ID M7X4Z3_RHOT1 Unreviewed; 165 AA.
AC M7X4Z3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=CENP-A homolog {ECO:0000256|ARBA:ARBA00044336};
DE AltName: Full=CENPA homolog {ECO:0000256|ARBA:ARBA00044234};
GN ORFNames=RHTO_05654 {ECO:0000313|EMBL:EMS18724.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18724.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18724.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18724.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- FUNCTION: Histone H3-like nucleosomal protein that is specifically
CC found in centromeric nucleosomes. Replaces conventional H3 in the
CC nucleosome core of centromeric chromatin that serves as an assembly
CC site for the inner 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.
CC {ECO:0000256|ARBA:ARBA00043846}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000256|ARBA:ARBA00004584}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC {ECO:0000256|ARBA:ARBA00010343}.
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DR EMBL; KB722676; EMS18724.1; -; Genomic_DNA.
DR RefSeq; XP_016269843.1; XM_016419315.1.
DR AlphaFoldDB; M7X4Z3; -.
DR GeneID; 27369667; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_3_3_1; -.
DR OrthoDB; 5482964at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
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:InterPro.
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; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR45810:SF10; HISTONE H3; 1.
DR PANTHER; PTHR45810; HISTONE H3.2; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 41..161
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 18489 MW; 849E43AD678A83E0 CRC64;
MAQTPRKQPA KKTVVAKKAV VQKKVAGKTL GGGAGKGPRK STGGKTRHGQ PAAQPVQRKP
RRFRPGTRAL QEIRHYQKGT DLLLRRLPFA RLVREIAMEF LADDEEGNAP GLRWQSSALL
ALQEATEAYL IHLFEDSNLC ALHAKRVTIM QRDMQLVRRI RGDFM
//
