ID   HYP1_HYPJE              Reviewed;          97 AA.
AC   P52754;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Hydrophobin-1;
DE   AltName: Full=Hydrophobin I;
DE            Short=HFBI;
DE   Flags: Precursor;
GN   Name=hfb1;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 68-97.
RC   STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX   PubMed=8631337; DOI=10.1111/j.1432-1033.1996.00248.x;
RA   Nakari-Setaelae T., Aro N., Kalkkinen N., Alatalo E., Penttilae M.;
RT   "Genetic and biochemical characterization of the Trichoderma reesei
RT   hydrophobin HFBI.";
RL   Eur. J. Biochem. 235:248-255(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-97, AND DISULFIDE BONDS.
RX   PubMed=16882996; DOI=10.1110/ps.062326706;
RA   Hakanpaa J., Szilvay G.R., Kaljunen H., Maksimainen M., Linder M.,
RA   Rouvinen J.;
RT   "Two crystal structures of Trichoderma reesei hydrophobin HFBI -- the
RT   structure of a protein amphiphile with and without detergent interaction.";
RL   Protein Sci. 15:2129-2140(2006).
CC   -!- FUNCTION: Contributes to surface hydrophobicity, which is important for
CC       processes such as association of hyphae in reproductive structures,
CC       dispersal of aerial spores and adhesion of pathogens to host
CC       structures.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted. Note=Secreted in
CC       aqueous environment.
CC   -!- PTM: Four disulfide bonds may be present.
CC   -!- SIMILARITY: Belongs to the cerato-ulmin hydrophobin family.
CC       {ECO:0000305}.
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DR   EMBL; Z68124; CAA92208.1; -; Genomic_DNA.
DR   PIR; S62621; S62621.
DR   PIR; S62625; S62625.
DR   PDB; 2FZ6; X-ray; 2.10 A; A/B/C/D=23-97.
DR   PDB; 2GVM; X-ray; 2.30 A; A/B/C/D=23-97.
DR   PDBsum; 2FZ6; -.
DR   PDBsum; 2GVM; -.
DR   AlphaFoldDB; P52754; -.
DR   SMR; P52754; -.
DR   VEuPathDB; FungiDB:TrQ_005079; -.
DR   OMA; QFTILAF; -.
DR   EvolutionaryTrace; P52754; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.20.120.10; -; 1.
DR   InterPro; IPR010636; Cerato-ulmin_hydrophobin.
DR   InterPro; IPR036686; Hydrophobin_sf.
DR   PANTHER; PTHR42341; PTHR42341; 1.
DR   Pfam; PF06766; Hydrophobin_2; 1.
DR   SUPFAM; SSF101751; SSF101751; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..22
FT                   /id="PRO_0000013519"
FT   CHAIN           23..97
FT                   /note="Hydrophobin-1"
FT                   /id="PRO_0000013520"
FT   DISULFID        30..79
FT                   /evidence="ECO:0000269|PubMed:16882996"
FT   DISULFID        40..70
FT                   /evidence="ECO:0000269|PubMed:16882996"
FT   DISULFID        41..53
FT                   /evidence="ECO:0000269|PubMed:16882996"
FT   DISULFID        80..91
FT                   /evidence="ECO:0000269|PubMed:16882996"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   STRAND          37..45
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:2FZ6"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:2FZ6"
SQ   SEQUENCE   97 AA;  9874 MW;  F30907B331EC3175 CRC64;
     MKFFAIAALF AAAAVAQPLE DRSNGNGNVC PPGLFSNPQC CATQVLGLIG LDCKVPSQNV
     YDGTDFRNVC AKTGAQPLCC VAPVAGQALL CQTAVGA