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AGGL_SCLS1
ID   AGGL_SCLS1              Reviewed;         153 AA.
AC   A7EWX9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Agglutinin {ECO:0000250|UniProtKB:A7XUK7};
GN   ORFNames=SS1G_09838;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1] {ECO:0000312|EMBL:EDN93971.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Lectin that primarily recognizes glycans with a non-reducing
CC       terminal N-acetylgalactosamine (GalNAc), with a preference for the
CC       alpha- over the beta-anomer. Can also bind non-reducing terminal
CC       galactose (Gal) residues but with a lower affinity. Strongly interacts
CC       with glycolipid type glycans with terminal non-reducing Gal or GalNAc
CC       but fails to bind sialylated or fucosylated forms of the same glycans.
CC       Strongly interacts with galactosylated N-glycans, displaying highest
CC       affinity for alpha-1-3 branched mono-antennary N-glycans but also
CC       binding to multi-antennary glycans (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A7XUK7}.
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DR   EMBL; CH476634; EDN93971.1; -; Genomic_DNA.
DR   RefSeq; XP_001589205.1; XM_001589155.1.
DR   AlphaFoldDB; A7EWX9; -.
DR   SMR; A7EWX9; -.
DR   GeneID; 5485273; -.
DR   KEGG; ssl:SS1G_09838; -.
DR   VEuPathDB; FungiDB:sscle_01g001830; -.
DR   InParanoid; A7EWX9; -.
DR   OMA; YEIVPYQ; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF14200; RicinB_lectin_2; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
PE   3: Inferred from homology;
KW   Lectin; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:A7XUK7"
FT   CHAIN           2..153
FT                   /note="Agglutinin"
FT                   /evidence="ECO:0000250|UniProtKB:A7XUK7"
FT                   /id="PRO_0000424171"
FT   DOMAIN          58..153
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255"
FT   BINDING         22..25
FT                   /ligand="beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:546807"
FT                   /evidence="ECO:0000250|UniProtKB:A7XUK7"
FT   BINDING         46
FT                   /ligand="beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:546807"
FT                   /evidence="ECO:0000250|UniProtKB:A7XUK7"
SQ   SEQUENCE   153 AA;  16740 MW;  BDAC0EF1FA1ED374 CRC64;
     MGFKGVGTYE IVPYQAPSLN LNAWEGKLEP GAVVRTYTRG DKPSDNAKWQ VALVAGSGDS
     AEYLIINVHS GYFLTATKEN HIVSTPQISP TDPSARWTIK PATTHQYEVF TINNKVSELG
     QLTVKDYSTH SGADVLSASA KTADNQKWYF DAK
 
 
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