ID   MO5_MOROL               Reviewed;          27 AA.
AC   C0HLV4;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Morintide mO5 {ECO:0000305};
DE   AltName: Full=Morintide hevein-like peptide 1 {ECO:0000303|PubMed:32068186};
DE            Short=Mo-HLP1 {ECO:0000303|PubMed:32068186};
DE   Flags: Fragment;
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:32068186};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY,
RP   AND BIOTECHNOLOGY.
RC   TISSUE=Seed {ECO:0000303|PubMed:32068186};
RX   PubMed=32068186; DOI=10.1016/j.jprot.2020.103692;
RA   Sousa A.M.P., Salles H.O., Oliveira H.D., Souza B.B.P., Cardozo Filho J.L.,
RA   Sifuentes D.N., Prates M.V., Bloch Junior C., Bemquerer M.P., Egito A.S.D.;
RT   "Mo-HLPs: New flocculating agents identified from Moringa oleifera seeds
RT   belong to the hevein-like peptide family.";
RL   J. Proteomics 217:103692-103692(2020).
CC   -!- FUNCTION: Chitin-binding protein which functions in defense against
CC       chitin-containing fungal pathogens. {ECO:0000250|UniProtKB:A0A1S6EK91}.
CC   -!- TISSUE SPECIFICITY: Seeds (at protein level).
CC       {ECO:0000269|PubMed:32068186}.
CC   -!- MASS SPECTROMETRY: Mass=4753; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:32068186};
CC   -!- BIOTECHNOLOGY: Has potential use as a flocculating agent in water
CC       treatment processes. {ECO:0000269|PubMed:32068186}.
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DR   AlphaFoldDB; C0HLV4; -.
DR   SMR; C0HLV4; -.
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; IPR036861; Endochitinase-like_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW   Fungicide.
FT   PEPTIDE         1..27
FT                   /note="Morintide mO5"
FT                   /evidence="ECO:0000269|PubMed:32068186"
FT                   /id="PRO_0000452812"
FT   DISULFID        4..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   UNSURE          3
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:32068186"
FT   UNSURE          7
FT                   /note="Q or K"
FT                   /evidence="ECO:0000269|PubMed:32068186"
FT   UNSURE          16
FT                   /note="Q or K"
FT                   /evidence="ECO:0000269|PubMed:32068186"
FT   UNSURE          25
FT                   /note="Q or K"
FT                   /evidence="ECO:0000269|PubMed:32068186"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:32068186"
FT   NON_TER         27
FT                   /evidence="ECO:0000303|PubMed:32068186"
SQ   SEQUENCE   27 AA;  2853 MW;  BFBF31AC54C20BC2 CRC64;
     NGLCCSQYGF CGTTSQYCSR ANGCQSN