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Lectin II (Fragment)

 Q9FVF8_ULEEU            Unreviewed;       258 AA.
Q9FVF8;
01-MAR-2001, integrated into UniProtKB/TrEMBL.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 95.
SubName: Full=Lectin II {ECO:0000313|EMBL:AAG16779.1};
Flags: Fragment;
Ulex europaeus (Furze).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Genisteae; Ulex.
NCBI_TaxID=3902 {ECO:0000313|EMBL:AAG16779.1};
[1] {ECO:0000213|PDB:1DZQ, ECO:0000213|PDB:1QOO, ECO:0000313|EMBL:AAG16779.1}
NUCLEOTIDE SEQUENCE.
PubMed=10966800; DOI=10.1006/jmbi.2000.4016;
Loris R., De Greve H., Dao-Thi M.H., Messens J., Imberty A., Wyns L.;
"Structural basis of carbohydrate recognition by lectin II from Ulex
europaeus, a protein with a promiscuous carbohydrate-binding site.";
J. Mol. Biol. 301:987-1002(2000).
-!- SIMILARITY: Belongs to the leguminous lectin family.
{ECO:0000256|SAAS:SAAS00549309}.
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EMBL; AF190633; AAG16779.1; -; mRNA.
PDB; 1DZQ; X-ray; 2.85 A; A/B/C/D=1-242.
PDB; 1QOO; X-ray; 2.75 A; A/B/C/D=1-242.
PDB; 1QOS; X-ray; 2.95 A; A/B=1-242.
PDB; 1QOT; X-ray; 3.00 A; A/B/C/D=1-242.
PDBsum; 1DZQ; -.
PDBsum; 1QOO; -.
PDBsum; 1QOS; -.
PDBsum; 1QOT; -.
ProteinModelPortal; Q9FVF8; -.
SMR; Q9FVF8; -.
PRIDE; Q9FVF8; -.
EvolutionaryTrace; Q9FVF8; -.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd06899; lectin_legume_LecRK_Arcelin_Co; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR016363; L-lectin.
InterPro; IPR000985; Lectin_LegA_CS.
InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
InterPro; IPR001220; Legume_lectin_dom.
Pfam; PF00139; Lectin_legB; 1.
PIRSF; PIRSF002690; L-type_lectin_plant; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:1DZQ, ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS, ECO:0000213|PDB:1QOT};
Calcium {ECO:0000213|PDB:1DZQ, ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS, ECO:0000213|PDB:1QOT};
Lectin {ECO:0000256|SAAS:SAAS00479709};
Manganese {ECO:0000213|PDB:1DZQ, ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS, ECO:0000213|PDB:1QOT};
Metal-binding {ECO:0000213|PDB:1DZQ, ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS, ECO:0000213|PDB:1QOT}.
DOMAIN 6 243 Lectin_legB. {ECO:0000259|Pfam:PF00139}.
REGION 101 104 N-acetyl-D-glucosamine binding.
{ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
REGION 135 136 N-acetyl-D-glucosamine binding.
{ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
REGION 220 223 Galactose binding. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOT}.
METAL 126 126 Manganese. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 128 128 Calcium. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 128 128 Manganese. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 130 130 Calcium; via carbonyl oxygen.
{ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 136 136 Calcium. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 139 139 Calcium. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 139 139 Manganese. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
METAL 144 144 Manganese; via tele nitrogen.
{ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
BINDING 86 86 Galactose. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOT}.
BINDING 86 86 N-acetyl-D-glucosamine.
{ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
BINDING 104 104 Fucose. {ECO:0000213|PDB:1QOT}.
BINDING 130 130 Galactose. {ECO:0000213|PDB:1QOT}.
BINDING 130 130 N-acetyl-D-glucosamine.
{ECO:0000213|PDB:1QOO}.
BINDING 135 135 Fucose. {ECO:0000213|PDB:1QOT}.
BINDING 135 135 Galactose. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOT}.
BINDING 199 199 N-acetyl-D-glucosamine; via carbonyl
oxygen. {ECO:0000213|PDB:1QOS}.
BINDING 219 219 N-acetyl-D-glucosamine; via carbonyl
oxygen. {ECO:0000213|PDB:1QOO}.
DISULFID 184 184 Interchain. {ECO:0000213|PDB:1DZQ,
ECO:0000213|PDB:1QOO,
ECO:0000213|PDB:1QOS}.
NON_TER 1 1 {ECO:0000313|EMBL:AAG16779.1}.
SEQUENCE 258 AA; 27909 MW; 581F6DD8F5E049FB CRC64;
NLSDDLSFNF DKFVPNQKNI IFQGAASVST TGVLQVTKVS KPTTTSIGRA LYAAPIQIWD
STTGKVASFA TSFSFVVKAD KSDGVDGLAF FLAPANSQIP SGSSASMFGL FNSSDSKSSN
QIIAVEFDTY FGKAYNPWDP DFKHIGIDVN SIKSIKTVKW DWRNGEVADV VITYRAPTKS
LTVCLSYPSD ETSNIITASV DLKAILPEWV SVGFSGGVGN AAEFETHDIL SWYFTSNLEA
NNPAAMEYND EHLASFTA


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