ID A0A229YYE4_9EURO Unreviewed; 214 AA.
AC A0A229YYE4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Transcription factor CBF/NF-Y/archaeal histone domain-containing protein {ECO:0000259|Pfam:PF00808};
GN ORFNames=CDV55_104327 {ECO:0000313|EMBL:RHZ63386.1}, CFD26_106330
GN {ECO:0000313|EMBL:RLL97178.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ63386.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL97178.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ63386.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RHZ63386.1}.
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DR EMBL; NKHV02000081; RHZ63386.1; -; Genomic_DNA.
DR EMBL; NIDN02000086; RLL97178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229YYE4; -.
DR STRING; 1245748.A0A229YYE4; -.
DR OrthoDB; 24067at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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:UP000215289};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 44..109
FT /note="Transcription factor CBF/NF-Y/archaeal histone"
FT /evidence="ECO:0000259|Pfam:PF00808"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 214 AA; 23193 MW; 11ACD9A918077CB1 CRC64;
MSASPSKEPE VEPEAQSGED QEHMDKDQEQ TQNQGEFEVK EQDRWLPIAN VARIMKLALP
ENAKIAKEAK ECMQECVSEF ISFITSEASE KCQQEKRKTV NGEDILFAMT SLGFENYAEA
LKIYLSKYRE TQSARGEHQN RPTSSGYNAG GPVGGSSNQG GRPGASASGG FPETADNTNN
IMNPGLDPTE QDSSAYGYPP MVGQGHNGAG GDSY
//
