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Conserved domains on  [gi|2098431]
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Chain C, CONCANAVALIN A

Protein Classification

L-type lectin family protein( domain architecture ID 10160924)

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 ...
 4-115 1.42e-44

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: 149.30  E-value: 1.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431    4 IVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQ-----NGKVGTAHIIYNSVDKRLSAVVSYPNA---DSATV 75
Cdd:cd06899 117 IVAVEFDTFQNPEFGDPDDNHVGIDVNSLVSVKAGYWDDDggklkSGKPMQAWIDYDSSSKRLSVTLAYSGVakpKKPLL 196

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2098431   76 SYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKL 115
Cdd:cd06899 197 SYPVDLSKVLPEEVYVGFSASTGLLTELHYILSWSFSSNG 236
lectin_L-type super family cl14058
legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate ...
 126-237 1.91e-31

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.


The actual alignment was detected with superfamily member cd06899:

Pssm-ID: 472686  Cd Length: 236  Bit Score: 115.40  E-value: 1.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431  126 LHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNgspqGSSVGRALFYAPVHIWESS-AVVASFEATFTFLIKSPD- 203
Cdd:cd06899   1 LSFNFNGFSSDQSNLTLQGDATISSNGALQLTNDTSP----ASSVGRALYSKPVRLWDSTtGKVASFSTSFSFSITPPNp 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 2098431  204 SHPADGIAFFISNIDSSIPsGSTGRLLGLFPDAN 237
Cdd:cd06899  77 SLGGDGLAFFLAPTDSLPP-ASSGGYLGLFNSSN 109
 
Name Accession Description Interval E-value
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
 4-115 1.42e-44

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: 149.30  E-value: 1.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431    4 IVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQ-----NGKVGTAHIIYNSVDKRLSAVVSYPNA---DSATV 75
Cdd:cd06899 117 IVAVEFDTFQNPEFGDPDDNHVGIDVNSLVSVKAGYWDDDggklkSGKPMQAWIDYDSSSKRLSVTLAYSGVakpKKPLL 196

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2098431   76 SYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKL 115
Cdd:cd06899 197 SYPVDLSKVLPEEVYVGFSASTGLLTELHYILSWSFSSNG 236
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
 126-237 1.91e-31

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: 115.40  E-value: 1.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431  126 LHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNgspqGSSVGRALFYAPVHIWESS-AVVASFEATFTFLIKSPD- 203
Cdd:cd06899   1 LSFNFNGFSSDQSNLTLQGDATISSNGALQLTNDTSP----ASSVGRALYSKPVRLWDSTtGKVASFSTSFSFSITPPNp 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 2098431  204 SHPADGIAFFISNIDSSIPsGSTGRLLGLFPDAN 237
Cdd:cd06899  77 SLGGDGLAFFLAPTDSLPP-ASSGGYLGLFNSSN 109
Lectin_legB pfam00139
Legume lectin domain;
4-113 3.77e-28

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 106.95  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431      4 IVAVELDTYPNTDIgDPSYPHIGIDIKSVRSKKT--AKW---NMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSA----T 74
Cdd:pfam00139 115 IVAVEFDTFQNPEF-DIPGNHVGIDVNSLVSVKSapAGWknlSLSSGKPMQVWIDYDGSTKNLSVTLAPYGLNNKpkrpL 193

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2098431     75 VSYDVDLDNVLPEwVRVGLSASTGLYKETNTILSWSFTS 113
Cdd:pfam00139 194 LSYPVDLSKVLPE-VYVGFSASTGNVSELHYILSWSFSS 231
Lectin_legB pfam00139
Legume lectin domain;
125-237 4.05e-21

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 88.46  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431    125 ALHFMFNQFSKDQkDLILQGDATTgTDGNLELTRVSSNgspqgSSVGRALFYAPVHIWE-SSAVVASFEATFTFLIKS-P 202
Cdd:pfam00139   1 SLSFNFNGFSNSS-NLSLDGDASV-SNGLLQLTNDTSN-----SSVGRAFYPKPLRLWDkASGNVASFSTSFVFAIPSsN 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2098431    203 DSHPADGIAFFISNiDSSIPSGSTGRLLGLFPDAN 237
Cdd:pfam00139  74 NSLSGHGLAFFLAP-TPSLPNASSGGYLGLFNSTT 107
 
Name Accession Description Interval E-value
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
 4-115 1.42e-44

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: 149.30  E-value: 1.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431    4 IVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQ-----NGKVGTAHIIYNSVDKRLSAVVSYPNA---DSATV 75
Cdd:cd06899 117 IVAVEFDTFQNPEFGDPDDNHVGIDVNSLVSVKAGYWDDDggklkSGKPMQAWIDYDSSSKRLSVTLAYSGVakpKKPLL 196

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2098431   76 SYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKL 115
Cdd:cd06899 197 SYPVDLSKVLPEEVYVGFSASTGLLTELHYILSWSFSSNG 236
lectin_legume_LecRK_Arcelin_ConA cd06899
legume lectins, lectin-like receptor kinases, arcelin, concanavalinA, and alpha-amylase ...
 126-237 1.91e-31

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: 115.40  E-value: 1.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431  126 LHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNgspqGSSVGRALFYAPVHIWESS-AVVASFEATFTFLIKSPD- 203
Cdd:cd06899   1 LSFNFNGFSSDQSNLTLQGDATISSNGALQLTNDTSP----ASSVGRALYSKPVRLWDSTtGKVASFSTSFSFSITPPNp 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 2098431  204 SHPADGIAFFISNIDSSIPsGSTGRLLGLFPDAN 237
Cdd:cd06899  77 SLGGDGLAFFLAPTDSLPP-ASSGGYLGLFNSSN 109
Lectin_legB pfam00139
Legume lectin domain;
4-113 3.77e-28

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 106.95  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431      4 IVAVELDTYPNTDIgDPSYPHIGIDIKSVRSKKT--AKW---NMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSA----T 74
Cdd:pfam00139 115 IVAVEFDTFQNPEF-DIPGNHVGIDVNSLVSVKSapAGWknlSLSSGKPMQVWIDYDGSTKNLSVTLAPYGLNNKpkrpL 193

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2098431     75 VSYDVDLDNVLPEwVRVGLSASTGLYKETNTILSWSFTS 113
Cdd:pfam00139 194 LSYPVDLSKVLPE-VYVGFSASTGNVSELHYILSWSFSS 231
Lectin_legB pfam00139
Legume lectin domain;
125-237 4.05e-21

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 88.46  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431    125 ALHFMFNQFSKDQkDLILQGDATTgTDGNLELTRVSSNgspqgSSVGRALFYAPVHIWE-SSAVVASFEATFTFLIKS-P 202
Cdd:pfam00139   1 SLSFNFNGFSNSS-NLSLDGDASV-SNGLLQLTNDTSN-----SSVGRAFYPKPLRLWDkASGNVASFSTSFVFAIPSsN 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2098431    203 DSHPADGIAFFISNiDSSIPSGSTGRLLGLFPDAN 237
Cdd:pfam00139  74 NSLSGHGLAFFLAP-TPSLPNASSGGYLGLFNSTT 107
lectin_L-type cd01951
legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate ...
 5-113 1.43e-15

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: 72.85  E-value: 1.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431    5 VAVELDTYPNTDIGDPSYPHIGIDIKS---------VRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYP-NADSAT 74
Cdd:cd01951 105 VAVEFDTYKNDDNNDPNGNHISIDVNGngnntalatSLGSASLPNGTGLGNEHTVRITYDPTTNTLTVYLDNGsTLTSLD 184

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2098431   75 VSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTS 113
Cdd:cd01951 185 ITIPVDLIQLGPTKAYFGFTASTGGLTNLHDILNWSFTS 223
lectin_L-type cd01951
legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate ...
 131-227 9.28e-11

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: 59.75  E-value: 9.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098431  131 NQFSKDQKDLILQGDAT-TGTDGNLELTrvssngSPQGSSVGRALFYAPVHIWessavvASFEATFTFLIKSPDSHPADG 209
Cdd:cd01951   7 NFSNNNQSNWQLNGSATlTTDSGVLRLT------PDTGNQAGSAWYKTPIDLS------KDFTTTFKFYLGTKGTNGADG 74

                        90
                ....*....|....*...
gi 2098431  210 IAFFISNIDSSIPSGSTG 227
Cdd:cd01951  75 IAFVLQNDPAGALGGGGG 92
 
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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