AFP_ASPGI
ID AFP_ASPGI Reviewed; 94 AA.
AC P17737;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Antifungal protein;
DE Flags: Precursor;
GN Name=afp;
OS Aspergillus giganteus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5060;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MDH 18894;
RX PubMed=8082203; DOI=10.1007/bf00351672;
RA Wnendt S., Ulbrich N., Stahl U.;
RT "Molecular cloning, sequence analysis and expression of the gene encoding
RT an antifungal-protein from Aspergillus giganteus.";
RL Curr. Genet. 25:519-523(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-94.
RC STRAIN=MDH 18894; TISSUE=Mycelium;
RX PubMed=2374718; DOI=10.1093/nar/18.13.3987;
RA Wnendt S., Ulbrich N., Stahl U.;
RT "Cloning and nucleotide sequence of a cDNA encoding the antifungal-protein
RT of Aspergillus giganteus and preliminary characterization of the native
RT gene.";
RL Nucleic Acids Res. 18:3987-3987(1990).
RN [3]
RP PROTEIN SEQUENCE OF 44-94, AND DISULFIDE BONDS.
RC STRAIN=MDH 18894;
RX PubMed=2226447; DOI=10.1111/j.1432-1033.1990.tb19300.x;
RA Nakaya K., Omata K., Okahashi I., Nakamura Y., Kolckenbrock H., Ulbrich N.;
RT "Amino acid sequence and disulfide bridges of an antifungal protein
RT isolated from Aspergillus giganteus.";
RL Eur. J. Biochem. 193:31-38(1990).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=7893713; DOI=10.1021/bi00009a032;
RA Campos-Olivas R., Bruix M., Santoro J., Lacadena J., Martinez del Pozo A.,
RA Gavilanes J.G., Rico M.;
RT "NMR solution structure of the antifungal protein from Aspergillus
RT giganteus: evidence for cysteine pairing isomerism.";
RL Biochemistry 34:3009-3021(1995).
CC -!- FUNCTION: This protein inhibits the growth of a variety of fungal
CC species.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; X60771; CAA43181.1; -; Genomic_DNA.
DR EMBL; X53432; CAA37523.1; -; mRNA.
DR PIR; S44064; S44064.
DR PDB; 1AFP; NMR; -; A=44-94.
DR PDBsum; 1AFP; -.
DR AlphaFoldDB; P17737; -.
DR SMR; P17737; -.
DR EvolutionaryTrace; P17737; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.40.50.60; -; 1.
DR InterPro; IPR023112; Antifungal-protein_dom_sf.
DR InterPro; IPR022706; Antifungal_prot.
DR Pfam; PF11402; Antifungal_prot; 1.
DR SUPFAM; SSF57598; SSF57598; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..43
FT /evidence="ECO:0000255"
FT /id="PRO_0000020639"
FT CHAIN 44..94
FT /note="Antifungal protein"
FT /evidence="ECO:0000269|PubMed:2226447"
FT /id="PRO_0000020640"
FT DISULFID 50..76
FT /evidence="ECO:0000269|PubMed:2226447"
FT DISULFID 57..83
FT /evidence="ECO:0000269|PubMed:2226447"
FT DISULFID 69..71
FT /evidence="ECO:0000269|PubMed:2226447"
FT DISULFID 92..94
FT /evidence="ECO:0000269|PubMed:2226447"
FT CONFLICT 35..41
FT /note="DARDESA -> MQEMRAR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1AFP"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1AFP"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1AFP"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1AFP"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1AFP"
SQ SEQUENCE 94 AA; 9994 MW; 0084E4F9047A8E1F CRC64;
MKFVSLASLG FALVAALGAV ATPVEADSLT AGGLDARDES AVLATYNGKC YKKDNICKYK
AQSGKTAICK CYVKKCPRDG AKCEFDSYKG KCYC
