ID   CENPA_MILFA             Reviewed;         158 AA.
AC   Q0MXD1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Histone H3-like centromeric protein CSE4;
DE   AltName: Full=CENP-A homolog;
GN   Name=CSE4;
OS   Millerozyma farinosa (Yeast) (Pichia farinosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=4920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 185 / DSM 3316 / JCM 10734 / NBRC 1163 / NRRL Y-7553;
RA   Baker R.E., Rogers K.;
RT   "Phylogenetic analysis of fungal cenH3 proteins.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone H3-like variant which exclusively replaces
CC       conventional H3 in the nucleosome core of centromeric chromatin at the
CC       inner plate of the kinetochore. Required for recruitment and assembly
CC       of kinetochore proteins, mitotic progression and chromosome
CC       segregation. May serve as an epigenetic mark that propagates centromere
CC       identity through replication and cell division (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the core kinetochore. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC       {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC       Note=Localizes exclusively in the kinetochore domain of centromeres.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Is degraded through ubiquitin mediated proteolysis
CC       when not protected by its association to the kinetochore. This may
CC       ensure exclusive localization of CSE4 to the kinetochore (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; DQ826420; ABH11659.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0MXD1; -.
DR   SMR; Q0MXD1; -.
DR   PRIDE; Q0MXD1; -.
DR   OMA; AENFIGM; -.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   3: Inferred from homology;
KW   Centromere; Chromosome; DNA-binding; Kinetochore; Nucleus; Ubl conjugation.
FT   CHAIN           1..158
FT                   /note="Histone H3-like centromeric protein CSE4"
FT                   /id="PRO_0000270601"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..157
FT                   /note="H3-like"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   158 AA;  17938 MW;  BBB7A331E3BB3E4E CRC64;
     MARISTSSNR PVPTSSALRR QRERDDGGRS TRAPGHNTGL YGNQPGDPPT IRSTNTTVKR
     RYRPGTKALR EIRRYQRSSE LLIRKLPFAR LVKEVAENYI GADYGIRWQS NAVLALQEAC
     EAFLVHLLED TNLCAIHAKR VTIMQKDIQL ARRIRGNI