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Conserved domains on  [gi|15228229|ref|NP_188274|]
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Legume lectin family protein [Arabidopsis thaliana]

Protein Classification

L-type lectin family protein( domain architecture ID 10160902)

L-type (leguminous) lectin family protein binds carbohydrates using a a dome-shaped beta-barrel carbohydrate recognition domain

CATH:  2.60.120.200
Gene Ontology:  GO:0030246|GO:0046872
PubMed:  14572026|14533788
SCOP:  4000327

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
20-270 8.52e-90

legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase inhibitor; This alignment model includes the legume lectins (also known as agglutinins), the arcelin (also known as phytohemagglutinin-L) family of lectin-like defense proteins, the LecRK family of lectin-like receptor kinases, concanavalinA (ConA), and an alpha-amylase inhibitor. Arcelin is a major seed glycoprotein discovered in kidney beans (Phaseolus vulgaris) that has insecticidal properties and protects the seeds from predation by larvae of various bruchids. Arcelin is devoid of monosaccharide binding properties and lacks a key metal-binding loop that is present in other members of this family. Phytohaemagglutinin (PHA) is a lectin found in plants, especially beans, that affects cell metabolism by inducing mitosis and by altering the permeability of the cell membrane to various proteins. PHA agglutinates most mammalian red blood cell types by binding glycans on the cell surface. Medically, PHA is used as a mitogen to trigger cell division in T-lymphocytes and to activate latent HIV-1 from human peripheral lymphocytes. Plant L-type lectins are primarily found in the seeds of leguminous plants where they constitute about 10% of the total soluble protein of the seed extracts. They are synthesized during seed development several weeks after flowering and transported to the vacuole where they become condensed into specialized vesicles called protein bodies. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely.


:

Pssm-ID: 173887  Cd Length: 236  Bit Score: 266.02  E-value: 8.52e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  20 VKFNFDSFDG--SNLLFLGDAElgpssdgVSRSGALSMTRDENP-FSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITP 96
Cdd:cd06899   1 LSFNFNGFSSdqSNLTLQGDAT-------ISSNGALQLTNDTSPaSSVGRALYSKPVRLWDSTTGKVASFSTSFSFSITP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  97 RTKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFLDISGNHVGVNINSMTSlvaEKA 176
Cdd:cd06899  74 PNPSLGGDGLAFFLAPTDSLPPASSGGYLGLFNSSNNGNSSNHIVAVEFDTFQNPEFGDPDDNHVGIDVNSLVS---VKA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229 177 GYwvqtrvgkrkvWSFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENVKKPKRALIEAPRVLNEVLLQNMYAGFAGSMG 256
Cdd:cd06899 151 GY-----------WDDDGGKLKSGKPMQAWIDYDSSSKRLSVTLAYSGVAKPKKPLLSYPVDLSKVLPEEVYVGFSASTG 219
                       250
                ....*....|....
gi 15228229 257 RAVERHDIWSWSFE 270
Cdd:cd06899 220 LLTELHYILSWSFS 233
 
Name Accession Description Interval E-value
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
20-270 8.52e-90

legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase inhibitor; This alignment model includes the legume lectins (also known as agglutinins), the arcelin (also known as phytohemagglutinin-L) family of lectin-like defense proteins, the LecRK family of lectin-like receptor kinases, concanavalinA (ConA), and an alpha-amylase inhibitor. Arcelin is a major seed glycoprotein discovered in kidney beans (Phaseolus vulgaris) that has insecticidal properties and protects the seeds from predation by larvae of various bruchids. Arcelin is devoid of monosaccharide binding properties and lacks a key metal-binding loop that is present in other members of this family. Phytohaemagglutinin (PHA) is a lectin found in plants, especially beans, that affects cell metabolism by inducing mitosis and by altering the permeability of the cell membrane to various proteins. PHA agglutinates most mammalian red blood cell types by binding glycans on the cell surface. Medically, PHA is used as a mitogen to trigger cell division in T-lymphocytes and to activate latent HIV-1 from human peripheral lymphocytes. Plant L-type lectins are primarily found in the seeds of leguminous plants where they constitute about 10% of the total soluble protein of the seed extracts. They are synthesized during seed development several weeks after flowering and transported to the vacuole where they become condensed into specialized vesicles called protein bodies. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely.


Pssm-ID: 173887  Cd Length: 236  Bit Score: 266.02  E-value: 8.52e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  20 VKFNFDSFDG--SNLLFLGDAElgpssdgVSRSGALSMTRDENP-FSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITP 96
Cdd:cd06899   1 LSFNFNGFSSdqSNLTLQGDAT-------ISSNGALQLTNDTSPaSSVGRALYSKPVRLWDSTTGKVASFSTSFSFSITP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  97 RTKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFLDISGNHVGVNINSMTSlvaEKA 176
Cdd:cd06899  74 PNPSLGGDGLAFFLAPTDSLPPASSGGYLGLFNSSNNGNSSNHIVAVEFDTFQNPEFGDPDDNHVGIDVNSLVS---VKA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229 177 GYwvqtrvgkrkvWSFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENVKKPKRALIEAPRVLNEVLLQNMYAGFAGSMG 256
Cdd:cd06899 151 GY-----------WDDDGGKLKSGKPMQAWIDYDSSSKRLSVTLAYSGVAKPKKPLLSYPVDLSKVLPEEVYVGFSASTG 219
                       250
                ....*....|....
gi 15228229 257 RAVERHDIWSWSFE 270
Cdd:cd06899 220 LLTELHYILSWSFS 233
Lectin_legB pfam00139
Legume lectin domain;
19-270 1.03e-80

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 243.31  E-value: 1.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229    19 AVKFNFDSF-DGSNLLFLGDAelgpssdgVSRSGALSMTRDENPFSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITPR 97
Cdd:pfam00139   1 SLSFNFNGFsNSSNLSLDGDA--------SVSNGLLQLTNDTSNSSVGRAFYPKPLRLWDKASGNVASFSTSFVFAIPSS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229    98 TKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFlDISGNHVGVNINSMTSLVAEKAG 177
Cdd:pfam00139  73 NNSLSGHGLAFFLAPTPSLPNASSGGYLGLFNSTTNGNSSNHIVAVEFDTFQNPEF-DIPGNHVGIDVNSLVSVKSAPAG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229   178 ywvqtrvgkrkvwsFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENV-KKPKRALIEAPRVLNEVlLQNMYAGFAGSMG 256
Cdd:pfam00139 152 --------------WKNLSLSSGKPMQVWIDYDGSTKNLSVTLAPYGLnNKPKRPLLSYPVDLSKV-LPEVYVGFSASTG 216
                         250
                  ....*....|....
gi 15228229   257 RAVERHDIWSWSFE 270
Cdd:pfam00139 217 NVSELHYILSWSFS 230
 
Name Accession Description Interval E-value
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
20-270 8.52e-90

legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase inhibitor; This alignment model includes the legume lectins (also known as agglutinins), the arcelin (also known as phytohemagglutinin-L) family of lectin-like defense proteins, the LecRK family of lectin-like receptor kinases, concanavalinA (ConA), and an alpha-amylase inhibitor. Arcelin is a major seed glycoprotein discovered in kidney beans (Phaseolus vulgaris) that has insecticidal properties and protects the seeds from predation by larvae of various bruchids. Arcelin is devoid of monosaccharide binding properties and lacks a key metal-binding loop that is present in other members of this family. Phytohaemagglutinin (PHA) is a lectin found in plants, especially beans, that affects cell metabolism by inducing mitosis and by altering the permeability of the cell membrane to various proteins. PHA agglutinates most mammalian red blood cell types by binding glycans on the cell surface. Medically, PHA is used as a mitogen to trigger cell division in T-lymphocytes and to activate latent HIV-1 from human peripheral lymphocytes. Plant L-type lectins are primarily found in the seeds of leguminous plants where they constitute about 10% of the total soluble protein of the seed extracts. They are synthesized during seed development several weeks after flowering and transported to the vacuole where they become condensed into specialized vesicles called protein bodies. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely.


Pssm-ID: 173887  Cd Length: 236  Bit Score: 266.02  E-value: 8.52e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  20 VKFNFDSFDG--SNLLFLGDAElgpssdgVSRSGALSMTRDENP-FSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITP 96
Cdd:cd06899   1 LSFNFNGFSSdqSNLTLQGDAT-------ISSNGALQLTNDTSPaSSVGRALYSKPVRLWDSTTGKVASFSTSFSFSITP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  97 RTKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFLDISGNHVGVNINSMTSlvaEKA 176
Cdd:cd06899  74 PNPSLGGDGLAFFLAPTDSLPPASSGGYLGLFNSSNNGNSSNHIVAVEFDTFQNPEFGDPDDNHVGIDVNSLVS---VKA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229 177 GYwvqtrvgkrkvWSFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENVKKPKRALIEAPRVLNEVLLQNMYAGFAGSMG 256
Cdd:cd06899 151 GY-----------WDDDGGKLKSGKPMQAWIDYDSSSKRLSVTLAYSGVAKPKKPLLSYPVDLSKVLPEEVYVGFSASTG 219
                       250
                ....*....|....
gi 15228229 257 RAVERHDIWSWSFE 270
Cdd:cd06899 220 LLTELHYILSWSFS 233
Lectin_legB pfam00139
Legume lectin domain;
19-270 1.03e-80

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 243.31  E-value: 1.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229    19 AVKFNFDSF-DGSNLLFLGDAelgpssdgVSRSGALSMTRDENPFSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITPR 97
Cdd:pfam00139   1 SLSFNFNGFsNSSNLSLDGDA--------SVSNGLLQLTNDTSNSSVGRAFYPKPLRLWDKASGNVASFSTSFVFAIPSS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229    98 TKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFlDISGNHVGVNINSMTSLVAEKAG 177
Cdd:pfam00139  73 NNSLSGHGLAFFLAPTPSLPNASSGGYLGLFNSTTNGNSSNHIVAVEFDTFQNPEF-DIPGNHVGIDVNSLVSVKSAPAG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229   178 ywvqtrvgkrkvwsFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENV-KKPKRALIEAPRVLNEVlLQNMYAGFAGSMG 256
Cdd:pfam00139 152 --------------WKNLSLSSGKPMQVWIDYDGSTKNLSVTLAPYGLnNKPKRPLLSYPVDLSKV-LPEVYVGFSASTG 216
                         250
                  ....*....|....
gi 15228229   257 RAVERHDIWSWSFE 270
Cdd:pfam00139 217 NVSELHYILSWSFS 230
lectin_L-type cd01951
legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate ...
22-269 3.35e-21

legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate binding proteins that generally display no enzymatic activity toward the sugars they bind. This family includes arcelin, concanavalinA, the lectin-like receptor kinases, the ERGIC-53/VIP36/EMP46 type1 transmembrane proteins, and an alpha-amylase inhibitor. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely.


Pssm-ID: 173886 [Multi-domain]  Cd Length: 223  Bit Score: 89.03  E-value: 3.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229  22 FNFDSFDGSNLLFLgdaELGPSSDGVSRSGALSMTRDENpFSHGQGLYINQIPFKpsntsspFSFETSFTFSITpRTKPN 101
Cdd:cd01951   3 LNFSNFSNNNQSNW---QLNGSATLTTDSGVLRLTPDTG-NQAGSAWYKTPIDLS-------KDFTTTFKFYLG-TKGTN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229 102 SGQGFAFIITPEADNSGASDGGYLGILNKTNdgkpeNHILAIEFDTFQNKEFLDISGNHVGVNINSMTSLVAEKAGywvq 181
Cdd:cd01951  71 GADGIAFVLQNDPAGALGGGGGGGGLGYGGI-----GNSVAVEFDTYKNDDNNDPNGNHISIDVNGNGNNTALATS---- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228229 182 trvgkRKVWSFKDVNlSSGERFKAWVEFRNKDSTITVTLapENVKKPKRALIEAPRVLNEVLLQNMYAGFAGSMGRAVER 261
Cdd:cd01951 142 -----LGSASLPNGT-GLGNEHTVRITYDPTTNTLTVYL--DNGSTLTSLDITIPVDLIQLGPTKAYFGFTASTGGLTNL 213

                ....*...
gi 15228229 262 HDIWSWSF 269
Cdd:cd01951 214 HDILNWSF 221
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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