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Database: UniProt
Entry: A0A139HYK1_9PEZI
LinkDB: A0A139HYK1_9PEZI
Original site: A0A139HYK1_9PEZI 
ID   A0A139HYK1_9PEZI        Unreviewed;       203 AA.
AC   A0A139HYK1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Transcription factor CBF/NF-Y/archaeal histone domain-containing protein {ECO:0000259|Pfam:PF00808};
GN   ORFNames=AC578_10139 {ECO:0000313|EMBL:KXT07571.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT07571.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT07571.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT07571.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009053}.
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:KXT07571.1}.
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DR   EMBL; LFZN01000001; KXT07571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HYK1; -.
DR   STRING; 321146.A0A139HYK1; -.
DR   OrthoDB; 24067at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IEA:InterPro.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR   InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR   PANTHER; PTHR11064; CCAAT-BINDING TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR11064:SF9; NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   PRINTS; PR00615; CCAATSUBUNTA.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00685; NFYB_HAP3; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          60..125
FT                   /note="Transcription factor CBF/NF-Y/archaeal histone"
FT                   /evidence="ECO:0000259|Pfam:PF00808"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   203 AA;  22290 MW;  DAB67EA25503A7B4 CRC64;
     MSQSPRDQTE AEAADTQSPA ENDQTADQPN SNGNGNDEEN MTALRPEDVG YDFEVKEQDR
     WLPIANVARI MKMALPENAK IAKEAKECMQ ECVSEFISFI TSEASEKCQQ EKRKTVNGED
     ILFAMTSLGF ENYGEALKIY LARYRENLVA RGEHQKPAVA GGSSGNVTSP TYGDSNHNVL
     DNTMDPSAEG TNAFDYGAGG QQY
//
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