ID   G276_ARTOA              Reviewed;         379 AA.
AC   G1X5Y2;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Fucose-specific lectin g276 {ECO:0000303|PubMed:35142828};
GN   ORFNames=AOL_s00054g276;
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491;
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=35142828; DOI=10.1093/femsle/fnac013;
RA   Si J., Dong X., Zhang G., Lu H., Tang K., Zhang L., Kong X., Sheng K.,
RA   Wang J., Zha X., Wang Y.;
RT   "The fucose-specific lectin gene AOL_s00054g276 affects trap formation and
RT   nematocidal activity of the nematophagous fungus Arthrobotrys oligospora.";
RL   FEMS Microbiol. Lett. 369:0-0(2022).
CC   -!- FUNCTION: Lectin that specifically binds to L-fucose (PubMed:35142828).
CC       Is associated with the morphogenesis of the fungus, and plays a role in
CC       the formation of the constricting rings involved in nematode-trapping
CC       (PubMed:35142828). {ECO:0000269|PubMed:35142828,
CC       ECO:0000305|PubMed:35142828}.
CC   -!- DISRUPTION PHENOTYPE: Delays trap formation and weakens nematocidal
CC       activity (PubMed:35142828). Does not affect mycelial growth, conidia
CC       production, conidial germination rates and adaption to environmental
CC       stresses (PubMed:35142828). {ECO:0000269|PubMed:35142828}.
CC   -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC       {ECO:0000305}.
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DR   EMBL; ADOT01000084; EGX51577.1; -; Genomic_DNA.
DR   RefSeq; XP_011119894.1; XM_011121592.1.
DR   SMR; G1X5Y2; -.
DR   EnsemblFungi; EGX51577; EGX51577; AOL_s00054g276.
DR   GeneID; 22890800; -.
DR   HOGENOM; CLU_729524_0_0_1; -.
DR   InParanoid; G1X5Y2; -.
DR   OrthoDB; 1081005at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   InterPro; IPR012475; Fungal_lectin.
DR   Pfam; PF07938; Fungal_lectin; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Virulence.
FT   CHAIN           1..379
FT                   /note="Fucose-specific lectin g276"
FT                   /id="PRO_0000456236"
FT   BINDING         126
FT                   /ligand="alpha-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         126
FT                   /ligand="beta-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42589"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         163
FT                   /ligand="beta-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42589"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         185
FT                   /ligand="alpha-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         185
FT                   /ligand="beta-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42589"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         222
FT                   /ligand="alpha-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         234
FT                   /ligand="alpha-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         242
FT                   /ligand="beta-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42589"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         282
FT                   /ligand="beta-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42589"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
FT   BINDING         289
FT                   /ligand="alpha-L-fucose"
FT                   /ligand_id="ChEBI:CHEBI:42548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P18891"
SQ   SEQUENCE   379 AA;  42411 MW;  666A3C624F2A2D69 CRC64;
     MPFEARDDNV DPDAIGNHYH DDGLLWQTHY AAVEVFDYPH ATMHMKIFCQ SYWGELHDLT
     FSYKRGSTKE PEEENAWETK FRQSLARPGT DEAAMMHTPL AAVVRYDTGN PTTHLFYIST
     GFKIREVIWK NGSQTNDCLG ITVCPTSSLA VTKWGAGSQT HFRLYYQSKA GTIEEHCLDC
     NAGTWTKGAT LSGPVSAYDD DSPLRGTSLS FINLAQDKPE LRGYFQTAKG SIQEFTYKGT
     KWSTSKIGVD AAPFRTPLAA ITVEKNKIAA LYYVDAYNRI NEVLWEGDWE GSERIDGESV
     APGTRLAVAS LKYIGHDKIH MFSSGLVNVI TQRVWTRENG AWGDRPTIVD FEAPVQVEVE
     PGLDPAIHLT KPTRDGRRV