ID   F0UFF0_AJEC8            Unreviewed;       374 AA.
AC   F0UFF0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGC44110.1};
GN   ORFNames=HCEG_03325 {ECO:0000313|EMBL:EGC44110.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CENP-X/MHF2 family.
CC       {ECO:0000256|ARBA:ARBA00009359}.
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DR   EMBL; DS990638; EGC44110.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UFF0; -.
DR   VEuPathDB; FungiDB:I7I53_02600; -.
DR   HOGENOM; CLU_789802_0_0_1; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR018552; CENP-X.
DR   InterPro; IPR009072; Histone-fold.
DR   PANTHER; PTHR28680; CENTROMERE PROTEIN X; 1.
DR   PANTHER; PTHR28680:SF1; CENTROMERE PROTEIN X; 1.
DR   Pfam; PF09415; CENP-X; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  40896 MW;  9D6B3CD13EDF5D1B CRC64;
     MDPPISLPKR KRPPFNPPRP RNGAGITKPS TTSTRSKSKP KPKPNSTART TTQKSASSSS
     TIHRRSPSTA HNNDNDDDTR ASSTSSRTPS PSGPNSSPRV TPSSDYESPG SRSRSPSDEP
     DYILAEITEP APLDPREELE SSDPLIKPKL LTTLLHRHFQ NDKTKITKDA VRALAKYVDI
     FVREALARAS YERAEGQSGK SASRDTRGGA RARVDNYLEI EDLERLAPHE GRGKNEIDPL
     HTIQFVNISK KPSLTQRRLN YNELRQGCPR FDVGLEGGVS PATAGTPSVD NLKQPCDTFK
     AFHASHQHPH SCMEQRSPLV SQAAGYLYLS STGATGSNGC DSNLHLTPGL ETRKATRFIP
     PAYPVLGTSP FLFE
//