ID A8NXR9_COPC7 Unreviewed; 164 AA.
AC A8NXR9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=CENP-A homolog {ECO:0000256|ARBA:ARBA00044336};
DE AltName: Full=CENPA homolog {ECO:0000256|ARBA:ARBA00044234};
GN ORFNames=CC1G_00384 {ECO:0000313|EMBL:EAU84865.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU84865.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU84865.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU84865.2}.
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DR EMBL; AACS02000005; EAU84865.2; -; Genomic_DNA.
DR RefSeq; XP_001837248.2; XM_001837196.2.
DR AlphaFoldDB; A8NXR9; -.
DR STRING; 240176.A8NXR9; -.
DR GeneID; 6013805; -.
DR KEGG; cci:CC1G_00384; -.
DR VEuPathDB; FungiDB:CC1G_00384; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_3_0_1; -.
DR InParanoid; A8NXR9; -.
DR OMA; PNRWQSQ; -.
DR OrthoDB; 5482964at2759; -.
DR Proteomes; UP000001861; 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.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT DOMAIN 31..157
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 164 AA; 18284 MW; E9DB5E3534B445BC CRC64;
MAQTAQKASS SKRRAPTDDS SDPPTPAKRP KSATARKSTG GHKPRRVAEP EPPKPKRRFH
PGTVALREIR KYQKSTDLLL RKLPFSRVVR EIALDMQTNL NGDADVALRW QSSALMALQE
AAEAYLVHLF EDANLCAIHA KRVTIMTRDI QLARRIRGPW GGLA
//