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Database: UniProt
Entry: S3CVD1_GLAL2
LinkDB: S3CVD1_GLAL2
Original site: S3CVD1_GLAL2 
ID   S3CVD1_GLAL2            Unreviewed;       246 AA.
AC   S3CVD1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Histone-fold containing protein {ECO:0000313|EMBL:EPE29620.1};
GN   ORFNames=GLAREA_00780 {ECO:0000313|EMBL:EPE29620.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE29620.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE29620.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009053}.
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DR   EMBL; KE145367; EPE29620.1; -; Genomic_DNA.
DR   RefSeq; XP_008083729.1; XM_008085538.1.
DR   AlphaFoldDB; S3CVD1; -.
DR   STRING; 1116229.S3CVD1; -.
DR   GeneID; 19459838; -.
DR   KEGG; glz:GLAREA_00780; -.
DR   eggNOG; KOG0869; Eukaryota.
DR   HOGENOM; CLU_066247_10_2_1; -.
DR   OMA; ADPNYMY; -.
DR   OrthoDB; 24067at2759; -.
DR   Proteomes; UP000016922; 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:UP000016922};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          90..150
FT                   /note="Transcription factor CBF/NF-Y/archaeal histone"
FT                   /evidence="ECO:0000259|Pfam:PF00808"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  25866 MW;  FA6AC202CAAB5A25 CRC64;
     MSAASASPPK EDAVASPEND AMNDPTDPHA AGLGYEFEVK EQDRWLPIAN AMSHKSPSPS
     PSSSSSPETN RTSKGGKSDG YPDANIRNFA PVARIMKTAL PDNAKIAKEA KECMQECVSE
     FISFITSEAS EKCHQEKRKT VNGEDILFAM TSLGFENYAE ALKIYLSKYR ETQSTRGEQR
     PSSQAGYGAT GASAPNAASS AFAGGADTNN NILGGQQAEG GDHDPPYGSL YGAQSGHNGA
     TGGDGY
//
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