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Conserved domains on  [gi|51535090|dbj|BAD37679|]
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putative dehydration stress-induced protein [Oryza sativa Japonica Group]

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 ...
 36-164 2.00e-83

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: 241.68  E-value: 2.00e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090  36 CVYTVFVRTGSAWKGGTDSTIGVEFAGADGRGVRIADLERWGGLMGAGHDYYERGNLDVFSGRGPCLPAAPCWMNLTSDG 115
Cdd:cd01754   1 CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 51535090 116 AGAHHGWYCNYVEVTATGPHRGCAQRRFDVEQWLATDASPYRLTAVRDQ 164
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 ...
 36-164 2.00e-83

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: 241.68  E-value: 2.00e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090  36 CVYTVFVRTGSAWKGGTDSTIGVEFAGADGRGVRIADLERWGGLMGAGHDYYERGNLDVFSGRGPCLPAAPCWMNLTSDG 115
Cdd:cd01754   1 CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 51535090 116 AGAHHGWYCNYVEVTATGPHRGCAQRRFDVEQWLATDASPYRLTAVRDQ 164
Cdd:cd01754  81 TGNHPGWYVNYVEVTQAGQHAPCMQHLFAVEQWLATDESPYMLTAVRNN 129
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 38-156 3.76e-13

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: 62.45  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090    38 YTVFVRTGSAWKGGTDSTIGVEFAGADGRGvriADLERWgglmgAGHDYYERGNLDVFSGRGPCLPAAPCWMNLTSDGAG 117
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGES---AQLEIT-----LDNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNG 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 51535090   118 AHHGWYCNYVEVTATGPHRGCAQrrFDVEQWLATDASPY 156
Cdd:pfam01477  73 LSDEWFLKSITVEVPGETGGKYT--FPCNSWVYGSKKYK 109
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
38-149 2.07e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 38.78  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090     38 YTVFVRTGSAWKGGTDSTIGVEFAGADGR-GVRIAD-LERWGGLMGAGHDYYergnLDVFSGRGPclPAApcwMNLTSDg 115
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDgKESKLDyLFKGIFARGSTYEFT----FDVDEDFGE--LGA---VKIKNE- 72

                           90       100       110
                   ....*....|....*....|....*....|....
gi 51535090    116 aGAHHGWYCNYVEVTATGPHRGCaqrRFDVEQWL 149
Cdd:smart00308  73 -HRHPEWFLKSITVKDLPTGGKY---HFPCNSWV 102
 
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 ...
 36-164 2.00e-83

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: 241.68  E-value: 2.00e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090  36 CVYTVFVRTGSAWKGGTDSTIGVEFAGADGRGVRIADLERWGGLMGAGHDYYERGNLDVFSGRGPCLPAAPCWMNLTSDG 115
Cdd:cd01754   1 CVYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 51535090 116 AGAHHGWYCNYVEVTATGPHRGCAQRRFDVEQWLATDASPYRLTAVRDQ 164
Cdd:cd01754  81 TGNHPGWYVNYVEVTQAGQHAPCMQHLFAVEQWLATDESPYMLTAVRNN 129
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 36-159 5.92e-17

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: 72.37  E-value: 5.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090  36 CVYTVFVRTGSAWKGGTDSTIGVEFAGADGRGVRIADLErwgglmgaGHDYYERGNLDVFSGRGPCLPAAPCWMNLTSDG 115
Cdd:cd00113   1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILD--------GPGSFERGSTDTFQIDLKLDIGDITKVYLRRDG 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51535090 116 AGAHHGWYCNYVEVTATGPHRGCaqrRFDVEQWL---ATDASPYRLT 159
Cdd:cd00113  73 SGLSDGWYCESITVQALGTKKVY---TFPVNRWVlggKWYTSVRSLK 116
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 38-156 3.76e-13

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: 62.45  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090    38 YTVFVRTGSAWKGGTDSTIGVEFAGADGRGvriADLERWgglmgAGHDYYERGNLDVFSGRGPCLPAAPCWMNLTSDGAG 117
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGES---AQLEIT-----LDNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNG 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 51535090   118 AHHGWYCNYVEVTATGPHRGCAQrrFDVEQWLATDASPY 156
Cdd:pfam01477  73 LSDEWFLKSITVEVPGETGGKYT--FPCNSWVYGSKKYK 109
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 37-152 1.82e-06

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: 44.85  E-value: 1.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090  37 VYTVFVRTGSAWKGGTDSTIGVEFAGADGR-GVRIadLERWGGlmgagHDYYERGNLDVFSgrgpcLPAAP----CWMNL 111
Cdd:cd01756   2 TYEVTVKTGDVKGAGTDANVFITLYGENGDtGKRK--LKKSNN-----KNKFERGQTDKFT-----VEAVDlgklKKIRI 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 51535090 112 TSDGAGAHHGWYCNYVEVTATGPHRGCaqrRFDVEQWLATD 152
Cdd:cd01756  70 GHDNSGLGAGWFLDKVEIREPGTGDEY---TFPCNRWLDKD 107
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
38-149 2.07e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 38.78  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090     38 YTVFVRTGSAWKGGTDSTIGVEFAGADGR-GVRIAD-LERWGGLMGAGHDYYergnLDVFSGRGPclPAApcwMNLTSDg 115
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDgKESKLDyLFKGIFARGSTYEFT----FDVDEDFGE--LGA---VKIKNE- 72

                           90       100       110
                   ....*....|....*....|....*....|....
gi 51535090    116 aGAHHGWYCNYVEVTATGPHRGCaqrRFDVEQWL 149
Cdd:smart00308  73 -HRHPEWFLKSITVKDLPTGGKY---HFPCNSWV 102
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 38-152 2.16e-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: 39.18  E-value: 2.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51535090  38 YTVFVRTGSAWKGGTDSTIGVEFAGADGR-GVRIadlerwggLMGAGHDYYERGNLDVFsgrgpcLPAAPC------WMN 110
Cdd:cd01752   3 YLVTVFTGWRRGAGTTAKVTITLYGAEGEsEPHH--------LRDPEKPIFERGSVDSF------LLTTPFplgelqSIR 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51535090 111 LTSDGAGAHHGWYCNYVEV----TATGPHrgcaqrrFDVEQWLATD 152
Cdd:cd01752  69 LWHDNSGLSPSWYLSRVIVrdlqTGKKWF-------FLCNDWLSVE 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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