ID   THYD_CLAFS              Reviewed;         394 AA.
AC   Q9UVI4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Trihydrophobin;
DE   AltName: Full=CFTH1;
DE   Flags: Precursor;
GN   Name=TH1;
OS   Claviceps fusiformis (Ergot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=40602 {ECO:0000312|EMBL:CAB61236.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 26245 / DSM 2942 / CBS 164.59;
RX   PubMed=10336622; DOI=10.1046/j.1432-1327.1999.00387.x;
RA   de Vries O.M.H., Moore S., Arntz C., Wessels J.G.H., Tudzynski P.;
RT   "Identification and characterization of a tri-partite hydrophobin from
RT   Claviceps fusiformis: a novel type of class II hydrophobin.";
RL   Eur. J. Biochem. 262:377-385(1999).
RN   [2] {ECO:0000305}
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 26245 / DSM 2942 / CBS 164.59;
RX   PubMed=9108144; DOI=10.1007/s002940050216;
RA   Arntz C., Tudzynski P.;
RT   "Identification of genes induced in alkaloid-producing cultures of
RT   Claviceps sp.";
RL   Curr. Genet. 31:357-360(1997).
CC   -!- FUNCTION: Self-assembles at hydrophilic-hydrophobic interfaces on
CC       hyphal surface. Reduces water surface tension dramatically upon
CC       assembly at the water-air interface. Probable role in growth of aerial
CC       hyphae. {ECO:0000269|PubMed:10336622, ECO:0000303|PubMed:10336622}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:10336622}.
CC   -!- PTM: Several N-termini starting at positions 17, 20, 22, 28 and 48 have
CC       been identified by direct sequencing. {ECO:0000269|PubMed:10336622}.
CC   -!- PTM: Contains a number of intrachain disulfide bonds.
CC       {ECO:0000269|PubMed:10336622}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:10336622}.
CC   -!- SIMILARITY: Belongs to the cerato-ulmin hydrophobin family.
CC       {ECO:0000305}.
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DR   EMBL; AJ133774; CAB61236.1; -; mRNA.
DR   AlphaFoldDB; Q9UVI4; -.
DR   SMR; Q9UVI4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030446; C:hyphal cell wall; IDA:UniProtKB.
DR   GO; GO:0045230; P:capsule organization; IDA:UniProtKB.
DR   GO; GO:0030448; P:hyphal growth; NAS:UniProtKB.
DR   Gene3D; 3.20.120.10; -; 3.
DR   InterPro; IPR010636; Cerato-ulmin_hydrophobin.
DR   InterPro; IPR036686; Hydrophobin_sf.
DR   PANTHER; PTHR42341; PTHR42341; 3.
DR   Pfam; PF06766; Hydrophobin_2; 3.
DR   SUPFAM; SSF101751; SSF101751; 3.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Disulfide bond; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:10336622"
FT   CHAIN           17..394
FT                   /note="Trihydrophobin"
FT                   /id="PRO_0000013516"
FT   REGION          17..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..117
FT                   /note="Hydrophobin 1"
FT   REGION          135..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..270
FT                   /note="Hydrophobin 2"
FT   REGION          326..394
FT                   /note="Hydrophobin 3"
SQ   SEQUENCE   394 AA;  36814 MW;  416900B37C49B3B8 CRC64;
     MKFLAAASLL VASTLAVPTS SGGSCRPRPP PGGGNGGNGG NGGNGGNGYQ PCPAGLYSNP
     QCCATDVLGV ADLDCKNPSS APMSGDNFKS ICNAVGQQAK CCVLPVAGQA VLCQDSINGG
     GNGGNNGGNG GNNGGNGGNN GGNTDYPGGN GGNNGGNNGG NNGGNNGGNN GGNNGGNNGG
     NNGGNNGGNN GGNGGNGGNG YQACPAGLLY SNPQCCSTGV LGVADLDCKN PSSAPTSGDD
     FQKICANGGQ QAQCCSIPVA GQAVLCQPAI GGGNPGGNGG NNGGNGGNGG NNGGNNGGNG
     DYPGGNGGNN GGSNGGGNGG NGGNGGSFKC PSGLYSVPQC CATDVLGVAD LDCGNPSRQP
     TDSSDFASVC AAKGQRARCC VLPLLGQAVL CTGA