKPTAAK PKAVVKPKSK VKPAKVAKTS VKTTPGKKVA AVKKVAAKKV
     PVKSVKAKSV KSPVKKVSVK RGGRK