GNKL1_PICSI
ID GNKL1_PICSI Reviewed; 133 AA.
AC A9NQT1;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Antifungal protein ginkbilobin-like protein 1 {ECO:0000305};
DE Flags: Precursor;
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bark {ECO:0000312|EMBL:ABK22992.1};
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
RN [2]
RP IDENTIFICATION.
RX PubMed=26315821; DOI=10.1007/s00709-015-0876-4;
RA Gao N., Wadhwani P., Muehlhaeuser P., Liu Q., Riemann M., Ulrich A.S.,
RA Nick P.;
RT "An antifungal protein from Ginkgo biloba binds actin and can trigger cell
RT death.";
RL Protoplasma 253:1159-1174(2016).
CC -!- FUNCTION: Exerts antifungal activity through its carbohydrate-binding
CC specificity. {ECO:0000250|UniProtKB:A4ZDL6}.
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DR EMBL; EF083656; ABK22992.1; -; mRNA.
DR AlphaFoldDB; A9NQT1; -.
DR SMR; A9NQT1; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.430.20; -; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR Pfam; PF01657; Stress-antifung; 1.
DR PROSITE; PS51473; GNK2; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Disulfide bond; Fungicide; Lectin;
KW Mannose-binding; Plant defense; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..133
FT /note="Antifungal protein ginkbilobin-like protein 1"
FT /id="PRO_5002741214"
FT DOMAIN 28..133
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT BINDING 36
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:A4ZDL6"
FT BINDING 118
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:A4ZDL6"
FT BINDING 129
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000250|UniProtKB:A4ZDL6"
FT DISULFID 35..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 87..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 99..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
SQ SEQUENCE 133 AA; 13879 MW; BDF6EDC020F75815 CRC64;
MSMGSFGFAL AVMVLAVLVA SAAGAPNTNF VSSACNTKKI PSGNPFFNNL GALLVNLEKN
TAFSGYDYKA SRAGSGGAPT AYGRGVCKQS ISQSDCTACL TNLGGRIWGI CKNAIGARVQ
LTDCFIRYEQ YSI