ID C1GCR9_PARBD Unreviewed; 177 AA.
AC C1GCR9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=CENP-A homolog {ECO:0000256|ARBA:ARBA00044336};
DE AltName: Full=CENPA homolog {ECO:0000256|ARBA:ARBA00044234};
GN ORFNames=PADG_04791 {ECO:0000313|EMBL:EEH48712.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH48712.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH48712.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH48712.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275961; EEH48712.2; -; Genomic_DNA.
DR RefSeq; XP_010760142.1; XM_010761840.1.
DR AlphaFoldDB; C1GCR9; -.
DR STRING; 502780.C1GCR9; -.
DR GeneID; 22583836; -.
DR KEGG; pbn:PADG_04791; -.
DR VEuPathDB; FungiDB:PADG_04791; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_3_1_1; -.
DR InParanoid; C1GCR9; -.
DR OMA; GQELRWQ; -.
DR OrthoDB; 5482964at2759; -.
DR Proteomes; UP000001628; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 68..170
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 19209 MW; 6EB190566D6AB2AE CRC64;
MSSRGRGGRP VPAGSPQARR TSGGGVGSRS ESAVAGPSSR GGISKVKKTG RDGKGVGDRT
TDIQPGDPLP RRHRYRPGTV ALKEIRRYQK SWDLLLLKLP FARLVREVAV DLLPAGVGEE
LRWQSQAIQA LQEAAEAFLV HLFEDTNLCA IHAKRVTIMQ KDIQLARRIR GAWAGLG
//
