CHZ1_KLULA
ID CHZ1_KLULA Reviewed; 172 AA.
AC Q6CWY0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Histone H2A.Z-specific chaperone CHZ1;
GN Name=CHZ1; OrderedLocusNames=KLLA0B00649g;
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: Forms a chaperone-bound H2A.Z-H2B complex that acts as a
CC source for SWR1 complex-dependent H2A to H2A.Z histone replacement in
CC chromatin. {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterotrimer with H2A.Z-H2B, stabilizing the
CC association of the histone dimer. Also, with a lower affinity, forms a
CC heterotrimer with H2A-H2B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CHZ1 family. {ECO:0000305}.
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DR EMBL; CR382122; CAH01952.1; -; Genomic_DNA.
DR RefSeq; XP_451559.1; XM_451559.1.
DR AlphaFoldDB; Q6CWY0; -.
DR SMR; Q6CWY0; -.
DR STRING; 28985.XP_451559.1; -.
DR EnsemblFungi; CAH01952; CAH01952; KLLA0_B00649g.
DR GeneID; 2897385; -.
DR KEGG; kla:KLLA0_B00649g; -.
DR eggNOG; ENOG502SCUM; Eukaryota.
DR HOGENOM; CLU_126134_0_0_1; -.
DR InParanoid; Q6CWY0; -.
DR OMA; RRNYDDY; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR InterPro; IPR019098; Histone_chaperone_domain_CHZ.
DR Pfam; PF09649; CHZ; 1.
DR SMART; SM01082; CHZ; 1.
PE 3: Inferred from homology;
KW Chaperone; Nucleus; Reference proteome.
FT CHAIN 1..172
FT /note="Histone H2A.Z-specific chaperone CHZ1"
FT /id="PRO_0000330211"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 19203 MW; 04796EAA60D498C3 CRC64;
MAEEIKDKQE FQIGAEEPDS SNVASQAKRS AESELASTAD ANDKKSKKKR RRRNYDDLDE
KIAQEDKASA TSGANKEEDS ESEVDDEKLD QMMVKEDEEE DDLSEIDSSN IITTGRRTRG
KIIDYKKTAE KLEKNGEVGK DDDDDEDDEE NDEEFKDPAA PAPAPASPTE PK