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Conserved domains on  [gi|939630223|ref|NP_001104126|]
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polycystine-related-Y [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
1019-1111 5.39e-09

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.


The actual alignment was detected with superfamily member cd01752:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 55.36  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223 1019 GGRYNAGTSANIIFAFKFFNQTRDIIVYQDPVFRTFKRNSTISLRLQNKHfciPTGI--AMR--HDNSGVYPHFFCRNVV 1094
Cdd:cd01752    10 GWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPF---PLGElqSIRlwHDNSGLSPSWYLSRVI 86
                          90
                  ....*....|....*..
gi 939630223 1095 VCDLQTNEGQLFSIQQW 1111
Cdd:cd01752    87 VRDLQTGKKWFFLCNDW 103
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor ...
217-476 3.04e-07

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor for egg jelly. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


The actual alignment was detected with superfamily member pfam02010:

Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 54.43  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   217 IPAYSQPNNQTLRVMLLIRStfDPLRTATTKQSIVFSSSRQLInVNIACVSNCNGNKYTIQMPIHLKGQCLRCQNKKISK 296
Cdd:pfam02010  164 IPASTLQANVTYTFKLTVSK--GSRNSASTTQTILVVDGNPPI-IILSCISNCNRKNNPVDRLVLLASTCLNCSSDLSDV 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   297 WI-WrvegLPVEGASKRLIFDVKETKK--RLLGIHLNVEAvNRYNSKLTYYGTSWVF-------------LEKNMGPADT 360
Cdd:pfam02010  241 TYrW----LSLGSENTSLVLDQLNSQTstGRSGPYLVIKA-GVLQSGVSYRFTLIVTvypglvsglasisFITNAPPTGG 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   361 MCTISPRVGNAHETQFLLHCNQSQARFKPLQYCIGV--------ENFLVDECKSDEDIQVRLPP--TEH-----VVVMIC 425
Cdd:pfam02010  316 TCSVTPTEGTALETKFTVTCQGWTDDDLPLTYQFGDisfreaseEWFLLYEGSSQISISTFLPPglPANdyqvtVVVVVY 395
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 939630223   426 DHFSVCDDVTVTVEVR-------RLEMDDSDNTVKEALslarhwFEYADWQKAFLLLY 476
Cdd:pfam02010  396 DSLGAATSVSLTITVTppsssdeLLYFLLGTTSDLSAL------LQSGDPQQAAQLIL 447
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1019-1111 5.39e-09

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: 55.36  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223 1019 GGRYNAGTSANIIFAFKFFNQTRDIIVYQDPVFRTFKRNSTISLRLQNKHfciPTGI--AMR--HDNSGVYPHFFCRNVV 1094
Cdd:cd01752    10 GWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPF---PLGElqSIRlwHDNSGLSPSWYLSRVI 86
                          90
                  ....*....|....*..
gi 939630223 1095 VCDLQTNEGQLFSIQQW 1111
Cdd:cd01752    87 VRDLQTGKKWFFLCNDW 103
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor ...
217-476 3.04e-07

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor for egg jelly. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 54.43  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   217 IPAYSQPNNQTLRVMLLIRStfDPLRTATTKQSIVFSSSRQLInVNIACVSNCNGNKYTIQMPIHLKGQCLRCQNKKISK 296
Cdd:pfam02010  164 IPASTLQANVTYTFKLTVSK--GSRNSASTTQTILVVDGNPPI-IILSCISNCNRKNNPVDRLVLLASTCLNCSSDLSDV 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   297 WI-WrvegLPVEGASKRLIFDVKETKK--RLLGIHLNVEAvNRYNSKLTYYGTSWVF-------------LEKNMGPADT 360
Cdd:pfam02010  241 TYrW----LSLGSENTSLVLDQLNSQTstGRSGPYLVIKA-GVLQSGVSYRFTLIVTvypglvsglasisFITNAPPTGG 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   361 MCTISPRVGNAHETQFLLHCNQSQARFKPLQYCIGV--------ENFLVDECKSDEDIQVRLPP--TEH-----VVVMIC 425
Cdd:pfam02010  316 TCSVTPTEGTALETKFTVTCQGWTDDDLPLTYQFGDisfreaseEWFLLYEGSSQISISTFLPPglPANdyqvtVVVVVY 395
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 939630223   426 DHFSVCDDVTVTVEVR-------RLEMDDSDNTVKEALslarhwFEYADWQKAFLLLY 476
Cdd:pfam02010  396 DSLGAATSVSLTITVTppsssdeLLYFLLGTTSDLSAL------LQSGDPQQAAQLIL 447
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
1017-1124 1.26e-06

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: 48.58  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223  1017 TFGGRYNAGTSANIIFAFKFFN-QTRDIIVYQDPvfRTFKRNSTISLRLqnkHFCIPTG----IAMRHDNSGVYPHFFCR 1091
Cdd:pfam01477    6 VTGDELGAGTDADVYISLYGKVgESAQLEITLDN--PDFERGAEDSFEI---DTDWDVGailkINLHWDNNGLSDEWFLK 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 939630223  1092 NVVVCDLQTNEGQL-FSIQQWIKCYTVYKTVTSF 1124
Cdd:pfam01477   81 SITVEVPGETGGKYtFPCNSWVYGSKKYKETRVF 114
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
1019-1111 5.39e-09

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: 55.36  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223 1019 GGRYNAGTSANIIFAFKFFNQTRDIIVYQDPVFRTFKRNSTISLRLQNKHfciPTGI--AMR--HDNSGVYPHFFCRNVV 1094
Cdd:cd01752    10 GWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPF---PLGElqSIRlwHDNSGLSPSWYLSRVI 86
                          90
                  ....*....|....*..
gi 939630223 1095 VCDLQTNEGQLFSIQQW 1111
Cdd:cd01752    87 VRDLQTGKKWFFLCNDW 103
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor ...
217-476 3.04e-07

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1 and the sperm receptor for egg jelly. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 54.43  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   217 IPAYSQPNNQTLRVMLLIRStfDPLRTATTKQSIVFSSSRQLInVNIACVSNCNGNKYTIQMPIHLKGQCLRCQNKKISK 296
Cdd:pfam02010  164 IPASTLQANVTYTFKLTVSK--GSRNSASTTQTILVVDGNPPI-IILSCISNCNRKNNPVDRLVLLASTCLNCSSDLSDV 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   297 WI-WrvegLPVEGASKRLIFDVKETKK--RLLGIHLNVEAvNRYNSKLTYYGTSWVF-------------LEKNMGPADT 360
Cdd:pfam02010  241 TYrW----LSLGSENTSLVLDQLNSQTstGRSGPYLVIKA-GVLQSGVSYRFTLIVTvypglvsglasisFITNAPPTGG 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223   361 MCTISPRVGNAHETQFLLHCNQSQARFKPLQYCIGV--------ENFLVDECKSDEDIQVRLPP--TEH-----VVVMIC 425
Cdd:pfam02010  316 TCSVTPTEGTALETKFTVTCQGWTDDDLPLTYQFGDisfreaseEWFLLYEGSSQISISTFLPPglPANdyqvtVVVVVY 395
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 939630223   426 DHFSVCDDVTVTVEVR-------RLEMDDSDNTVKEALslarhwFEYADWQKAFLLLY 476
Cdd:pfam02010  396 DSLGAATSVSLTITVTppsssdeLLYFLLGTTSDLSAL------LQSGDPQQAAQLIL 447
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
1017-1124 7.76e-07

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: 48.87  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223 1017 TFGGRYNAGTSANIIFAFKFFNQTRDIIVYQDPVFRtFKRNSTISLRLQNK-HFCIPTGIAMRHDNSGVYPHFFCRNVVV 1095
Cdd:cd00113     8 KTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGS-FERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGWYCESITV 86
                          90       100
                  ....*....|....*....|....*....
gi 939630223 1096 CDLQTNEGQLFSIQQWIKCYTVYKTVTSF 1124
Cdd:cd00113    87 QALGTKKVYTFPVNRWVLGGKWYTSVRSL 115
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
1017-1124 1.26e-06

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: 48.58  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939630223  1017 TFGGRYNAGTSANIIFAFKFFN-QTRDIIVYQDPvfRTFKRNSTISLRLqnkHFCIPTG----IAMRHDNSGVYPHFFCR 1091
Cdd:pfam01477    6 VTGDELGAGTDADVYISLYGKVgESAQLEITLDN--PDFERGAEDSFEI---DTDWDVGailkINLHWDNNGLSDEWFLK 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 939630223  1092 NVVVCDLQTNEGQL-FSIQQWIKCYTVYKTVTSF 1124
Cdd:pfam01477   81 SITVEVPGETGGKYtFPCNSWVYGSKKYKETRVF 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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