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Conserved domains on  [gi|339515817|gb|AEJ82289|]
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casparian strip protein 3, partial [Cloning vector p35S::CASP3:GFP]

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 ...
56-205 2.19e-38

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: 130.13  E-value: 2.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339515817   56 KRGVAIFDFVLRLIAAITAMAAAAKMATTEETLPFFtqFLQFQADYTDLPTMSSFVIVNSIVGGYLTLSLPFSIVCILR- 134
Cdd:pfam04535   1 GRPLRLAELVLRLAAFVLALAAAVVMGTNKQTKSFF--FIQFKAKFSDYPAFRYLVVANAIAAGYSLLQLVLSVYSLSRk 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339515817  135 -PLAVPPRLFLILCDTVMMGLTLMAASASAAIVYLAHNGNSSSNWLPVCQQFGDFCQGTSGAVVASFIAATL 205
Cdd:pfam04535  79 rLRSAALAWLLFILDQVMAYLLLSAASAAAAIVYLARNGNSHAQWLKICNQFGRFCNRVAASVALSFLAFLL 150
 
Name Accession Description Interval E-value
CASP_dom pfam04535
Casparian strip membrane protein domain; This domain is found mainly in plant proteins known ...
56-205 2.19e-38

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: 130.13  E-value: 2.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339515817   56 KRGVAIFDFVLRLIAAITAMAAAAKMATTEETLPFFtqFLQFQADYTDLPTMSSFVIVNSIVGGYLTLSLPFSIVCILR- 134
Cdd:pfam04535   1 GRPLRLAELVLRLAAFVLALAAAVVMGTNKQTKSFF--FIQFKAKFSDYPAFRYLVVANAIAAGYSLLQLVLSVYSLSRk 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339515817  135 -PLAVPPRLFLILCDTVMMGLTLMAASASAAIVYLAHNGNSSSNWLPVCQQFGDFCQGTSGAVVASFIAATL 205
Cdd:pfam04535  79 rLRSAALAWLLFILDQVMAYLLLSAASAAAAIVYLARNGNSHAQWLKICNQFGRFCNRVAASVALSFLAFLL 150
A_tha_TIGR01569 TIGR01569
plant integral membrane protein TIGR01569; This model describes a region of ~160 residues ...
64-217 1.04e-33

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: 118.27  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339515817   64 FVLRLIAAITAMAAAAKMATTEETLPFFTQFLQFQADYTDLPTMSSFVIVNSIVGGYLTLSLPFSIVCILRPLAVPPRLF 143
Cdd:TIGR01569   1 LILRVLAFSATLAAAIVMGTNRETKVVFVQLITFKAKFSDLPAFVYFVVANAIACGYSLLSLVVSIFGLLKRRVFFKLIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339515817  144 LILCDTVMMGLTLMAASASAAIVYLAHNGNSSSNWLPVCQQFGDFCQGTSGAVVASFIAATLLMFLVILSAFAL 217
Cdd:TIGR01569  81 LFFLDLVMLALLSSGTSAAAAVAYVGKLGNKEAGWLKICGVFGKFCDRIAGSLALSLFAVILLVLLSILSAISL 154
 
Name Accession Description Interval E-value
CASP_dom pfam04535
Casparian strip membrane protein domain; This domain is found mainly in plant proteins known ...
56-205 2.19e-38

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: 130.13  E-value: 2.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339515817   56 KRGVAIFDFVLRLIAAITAMAAAAKMATTEETLPFFtqFLQFQADYTDLPTMSSFVIVNSIVGGYLTLSLPFSIVCILR- 134
Cdd:pfam04535   1 GRPLRLAELVLRLAAFVLALAAAVVMGTNKQTKSFF--FIQFKAKFSDYPAFRYLVVANAIAAGYSLLQLVLSVYSLSRk 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339515817  135 -PLAVPPRLFLILCDTVMMGLTLMAASASAAIVYLAHNGNSSSNWLPVCQQFGDFCQGTSGAVVASFIAATL 205
Cdd:pfam04535  79 rLRSAALAWLLFILDQVMAYLLLSAASAAAAIVYLARNGNSHAQWLKICNQFGRFCNRVAASVALSFLAFLL 150
A_tha_TIGR01569 TIGR01569
plant integral membrane protein TIGR01569; This model describes a region of ~160 residues ...
64-217 1.04e-33

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: 118.27  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339515817   64 FVLRLIAAITAMAAAAKMATTEETLPFFTQFLQFQADYTDLPTMSSFVIVNSIVGGYLTLSLPFSIVCILRPLAVPPRLF 143
Cdd:TIGR01569   1 LILRVLAFSATLAAAIVMGTNRETKVVFVQLITFKAKFSDLPAFVYFVVANAIACGYSLLSLVVSIFGLLKRRVFFKLIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339515817  144 LILCDTVMMGLTLMAASASAAIVYLAHNGNSSSNWLPVCQQFGDFCQGTSGAVVASFIAATLLMFLVILSAFAL 217
Cdd:TIGR01569  81 LFFLDLVMLALLSSGTSAAAAVAYVGKLGNKEAGWLKICGVFGKFCDRIAGSLALSLFAVILLVLLSILSAISL 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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