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Conserved domains on  [gi|6522572|emb|CAB62016|]
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remorin-like protein [Arabidopsis thaliana]

Protein Classification

remorin family protein( domain architecture ID 11145301)

remorin family protein similar to remorins which are plant-specific plasma membrane-associated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 65-170 7.12e-33

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


:

Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 113.05  E-value: 7.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6522572     65 KRISLIKAWEEAEKSKVENKAQKKISSVGAWENSKKASVEAELKKIEEQLNKKKAHYTEQMKNKIAQIHKEAEEKRAMTE 144
Cdd:pfam03763   1 KRESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAE 80

                          90       100
                  ....*....|....*....|....*.
gi 6522572    145 AKRGEDVLKAEEMAAKYRATGTAPTK 170
Cdd:pfam03763  81 AKRGEEELKTEEKAAKIRATGKIPSK 106
Remorin_N pfam03766
Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 15-61 4.48e-05

Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich C-half and a more conserved N-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


:

Pssm-ID: 367646 [Multi-domain]  Cd Length: 51  Bit Score: 39.33  E-value: 4.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6522572     15 VASEPS---PPSKEEKSDDSKAIVLV-VAAKEPTEDKKVGSVHRDAVLVRL 61
Cdd:pfam03766   1 VAEEKAvipPPPPEEKPDDSKALAVVeKVEESAEEKPSGGSVDRDAVLARV 51
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 65-170 7.12e-33

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 113.05  E-value: 7.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6522572     65 KRISLIKAWEEAEKSKVENKAQKKISSVGAWENSKKASVEAELKKIEEQLNKKKAHYTEQMKNKIAQIHKEAEEKRAMTE 144
Cdd:pfam03763   1 KRESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAE 80

                          90       100
                  ....*....|....*....|....*.
gi 6522572    145 AKRGEDVLKAEEMAAKYRATGTAPTK 170
Cdd:pfam03763  81 AKRGEEELKTEEKAAKIRATGKIPSK 106
Remorin_N pfam03766
Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 15-61 4.48e-05

Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich C-half and a more conserved N-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 367646 [Multi-domain]  Cd Length: 51  Bit Score: 39.33  E-value: 4.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6522572     15 VASEPS---PPSKEEKSDDSKAIVLV-VAAKEPTEDKKVGSVHRDAVLVRL 61
Cdd:pfam03766   1 VAEEKAvipPPPPEEKPDDSKALAVVeKVEESAEEKPSGGSVDRDAVLARV 51
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 65-170 7.12e-33

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 113.05  E-value: 7.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6522572     65 KRISLIKAWEEAEKSKVENKAQKKISSVGAWENSKKASVEAELKKIEEQLNKKKAHYTEQMKNKIAQIHKEAEEKRAMTE 144
Cdd:pfam03763   1 KRESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAE 80

                          90       100
                  ....*....|....*....|....*.
gi 6522572    145 AKRGEDVLKAEEMAAKYRATGTAPTK 170
Cdd:pfam03763  81 AKRGEEELKTEEKAAKIRATGKIPSK 106
Remorin_N pfam03766
Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 15-61 4.48e-05

Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich C-half and a more conserved N-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 367646 [Multi-domain]  Cd Length: 51  Bit Score: 39.33  E-value: 4.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6522572     15 VASEPS---PPSKEEKSDDSKAIVLV-VAAKEPTEDKKVGSVHRDAVLVRL 61
Cdd:pfam03766   1 VAEEKAvipPPPPEEKPDDSKALAVVeKVEESAEEKPSGGSVDRDAVLARV 51
 
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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