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1.C.4.4.3
Hemolytic lectin LSLc exhibits hemolytic and hemagglutinating activities. The structure at 2.6 Å resolution has been determined (Mancheño et al., 2005). The protein is hexameric. The monomer (35kDa) consists of two distinct modules: an N-terminal lectin module (a β-trefoil scaffold) and a pore-forming module (composed of domains 2 and 4) which resemble the β-pore-forming domains of aerolysin and ε-toxin (Mancheño et al., 2005).

Accession Number:Q7Z8U9
Protein Name:Hemolytic lectin LSLc
Length:315
Molecular Weight:35233.00
Species:Laetiporus sulphureus [5630]
Location1 / Topology2 / Orientation3: Secreted1
Substrate small molecules

Cross database links:

Gene Ontology

GO:0005529 F:sugar binding

References (1)

[1] “Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins.”  Tateno H.et.al.   12900403

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FASTA formatted sequence
1:	MIDIYIPPND LYFRLLGFVS QKVIYAYPFP RPDVGLSEVN DESTQQYFSL IHGTGERAGL 
61:	YAIKSKATGN VLFSRTHRDP YVGQDPENAR YNDNWFKIEP GKDDLSKYFR LVVPSTGTAL 
121:	VSRTNLEPYF WNSAQTPIRS DQYFIFLFKD MRIDKIEYDL KDGRILSSTP NVLATQTLAN 
181:	TSSQTQEMSF NLSQTLTQTS TFAYTAGFTI AVGTAFKAGV PIFAETEFKV DISVDNQWNW 
241:	GEENTFSKTC TATFSVRAGP GETVKAVSTV DSGIINVPFT AYLSSKSTGF EVTTEGIWRG 
301:	VSSWDLRHTL TSVTA