ID   MO1_MOROL               Reviewed;          79 AA.
AC   A0A1S6EK91; A0A1S4NYG2;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Morintide mO1 {ECO:0000303|PubMed:28359256};
DE   AltName: Full=8C-hevein-like protein {ECO:0000312|EMBL:AQR58371.1};
DE   Flags: Precursor;
OS   Moringa oleifera (Horseradish tree) (Moringa pterygosperma).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Moringaceae; Moringa.
OX   NCBI_TaxID=3735 {ECO:0000303|PubMed:28359256};
RN   [1] {ECO:0000312|EMBL:AQR58371.1, ECO:0000312|PDB:5WUZ, ECO:0007744|PDB:5WUZ}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-63, STRUCTURE BY NMR OF
RP   21-63, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BONDS.
RC   TISSUE=Leaf {ECO:0000303|PubMed:28359256};
RX   PubMed=28359256; DOI=10.1186/s12870-017-1014-6;
RA   Kini S.G., Wong K.H., Tan W.L., Xiao T., Tam J.P.;
RT   "Morintides: cargo-free chitin-binding peptides from Moringa oleifera.";
RL   BMC Plant Biol. 17:68-68(2017).
CC   -!- FUNCTION: Chitin-binding protein which functions in defense against
CC       chitin-containing fungal pathogens. Inhibits the growth of budding
CC       hyphae in A. alternata and A. brassiciola.
CC       {ECO:0000269|PubMed:28359256}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. Loses 5% of activity at 100 degrees Celsius after 1
CC         hour incubation. {ECO:0000269|PubMed:28359256};
CC   -!- TISSUE SPECIFICITY: Leaves (at protein level).
CC       {ECO:0000269|PubMed:28359256}.
CC   -!- MASS SPECTROMETRY: Mass=4536.71; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28359256};
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DR   EMBL; KY436355; AQR58371.1; -; mRNA.
DR   PDB; 5WUZ; NMR; -; A=21-63.
DR   PDBsum; 5WUZ; -.
DR   AlphaFoldDB; A0A1S6EK91; -.
DR   SMR; A0A1S6EK91; -.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
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   InterPro; IPR044301; PR4.
DR   PANTHER; PTHR46351; PTHR46351; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
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   3D-structure; Antimicrobial; Chitin-binding; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:28359256"
FT   PEPTIDE         21..63
FT                   /note="Morintide mO1"
FT                   /evidence="ECO:0000269|PubMed:28359256"
FT                   /id="PRO_0000449242"
FT   PROPEP          64..79
FT                   /evidence="ECO:0000269|PubMed:28359256"
FT                   /id="PRO_0000449243"
FT   DOMAIN          21..63
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        23..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:28359256, ECO:0007744|PDB:5WUZ"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:28359256, ECO:0007744|PDB:5WUZ"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:28359256, ECO:0007744|PDB:5WUZ"
FT   DISULFID        57..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:28359256, ECO:0007744|PDB:5WUZ"
FT   TURN            25..28
FT                   /evidence="ECO:0007829|PDB:5WUZ"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:5WUZ"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:5WUZ"
FT   TURN            48..50
FT                   /evidence="ECO:0007829|PDB:5WUZ"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:5WUZ"
SQ   SEQUENCE   79 AA;  7779 MW;  7E27961B92DFA4A0 CRC64;
     MAKLSFLSLF LLCLVATATA QNCGRQAGNR ACANQLCCSQ YGFCGSTSEY CSRANGCQSN
     CRGGGGADGA GGEAGGGGP