ID   EAP1_EUCUL              Reviewed;          41 AA.
AC   P83596;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Antifungal peptide 1;
DE   AltName: Full=EAFP1;
OS   Eucommia ulmoides (Hardy rubber tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Garryales; Eucommiaceae; Eucommia.
OX   NCBI_TaxID=4392;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, DISULFIDE BONDS,
RP   AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Bark;
RX   PubMed=12067732; DOI=10.1016/s0014-5793(02)02829-6;
RA   Huang R.-H., Xiang Y., Liu X.-Z., Zhang Y., Hu Z., Wang D.-C.;
RT   "Two novel antifungal peptides distinct with a five-disulfide motif from
RT   the bark of Eucommia ulmoides Oliv.";
RL   FEBS Lett. 521:87-90(2002).
CC   -!- FUNCTION: Has antifungal activity against P.infestans, A.lycopersici,
CC       V.dahliae, G.zeae, A.nicotianae, F.moniliforme, F.oxysporum and
CC       C.gossypii. {ECO:0000269|PubMed:12067732}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12067732}.
CC   -!- MASS SPECTROMETRY: Mass=4201.43; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12067732};
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DR   AlphaFoldDB; P83596; -.
DR   BMRB; P83596; -.
DR   SMR; P83596; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense; Pyrrolidone carboxylic acid.
FT   CHAIN           1..41
FT                   /note="Antifungal peptide 1"
FT                   /id="PRO_0000124816"
FT   DOMAIN          4..41
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:12067732"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        7..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        11..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        16..30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   41 AA;  4229 MW;  8F775334FAABAAB4 CRC64;
     QTCASRCPRP CNAGLCCSIY GYCGSGNAYC GAGNCRCQCR G