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CENPA_KLULA
ID   CENPA_KLULA             Reviewed;         184 AA.
AC   Q6CTI2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Histone H3-like centromeric protein CSE4;
DE   AltName: Full=CENP-A homolog;
DE   AltName: Full=Chromosome segregation protein 4;
GN   Name=CSE4; OrderedLocusNames=KLLA0C12529g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- INTERACTION:
CC       Q6CTI2; Q6CMU6: KLLA0_E17601g; NbExp=4; IntAct=EBI-15928212, EBI-15928236;
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; CR382123; CAH01608.1; -; Genomic_DNA.
DR   RefSeq; XP_452757.1; XM_452757.1.
DR   PDB; 2YFV; X-ray; 2.32 A; A=81-180.
DR   PDB; 2YFW; X-ray; 2.60 A; A/C/E/G=93-184.
DR   PDBsum; 2YFV; -.
DR   PDBsum; 2YFW; -.
DR   AlphaFoldDB; Q6CTI2; -.
DR   SMR; Q6CTI2; -.
DR   DIP; DIP-60345N; -.
DR   IntAct; Q6CTI2; 2.
DR   STRING; 28985.XP_452757.1; -.
DR   EnsemblFungi; CAH01608; CAH01608; KLLA0_C12529g.
DR   GeneID; 2891972; -.
DR   KEGG; kla:KLLA0_C12529g; -.
DR   eggNOG; KOG1745; Eukaryota.
DR   HOGENOM; CLU_078295_3_0_1; -.
DR   InParanoid; Q6CTI2; -.
DR   OMA; KRITIMR; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005729; C:2-micrometer circle DNA; IEA:EnsemblFungi.
DR   GO; GO:0043505; C:CENP-A containing nucleosome; IEA:EnsemblFungi.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019237; F:centromeric DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0030543; P:2-micrometer plasmid partitioning; IEA:EnsemblFungi.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:EnsemblFungi.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:EnsemblFungi.
DR   GO; GO:0061644; P:protein localization to CENP-A containing chromatin; IEA:EnsemblFungi.
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   1: Evidence at protein level;
KW   3D-structure; Centromere; Chromosome; DNA-binding; Kinetochore; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..184
FT                   /note="Histone H3-like centromeric protein CSE4"
FT                   /id="PRO_0000270598"
FT   REGION          54..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..182
FT                   /note="H3-like"
FT   HELIX           94..101
FT                   /evidence="ECO:0007829|PDB:2YFW"
FT   HELIX           110..122
FT                   /evidence="ECO:0007829|PDB:2YFV"
FT   HELIX           135..162
FT                   /evidence="ECO:0007829|PDB:2YFV"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:2YFV"
FT   HELIX           170..178
FT                   /evidence="ECO:0007829|PDB:2YFV"
SQ   SEQUENCE   184 AA;  21410 MW;  D9507DA4E536DCD9 CRC64;
     MEQSIRSIDG SRSLSNVGAS LIDRESINQR ALQLLQRNRR RRLLLNRSED KARYIQPERS
     ASSQQIHPPE HHISAHERIT KARGTRYKPT DLALAEIRKY QRSTDLLISR MPFARLVKEV
     TDQFTTESEP LRWQSMAIMA LQEASEAYLV GLLEHTNLLA LHAKRITIMR KDMQLARRIR
     GQFI
 
 
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