ID   CENPA_KAZSE             Reviewed;         293 AA.
AC   Q0MXD0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Histone H3-like centromeric protein CSE4;
DE   AltName: Full=CENP-A homolog;
GN   Name=CSE4;
OS   Kazachstania servazzii (Yeast) (Saccharomyces servazzii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=27293;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ARSCC Y-12661;
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; DQ826421; ABH11660.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0MXD0; -.
DR   SMR; Q0MXD0; -.
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..293
FT                   /note="Histone H3-like centromeric protein CSE4"
FT                   /id="PRO_0000270602"
FT   REGION          132..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..291
FT                   /note="H3-like"
FT   COMPBIAS        150..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  34129 MW;  D79BF5399961DF5D CRC64;
     MQSQQYSTPN LSLFNDGSAI IGEIRPIHGA NQDVINDRAL QLLQRTREHR NFLHRAHDDI
     RRYEPPTTQI DALENDEDEN FYLNDMNTNE EYQSDRESVK SGLNSIANRY KNAVQSSPSD
     LDDIDFVGEE EQDLSYDESD YSDPLQEIDS NYRESPRRTT DKILKSSSKN YRRRENLGGE
     IRKIRQEKAN KTATRYRPSD LALYEIRKYQ QSTDLLISKI PFARLVKEVT DNFILENQHL
     QWHSMAILAL QEASEAYLVG LLEHANLLAL HAKRITLMKK DVQLARRIRG QFI