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Conserved domains on  [gi|15240435|ref|NP_200309|]
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Uncharacterized protein family (UPF0497) [Arabidopsis thaliana]

Protein Classification

CASP domain-containing protein( domain architecture ID 10517609)

CASP (Casparian strip membrane protein) domain-containing protein similar to CASPs, which are four-membrane-span proteins that mediate the deposition of Casparian strips in the endodermis by recruiting the lignin polymerization machinery

Gene Ontology:  GO:0016020
PubMed:  21593871

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CASP_dom pfam04535
Casparian strip membrane protein domain; This domain is found mainly in plant proteins known ...
 26-160 4.32e-33

Casparian strip membrane protein domain; This domain is found mainly in plant proteins known as Casparian strip membrane proteins (CASPs) and CASP-like proteins (CASPLs). CASPs are four-membrane-span proteins that mediate the deposition of Casparian strips in the endodermis by recruiting the lignin polymerization machinery. Interestingly, the CASP first extracellular loop was found conserved in euphyllophytes but absent in plants lacking Casparian strips.


:

Pssm-ID: 367980  Cd Length: 150  Bit Score: 115.49  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240435    26 PMSLKIIDSCLRLSVVPLSVATIWLTVTNHESNPDY---GNLEYNSIMGLKYMVGVSAISAIYALLSTVSSWV------T 96
Cdd:pfam04535   1 GRPLRLAELVLRLAAFVLALAAAVVMGTNKQTKSFFfiqFKAKFSDYPAFRYLVVANAIAAGYSLLQLVLSVYslsrkrL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240435    97 CLVSKAWLFFIPDQVLAYVMTTSVAGATEIVYLLNKGDKIVTWSEMCSSYPHYCSKLTIALGLH 160
Cdd:pfam04535  81 RSAALAWLLFILDQVMAYLLLSAASAAAAIVYLARNGNSHAQWLKICNQFGRFCNRVAASVALS 144
 
Name Accession Description Interval E-value
CASP_dom pfam04535
Casparian strip membrane protein domain; This domain is found mainly in plant proteins known ...
 26-160 4.32e-33

Casparian strip membrane protein domain; This domain is found mainly in plant proteins known as Casparian strip membrane proteins (CASPs) and CASP-like proteins (CASPLs). CASPs are four-membrane-span proteins that mediate the deposition of Casparian strips in the endodermis by recruiting the lignin polymerization machinery. Interestingly, the CASP first extracellular loop was found conserved in euphyllophytes but absent in plants lacking Casparian strips.


Pssm-ID: 367980  Cd Length: 150  Bit Score: 115.49  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240435    26 PMSLKIIDSCLRLSVVPLSVATIWLTVTNHESNPDY---GNLEYNSIMGLKYMVGVSAISAIYALLSTVSSWV------T 96
Cdd:pfam04535   1 GRPLRLAELVLRLAAFVLALAAAVVMGTNKQTKSFFfiqFKAKFSDYPAFRYLVVANAIAAGYSLLQLVLSVYslsrkrL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240435    97 CLVSKAWLFFIPDQVLAYVMTTSVAGATEIVYLLNKGDKIVTWSEMCSSYPHYCSKLTIALGLH 160
Cdd:pfam04535  81 RSAALAWLLFILDQVMAYLLLSAASAAAAIVYLARNGNSHAQWLKICNQFGRFCNRVAASVALS 144
A_tha_TIGR01569 TIGR01569
plant integral membrane protein TIGR01569; This model describes a region of ~160 residues ...
 36-178 1.85e-12

plant integral membrane protein TIGR01569; This model describes a region of ~160 residues found exclusively in plant proteins, generally as the near complete length of the protein. At least 24 different members are found in Arabidopsis thaliana. Members have four predicted transmembrane regions, the last of which is preceded by an invariant CXXXXX[FY]C motif. The family is not functionally characterized.


Pssm-ID: 273695  Cd Length: 154  Bit Score: 62.03  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240435    36 LRLSVVPLSVATIWLTVTNHESNPDYGNL-----EYNSIMGLKYMVGVSAISAIYALLSTVSSWV----TCLVSKAWLFF 106
Cdd:TIGR01569   3 LRVLAFSATLAAAIVMGTNRETKVVFVQLitfkaKFSDLPAFVYFVVANAIACGYSLLSLVVSIFgllkRRVFFKLIALF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240435   107 IPDQVLAYVMTTSVAGATEIVYLLNKGDKIVTWSEMCSSYPHYCSKLTIALGLHVFVLFFFLFLSVISAYRA 178
Cdd:TIGR01569  83 FLDLVMLALLSSGTSAAAAVAYVGKLGNKEAGWLKICGVFGKFCDRIAGSLALSLFAVILLVLLSILSAISL 154
 
Name Accession Description Interval E-value
CASP_dom pfam04535
Casparian strip membrane protein domain; This domain is found mainly in plant proteins known ...
 26-160 4.32e-33

Casparian strip membrane protein domain; This domain is found mainly in plant proteins known as Casparian strip membrane proteins (CASPs) and CASP-like proteins (CASPLs). CASPs are four-membrane-span proteins that mediate the deposition of Casparian strips in the endodermis by recruiting the lignin polymerization machinery. Interestingly, the CASP first extracellular loop was found conserved in euphyllophytes but absent in plants lacking Casparian strips.


Pssm-ID: 367980  Cd Length: 150  Bit Score: 115.49  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240435    26 PMSLKIIDSCLRLSVVPLSVATIWLTVTNHESNPDY---GNLEYNSIMGLKYMVGVSAISAIYALLSTVSSWV------T 96
Cdd:pfam04535   1 GRPLRLAELVLRLAAFVLALAAAVVMGTNKQTKSFFfiqFKAKFSDYPAFRYLVVANAIAAGYSLLQLVLSVYslsrkrL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240435    97 CLVSKAWLFFIPDQVLAYVMTTSVAGATEIVYLLNKGDKIVTWSEMCSSYPHYCSKLTIALGLH 160
Cdd:pfam04535  81 RSAALAWLLFILDQVMAYLLLSAASAAAAIVYLARNGNSHAQWLKICNQFGRFCNRVAASVALS 144
A_tha_TIGR01569 TIGR01569
plant integral membrane protein TIGR01569; This model describes a region of ~160 residues ...
 36-178 1.85e-12

plant integral membrane protein TIGR01569; This model describes a region of ~160 residues found exclusively in plant proteins, generally as the near complete length of the protein. At least 24 different members are found in Arabidopsis thaliana. Members have four predicted transmembrane regions, the last of which is preceded by an invariant CXXXXX[FY]C motif. The family is not functionally characterized.


Pssm-ID: 273695  Cd Length: 154  Bit Score: 62.03  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240435    36 LRLSVVPLSVATIWLTVTNHESNPDYGNL-----EYNSIMGLKYMVGVSAISAIYALLSTVSSWV----TCLVSKAWLFF 106
Cdd:TIGR01569   3 LRVLAFSATLAAAIVMGTNRETKVVFVQLitfkaKFSDLPAFVYFVVANAIACGYSLLSLVVSIFgllkRRVFFKLIALF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240435   107 IPDQVLAYVMTTSVAGATEIVYLLNKGDKIVTWSEMCSSYPHYCSKLTIALGLHVFVLFFFLFLSVISAYRA 178
Cdd:TIGR01569  83 FLDLVMLALLSSGTSAAAAVAYVGKLGNKEAGWLKICGVFGKFCDRIAGSLALSLFAVILLVLLSILSAISL 154
 
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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