ID   CENPA_KLUMA             Reviewed;         192 AA.
AC   Q0MTC0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Histone H3-like centromeric protein CSE4;
DE   AltName: Full=CENP-A homolog;
GN   Name=CSE4;
OS   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ARSCC Y-8281;
RA   Baker R.E., Rogers K.;
RT   "Phylogenetic analysis of fungal cenH3 proteins.";
RL   Submitted (JUL-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; DQ846848; ABH11662.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0MTC0; -.
DR   SMR; Q0MTC0; -.
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..192
FT                   /note="Histone H3-like centromeric protein CSE4"
FT                   /id="PRO_0000270599"
FT   REGION          88..190
FT                   /note="H3-like"
SQ   SEQUENCE   192 AA;  22435 MW;  BD04DC8E6B530D34 CRC64;
     MEQSVRSIDG ARSVAGAGRT IIDRESINQR ALQLLQRNRQ RRLLLKRSED RARYIPERRE
     QKRELDETLE TRNVPQHHIS AHERITKAKS HGSKYKPSDL ALAEIRKYQR STDLLISRMP
     FARLVKEVTD QFASDEEPLR WQSMAIMALQ EASEAYLVGL LEHTNLLALH AKRITIMRKD
     MQLARRIRGQ FI