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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //