CHZ1_ASPOR
ID CHZ1_ASPOR Reviewed; 110 AA.
AC Q2UBH8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Histone H2A.Z-specific chaperone chz1;
GN Name=chz1; ORFNames=AO090012000994;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007161; BAE61087.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UBH8; -.
DR SMR; Q2UBH8; -.
DR EnsemblFungi; BAE61087; BAE61087; AO090012000994.
DR HOGENOM; CLU_130004_1_1_1; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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..110
FT /note="Histone H2A.Z-specific chaperone chz1"
FT /id="PRO_0000330202"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 110 AA; 11863 MW; 2FC685E4D7262EA5 CRC64;
MDDNNQATTL SNDPAVNAPD TATLGRDKGK ATQDPAPTDT SMDEGESDES ENEDIVKEDE
DGGDDLAPID SSNIISGRRT RGKTIDFVDA AQKLKDDEGE DDEDDEDFEP