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Conserved domains on  [gi|15233068|ref|NP_191685|]
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Remorin family 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. ...
 102-206 1.35e-31

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: 111.13  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068   102 KRLSFVRAWEESEKSKAENKAEKKIADVHAWENSKKAAVEAQLKKIEEQLEKKKAEYAERMKNKVAAIHKEAEERRAMIE 181
Cdd:pfam03763   1 KRESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAE 80

                          90       100
                  ....*....|....*....|....*
gi 15233068   182 AKRGEDVLKAEETAAKYRATGIVPK 206
Cdd:pfam03763  81 AKRGEEELKTEEKAAKIRATGKIPS 105
Remorin_N pfam03766
Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 49-98 6.09e-08

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: 47.81  E-value: 6.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15233068    49 VAEEKIQNPPP--EQIFDDSKALTVVEKpVEEPAPAKPASASLDRDVKLADL 98
Cdd:pfam03766   1 VAEEKAVIPPPppEEKPDDSKALAVVEK-VEESAEEKPSGGSVDRDAVLARV 51
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 102-206 1.35e-31

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: 111.13  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068   102 KRLSFVRAWEESEKSKAENKAEKKIADVHAWENSKKAAVEAQLKKIEEQLEKKKAEYAERMKNKVAAIHKEAEERRAMIE 181
Cdd:pfam03763   1 KRESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAE 80

                          90       100
                  ....*....|....*....|....*
gi 15233068   182 AKRGEDVLKAEETAAKYRATGIVPK 206
Cdd:pfam03763  81 AKRGEEELKTEEKAAKIRATGKIPS 105
Remorin_N pfam03766
Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 49-98 6.09e-08

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: 47.81  E-value: 6.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15233068    49 VAEEKIQNPPP--EQIFDDSKALTVVEKpVEEPAPAKPASASLDRDVKLADL 98
Cdd:pfam03766   1 VAEEKAVIPPPppEEKPDDSKALAVVEK-VEESAEEKPSGGSVDRDAVLARV 51
PTZ00121 PTZ00121
MAEBL; Provisional
 2-197 3.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068     2 AEEQKIALESESPAKVTTPAPADTPAPAPAEIPAPAPAPTPADVTKDVAE--EKIQNPPPEQIFDDSKALTVVEKPVEEP 79
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068    80 APAKPASASLDRDVKLADLSKEKRLSFVRAWEESEKSKAENKAE---KKIADVHAWENSKKAAVEAQ-----LKKIEEQL 151
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeakKKAEEAKKADEAKKKAEEAKkaeeaKKKAEEAK 1470

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15233068   152 E----KKKAE---YAERMKNKVAAIHKEAEERRAMIEAKRGEDVLKAEETAAK 197
Cdd:PTZ00121 1471 KadeaKKKAEeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
 
Name Accession Description Interval E-value
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 102-206 1.35e-31

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: 111.13  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068   102 KRLSFVRAWEESEKSKAENKAEKKIADVHAWENSKKAAVEAQLKKIEEQLEKKKAEYAERMKNKVAAIHKEAEERRAMIE 181
Cdd:pfam03763   1 KRESKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIEEKLEKKRAEALEKMKNKLARIHKKAEEKRASAE 80

                          90       100
                  ....*....|....*....|....*
gi 15233068   182 AKRGEDVLKAEETAAKYRATGIVPK 206
Cdd:pfam03763  81 AKRGEEELKTEEKAAKIRATGKIPS 105
Remorin_N pfam03766
Remorin, N-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 49-98 6.09e-08

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: 47.81  E-value: 6.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15233068    49 VAEEKIQNPPP--EQIFDDSKALTVVEKpVEEPAPAKPASASLDRDVKLADL 98
Cdd:pfam03766   1 VAEEKAVIPPPppEEKPDDSKALAVVEK-VEESAEEKPSGGSVDRDAVLARV 51
PTZ00121 PTZ00121
MAEBL; Provisional
 2-197 3.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068     2 AEEQKIALESESPAKVTTPAPADTPAPAPAEIPAPAPAPTPADVTKDVAE--EKIQNPPPEQIFDDSKALTVVEKPVEEP 79
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068    80 APAKPASASLDRDVKLADLSKEKRLSFVRAWEESEKSKAENKAE---KKIADVHAWENSKKAAVEAQ-----LKKIEEQL 151
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeakKKAEEAKKADEAKKKAEEAKkaeeaKKKAEEAK 1470

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15233068   152 E----KKKAE---YAERMKNKVAAIHKEAEERRAMIEAKRGEDVLKAEETAAK 197
Cdd:PTZ00121 1471 KadeaKKKAEeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
PTZ00121 PTZ00121
MAEBL; Provisional
 5-193 7.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.04  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068     5 QKIALESESPAKVTTPAPADTPAPAPAEIPAPAPAPTPADVTKDVAEEKIQNPPPEQIFDDSKALTVVEKPVEEPAPAKP 84
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233068    85 ASASLDRDVKLADLSK--EKRLSFVRAWEESEKSKAENKAEKKIADVHAWENSKKAAVEAQLKKIE---EQLEKKKAEYA 159
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEA 1515

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15233068   160 ERMKNKVAAIH-KEAEERRAMIEAKRGEDVLKAEE 193
Cdd:PTZ00121 1516 KKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADE 1550
 
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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