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Conserved domains on  [gi|1901122912|emb|CAD5330420|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

phospholipase C( domain architecture ID 10109873)

phospholipase C catayzes the hydroysis of a phosphatidylcholine to form 1,2-diacyl-sn-glycerol and phosphocholine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 29-157 1.23e-86

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238852  Cd Length: 129  Bit Score: 250.15  E-value: 1.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  29 CVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDG 108
Cdd:cd01754     1 CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1901122912 109 SGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNN 157
Cdd:cd01754    81 TGNHPGWYVNYVEVTQAGQHAPCMQHLFAVEQWLATDESPYMLTAVRNN 129
 
Name Accession Description Interval E-value
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 29-157 1.23e-86

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 250.15  E-value: 1.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  29 CVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDG 108
Cdd:cd01754     1 CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1901122912 109 SGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNN 157
Cdd:cd01754    81 TGNHPGWYVNYVEVTQAGQHAPCMQHLFAVEQWLATDESPYMLTAVRNN 129
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 31-150 1.25e-18

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 77.09  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  31 YTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQawaglmgpDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSG 110
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--------DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1901122912 111 DHHGWYVNYVEITTAGVHAqcSTQDFEIEQWLATDTSPYE 150
Cdd:pfam01477  73 LSDEWFLKSITVEVPGETG--GKYTFPCNSWVYGSKKYKE 110
 
Name Accession Description Interval E-value
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 29-157 1.23e-86

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 250.15  E-value: 1.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  29 CVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDG 108
Cdd:cd01754     1 CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1901122912 109 SGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNN 157
Cdd:cd01754    81 TGNHPGWYVNYVEVTQAGQHAPCMQHLFAVEQWLATDESPYMLTAVRNN 129
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 31-150 1.25e-18

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 77.09  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  31 YTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQawaglmgpDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSG 110
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--------DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1901122912 111 DHHGWYVNYVEITTAGVHAqcSTQDFEIEQWLATDTSPYE 150
Cdd:pfam01477  73 LSDEWFLKSITVEVPGETG--GKYTFPCNSWVYGSKKYKE 110
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 29-152 6.51e-14

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 64.67  E-value: 6.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  29 CVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGlmgpdynyFERGNLDIFSGRAPCLPSPICALNLTSDG 108
Cdd:cd00113     1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGS--------FERGSTDTFQIDLKLDIGDITKVYLRRDG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1901122912 109 SGDHHGWYVNYVEITTAGVHAQCstqDFEIEQWL---ATDTSPYELT 152
Cdd:cd00113    73 SGLSDGWYCESITVQALGTKKVY---TFPVNRWVlggKWYTSVRSLK 116
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 30-145 3.28e-13

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 62.96  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  30 VYTFYLRTGSIWKAGTDSIISARIYDKDGDyIGIKNLQAWAGLmgpdyNYFERGNLDIFSGRAPCLpSPICALNLTSDGS 109
Cdd:cd01756     2 TYEVTVKTGDVKGAGTDANVFITLYGENGD-TGKRKLKKSNNK-----NKFERGQTDKFTVEAVDL-GKLKKIRIGHDNS 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1901122912 110 GDHHGWYVNYVEITTAGVHaqcSTQDFEIEQWLATD 145
Cdd:cd01756    75 GLGAGWFLDKVEIREPGTG---DEYTFPCNRWLDKD 107
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 37-145 1.11e-04

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 39.95  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122912  37 TGSIWKAGTDSIISARIYDKDGDYiGIKNLQawaglmGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSGDHHGWY 116
Cdd:cd01752     9 TGWRRGAGTTAKVTITLYGAEGES-EPHHLR------DPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSWY 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1901122912 117 VNYVEITtagvhaQCSTQD---FEIEQWLATD 145
Cdd:cd01752    82 LSRVIVR------DLQTGKkwfFLCNDWLSVE 107
 
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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