CONA_CANRO
ID CONA_CANRO Reviewed; 236 AA.
AC P81364;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Concanavalin-Ma;
DE Short=Con Ma;
OS Canavalia rosea (Beach bean) (Canavalia maritima).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX NCBI_TaxID=3825;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1367779; DOI=10.1016/0031-9422(91)85111-c;
RA Perez G., Perez C., Sousa-Cavada B., Moreira R., Richardson M.;
RT "Comparison of the amino acid sequences of the lectins from seeds of
RT Dioclea lehmanni and Canavalia maritima.";
RL Phytochemistry 30:2619-2621(1991).
CC -!- FUNCTION: Glucose/D-mannose specific lectin.
CC -!- SUBUNIT: Homotetramer.
CC -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC and one calcium ion. The metal ions are essential for the saccharide-
CC binding and cell-agglutinating activities.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; B45587; B45587.
DR PDB; 2CWM; X-ray; 1.95 A; A/D=1-236.
DR PDB; 2OW4; X-ray; 1.60 A; A=1-236.
DR PDB; 2P34; X-ray; 2.10 A; A/B/C/D=1-236.
DR PDB; 2P37; X-ray; 2.10 A; A/B/C/D=1-236.
DR PDBsum; 2CWM; -.
DR PDBsum; 2OW4; -.
DR PDBsum; 2P34; -.
DR PDBsum; 2P37; -.
DR SMR; P81364; -.
DR UniLectin; P81364; -.
DR EvolutionaryTrace; P81364; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..236
FT /note="Concanavalin-Ma"
FT /id="PRO_0000105086"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 98..99
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2OW4"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:2OW4"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2OW4"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2CWM"
FT STRAND 104..120
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2CWM"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2OW4"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:2OW4"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2OW4"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2OW4"
SQ SEQUENCE 236 AA; 25364 MW; D67791C3B0EB150A CRC64;
ADTIVAVELD TYPNTDVGDP SYPHXXXXXX SVRXXTAKWN MQNGKVGTAH ISYNSVGKRL
SAVVSYPNGD SATVSYDVDL DNVLPEWVRV GLSASTGLYK ETNTILSWSF TSKLKSNSTH
ETNALHFMFN QFTKDQKDLI LQSDATTGTD GNLXXTRVSS NGPSQGSTVG RALFYAPVHI
WESSATVAGF DATFXXLIKS PDSHPADGIA FFISNIDSSI PSGSTGRLLG LFPDAN