ID   AMP_AMARE               Reviewed;          89 AA.
AC   Q5I2B2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Antimicrobial peptide Ar-AMP;
DE   Flags: Precursor;
OS   Amaranthus retroflexus (Redroot amaranth) (American pigweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=124763;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAW56634.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-55, FUNCTION, DISULFIDE
RP   BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:16126239};
RX   PubMed=16126239; DOI=10.1016/j.phytochem.2005.07.015;
RA   Lipkin A., Anisimova V., Nikonorova A., Babakov A., Krause E., Bienert M.,
RA   Grishin E., Egorov T.;
RT   "An antimicrobial peptide Ar-AMP from amaranth (Amaranthus retroflexus L.)
RT   seeds.";
RL   Phytochemistry 66:2426-2431(2005).
CC   -!- FUNCTION: Chitin-binding protein that inhibits the growth of the fungal
CC       pathogens B.cinerea, F.culmorum, H.sativum and A.consortiale, but not
CC       that of R.solani. Induces morphological changes in the fungal pathogens
CC       F.culmorum, H.sativum and R.solani, but not in A.consortiale and
CC       B.cinerea. Has antibacterial activity against the Gram-positive
CC       bacterium B.subtilis, but lacks antibacterial activity against the
CC       Gram-negative bacterium E.coli. {ECO:0000269|PubMed:16126239}.
CC   -!- MASS SPECTROMETRY: Mass=3153.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16126239};
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DR   EMBL; AY861660; AAW56634.1; -; mRNA.
DR   AlphaFoldDB; Q5I2B2; -.
DR   SMR; Q5I2B2; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR013006; Antimicrobial_C6_CS.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
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.
DR   PROSITE; PS60011; PLANT_C6_AMP; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Chitin-binding; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Plant defense; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:16126239"
FT   PEPTIDE         26..55
FT                   /note="Antimicrobial peptide Ar-AMP"
FT                   /id="PRO_0000257981"
FT   PROPEP          56..89
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:16126239"
FT                   /id="PRO_0000257982"
FT   DOMAIN          26..68
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        29..40
FT                   /evidence="ECO:0000250|UniProtKB:P27275,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        34..46
FT                   /evidence="ECO:0000250|UniProtKB:P27275,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000250|UniProtKB:P27275,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   89 AA;  9039 MW;  B74BF22FE38E0488 CRC64;
     MVNMKSVALI VIVMMAFMMV DPSMGAGECV QGRCPSGMCC SQFGYCGRGP KYCGRASTTV
     DHQADAAAAA ATKTANNPTD AKLAGAGSP