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Conserved domains on  [gi|18400173|ref|NP_565548|]
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Late embryogenesis abundant protein, group 6 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LEA_6 super family cl11310
Late embryogenesis abundant protein 18; This is a family of late embryogenesis-abundant ...
20-77 1.19e-14

Late embryogenesis abundant protein 18; This is a family of late embryogenesis-abundant proteins There is high accumulation of this protein in dry seeds, and in the roots of full-grown plants in response to dehydration and ABA (abscisic acid application) treatments. This LEA protein disappears after germination. It accumulates in growing regions of well irrigated hypocotyls and meristems suggesting a role in seedling growth resumption on rehydration. As a group the LEA proteins are highly hydrophilic, contain a high percentage of glycine residues, lack Cys and Trp residues and do not coagulate upon exposure to high temperature, and for these reasons are considered to be members of a group of proteins called hydrophilins. Expression of the protein is negatively regulated during etiolating growth, particularly in roots, in contrast to its expression patterns during normal growth.


The actual alignment was detected with superfamily member pfam10714:

Pssm-ID: 371207  Cd Length: 75  Bit Score: 62.17  E-value: 1.19e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18400173   20 QVKDNDLPT-DSPYMATGTLEDYKLKAYGAEGHQEPTPGLGGGSTDAPTPSGDAPAATT 77
Cdd:pfam10714  3 ESKLDGLPMeSSPYLKYKDLEDYKRQGYGTQGHQEPKPGRGGGATDAPTLSGGGDSSSA 61
 
Name Accession Description Interval E-value
LEA_6 pfam10714
Late embryogenesis abundant protein 18; This is a family of late embryogenesis-abundant ...
20-77 1.19e-14

Late embryogenesis abundant protein 18; This is a family of late embryogenesis-abundant proteins There is high accumulation of this protein in dry seeds, and in the roots of full-grown plants in response to dehydration and ABA (abscisic acid application) treatments. This LEA protein disappears after germination. It accumulates in growing regions of well irrigated hypocotyls and meristems suggesting a role in seedling growth resumption on rehydration. As a group the LEA proteins are highly hydrophilic, contain a high percentage of glycine residues, lack Cys and Trp residues and do not coagulate upon exposure to high temperature, and for these reasons are considered to be members of a group of proteins called hydrophilins. Expression of the protein is negatively regulated during etiolating growth, particularly in roots, in contrast to its expression patterns during normal growth.


Pssm-ID: 371207  Cd Length: 75  Bit Score: 62.17  E-value: 1.19e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18400173   20 QVKDNDLPT-DSPYMATGTLEDYKLKAYGAEGHQEPTPGLGGGSTDAPTPSGDAPAATT 77
Cdd:pfam10714  3 ESKLDGLPMeSSPYLKYKDLEDYKRQGYGTQGHQEPKPGRGGGATDAPTLSGGGDSSSA 61
 
Name Accession Description Interval E-value
LEA_6 pfam10714
Late embryogenesis abundant protein 18; This is a family of late embryogenesis-abundant ...
20-77 1.19e-14

Late embryogenesis abundant protein 18; This is a family of late embryogenesis-abundant proteins There is high accumulation of this protein in dry seeds, and in the roots of full-grown plants in response to dehydration and ABA (abscisic acid application) treatments. This LEA protein disappears after germination. It accumulates in growing regions of well irrigated hypocotyls and meristems suggesting a role in seedling growth resumption on rehydration. As a group the LEA proteins are highly hydrophilic, contain a high percentage of glycine residues, lack Cys and Trp residues and do not coagulate upon exposure to high temperature, and for these reasons are considered to be members of a group of proteins called hydrophilins. Expression of the protein is negatively regulated during etiolating growth, particularly in roots, in contrast to its expression patterns during normal growth.


Pssm-ID: 371207  Cd Length: 75  Bit Score: 62.17  E-value: 1.19e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18400173   20 QVKDNDLPT-DSPYMATGTLEDYKLKAYGAEGHQEPTPGLGGGSTDAPTPSGDAPAATT 77
Cdd:pfam10714  3 ESKLDGLPMeSSPYLKYKDLEDYKRQGYGTQGHQEPKPGRGGGATDAPTLSGGGDSSSA 61
 
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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