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Conserved domains on  [gi|290542348|ref|NP_001166600|]
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lipoxygenase homology domain-containing protein 1 isoform 4 [Homo sapiens]

Protein Classification

phospholipase C( domain architecture ID 10109877)

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_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 124-244 9.05e-57

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: 183.53  E-value: 9.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 124 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 203
Cdd:cd01756    1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 290542348 204 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 244
Cdd:cd01756   80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1-114 1.10e-44

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: 151.94  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   1 MTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEWFLER 78
Cdd:cd01756    5 VTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFLDK 84

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 290542348  79 ILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 114
Cdd:cd01756   85 VEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 393-457 1.87e-28

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 cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 108.80  E-value: 1.87e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 290542348 393 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQK-MRNLFERGSTDRFFLETLELGELRK 457
Cdd:cd01756    1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnNKNKFERGQTDKFTVEAVDLGKLKK 66
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 257-358 2.43e-05

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 cd00113:

Pssm-ID: 412108  Cd Length: 116  Bit Score: 43.48  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 257 YEIVIETGN--GGETRENVWLILEGR-KNRSKEFLMENSSRqraFRKGTTDTFEFDSiyLGDIASLCVGHLAREDrfiPK 333
Cdd:cd00113    3 YTVTIKTGDkkGAGTDSNISLALYGEnGNSSDIPILDGPGS---FERGSTDTFQIDL--KLDIGDITKVYLRRDG---SG 74

                         90       100
                 ....*....|....*....|....*
gi 290542348 334 RELAWHVKTITITEMEYGNVYFFNC 358
Cdd:cd00113   75 LSDGWYCESITVQALGTKKVYTFPV 99
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 124-244 9.05e-57

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: 183.53  E-value: 9.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 124 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 203
Cdd:cd01756    1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 290542348 204 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 244
Cdd:cd01756   80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1-114 1.10e-44

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: 151.94  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   1 MTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEWFLER 78
Cdd:cd01756    5 VTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFLDK 84

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 290542348  79 ILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 114
Cdd:cd01756   85 VEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 393-457 1.87e-28

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: 108.80  E-value: 1.87e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 290542348 393 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQK-MRNLFERGSTDRFFLETLELGELRK 457
Cdd:cd01756    1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnNKNKFERGQTDKFTVEAVDLGKLKK 66
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 126-237 1.57e-21

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: 89.41  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348  126 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQsaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 205
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 290542348  206 LSYVDVKDNSRDE-TFHFQCDCWLSKSEGDGQT 237
Cdd:pfam01477  79 LKSITVEVPGETGgKYTFPCNSWVYGSKKYKET 111
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 5-108 5.43e-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: 65.15  E-value: 5.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348    5 TGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLERILL-K 82
Cdd:pfam01477   7 TGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEWFLKSITVeV 86

                          90       100
                  ....*....|....*....|....*..
gi 290542348   83 NMNTGDLTMFYYGDWLSQ-RKGKKTLV 108
Cdd:pfam01477  87 PGETGGKYTFPCNSWVYGsKKYKETRV 113
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
126-230 2.38e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.57  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   126 YTVAVKTSDILGAGTDANVFIIIFGENGDSGtLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKgiFPGWH 205
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGK-ESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEWF 79

                           90       100
                   ....*....|....*....|....*
gi 290542348   206 LSYVDVKDNSRDETFHFQCDCWLSK 230
Cdd:smart00308  80 LKSITVKDLPTGGKYHFPCNSWVYP 104
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 395-457 5.91e-08

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: 50.89  E-value: 5.91e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 290542348  395 YEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKmRNLFERGSTDRFFLET-LELGELRK 457
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLD-NPDFERGAEDSFEIDTdWDVGAILK 63
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
394-455 3.18e-06

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 45.71  E-value: 3.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 290542348   394 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRFFLET-LELGEL 455
Cdd:smart00308   2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVdEDFGEL 64
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 257-358 2.43e-05

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: 43.48  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 257 YEIVIETGN--GGETRENVWLILEGR-KNRSKEFLMENSSRqraFRKGTTDTFEFDSiyLGDIASLCVGHLAREDrfiPK 333
Cdd:cd00113    3 YTVTIKTGDkkGAGTDSNISLALYGEnGNSSDIPILDGPGS---FERGSTDTFQIDL--KLDIGDITKVYLRRDG---SG 74

                         90       100
                 ....*....|....*....|....*
gi 290542348 334 RELAWHVKTITITEMEYGNVYFFNC 358
Cdd:cd00113   75 LSDGWYCESITVQALGTKKVYTFPV 99
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
2-99 4.03e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 42.63  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348     2 TVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDK-KKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGlgSRPEWFLERI 79
Cdd:smart00308   6 TVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYlFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFLKSI 83

                           90       100
                   ....*....|....*....|
gi 290542348    80 LLKNMNTGDLTMFYYGDWLS 99
Cdd:smart00308  84 TVKDLPTGGKYHFPCNSWVY 103
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 124-244 9.05e-57

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: 183.53  E-value: 9.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 124 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 203
Cdd:cd01756    1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 290542348 204 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 244
Cdd:cd01756   80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1-114 1.10e-44

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: 151.94  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   1 MTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEWFLER 78
Cdd:cd01756    5 VTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFLDK 84

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 290542348  79 ILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 114
Cdd:cd01756   85 VEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1-109 1.62e-30

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: 113.97  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   1 MTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLERI 79
Cdd:cd00113    5 VTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGWYCESI 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 290542348  80 LLKNMNTGDLTMFYYGDWLSQRKGKKTLVC 109
Cdd:cd00113   85 TVQALGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 125-244 7.99e-30

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: 112.37  E-value: 7.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 125 SYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGW 204
Cdd:cd01752    2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDP-EKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 290542348 205 HLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 244
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 393-457 1.87e-28

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: 108.80  E-value: 1.87e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 290542348 393 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQK-MRNLFERGSTDRFFLETLELGELRK 457
Cdd:cd01756    1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnNKNKFERGQTDKFTVEAVDLGKLKK 66
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 126-237 1.57e-21

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: 89.41  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348  126 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQsaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 205
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 290542348  206 LSYVDVKDNSRDE-TFHFQCDCWLSKSEGDGQT 237
Cdd:pfam01477  79 LKSITVEVPGETGgKYTFPCNSWVYGSKKYKET 111
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 126-239 2.70e-20

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: 85.85  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 126 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLalKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 205
Cdd:cd00113    3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDI--PILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 290542348 206 LSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVR 239
Cdd:cd00113   81 CESITVQALGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 394-457 2.00e-15

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: 72.31  E-value: 2.00e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290542348 394 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRFFLETLE-LGELRK 457
Cdd:cd01752    2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFpLGELQS 66
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 2-107 4.64e-14

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: 68.46  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   2 TVWTGDVVGGGTDSNIFMTLYGINGSTEEMQL-DKKKARFEREQNDTFIMEildiAPF-----TKMRIRIDGLGSRPEWF 75
Cdd:cd01752    6 TVFTGWRRGAGTTAKVTITLYGAEGESEPHHLrDPEKPIFERGSVDSFLLT----TPFplgelQSIRLWHDNSGLSPSWY 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 290542348  76 LERILLKNMNTGDLTMFYYGDWLSQRKGKKTL 107
Cdd:cd01752   82 LSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTV 113
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 5-108 5.43e-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: 65.15  E-value: 5.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348    5 TGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLERILL-K 82
Cdd:pfam01477   7 TGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEWFLKSITVeV 86

                          90       100
                  ....*....|....*....|....*..
gi 290542348   83 NMNTGDLTMFYYGDWLSQ-RKGKKTLV 108
Cdd:pfam01477  87 PGETGGKYTFPCNSWVYGsKKYKETRV 113
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 126-232 1.53e-12

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: 64.48  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 126 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQS------ANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKG 199
Cdd:cd01754    3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAwgglmgAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 290542348 200 IFPGWHLSYVDVK---DNSRDETFHFQCDCWLSKSE 232
Cdd:cd01754   83 NHPGWYVNYVEVTqagQHAPCMQHLFAVEQWLATDE 118
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
126-230 2.38e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.57  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   126 YTVAVKTSDILGAGTDANVFIIIFGENGDSGtLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKgiFPGWH 205
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGK-ESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEWF 79

                           90       100
                   ....*....|....*....|....*
gi 290542348   206 LSYVDVKDNSRDETFHFQCDCWLSK 230
Cdd:smart00308  80 LKSITVKDLPTGGKYHFPCNSWVYP 104
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 128-237 2.62e-08

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 51.77  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 128 VAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNtdtfnfpdmlsLGHLCKLRVWHDNKGIFPGWHLS 207
Cdd:cd01757    6 VIVPSKKLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFDCQN-----------LGKLTTVQIGHDNSGLLAKWLVE 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 290542348 208 YVDVKDNSRDETFHFQCDCWLSKSEGDGQT 237
Cdd:cd01757   75 YVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 395-457 5.91e-08

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: 50.89  E-value: 5.91e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 290542348  395 YEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKmRNLFERGSTDRFFLET-LELGELRK 457
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLD-NPDFERGAEDSFEIDTdWDVGAILK 63
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 125-235 1.58e-07

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 49.61  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 125 SYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKqsaNWNK-FERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPG 203
Cdd:cd01753    2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLD---RPGYdFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 290542348 204 WHLSYVDVKDNSRDEtFHFQCDCWLsksEGDG 235
Cdd:cd01753   79 WFCNYITVTGPGGDE-YHFPCYRWI---EGYG 106
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 394-445 1.60e-06

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: 46.95  E-value: 1.60e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 290542348 394 KYEVIVTTGYEPGAGTDANVFVTIFGANgdtGKRELKQKMRNL--FERGSTDRF 445
Cdd:cd00113    2 RYTVTIKTGDKKGAGTDSNISLALYGEN---GNSSDIPILDGPgsFERGSTDTF 52
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
394-455 3.18e-06

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 45.71  E-value: 3.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 290542348   394 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRFFLET-LELGEL 455
Cdd:smart00308   2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVdEDFGEL 64
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 257-358 2.43e-05

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: 43.48  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 257 YEIVIETGN--GGETRENVWLILEGR-KNRSKEFLMENSSRqraFRKGTTDTFEFDSiyLGDIASLCVGHLAREDrfiPK 333
Cdd:cd00113    3 YTVTIKTGDkkGAGTDSNISLALYGEnGNSSDIPILDGPGS---FERGSTDTFQIDL--KLDIGDITKVYLRRDG---SG 74

                         90       100
                 ....*....|....*....|....*
gi 290542348 334 RELAWHVKTITITEMEYGNVYFFNC 358
Cdd:cd00113   75 LSDGWYCESITVQALGTKKVYTFPV 99
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 257-360 3.58e-05

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: 43.03  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348 257 YEIVIETG--NGGETRENVWLILEGRKNRSKEFLMENSSRQrAFRKGTTDTF----EFDsiyLGDIASLCVGHLAREDRf 330
Cdd:cd01752    3 YLVTVFTGwrRGAGTTAKVTITLYGAEGESEPHHLRDPEKP-IFERGSVDSFllttPFP---LGELQSIRLWHDNSGLS- 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 290542348 331 iPkrelAWHVKTITITEMEYGNVYFFNCDC 360
Cdd:cd01752   78 -P----SWYLSRVIVRDLQTGKKWFFLCND 102
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 393-455 3.94e-05

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 42.68  E-value: 3.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 290542348 393 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNlFERGSTDRFFLE-TLELGEL 455
Cdd:cd01753    1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD-FERGAVDEYKVKvPEDLGEL 63
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
2-99 4.03e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 42.63  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348     2 TVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDK-KKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGlgSRPEWFLERI 79
Cdd:smart00308   6 TVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYlFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFLKSI 83

                           90       100
                   ....*....|....*....|
gi 290542348    80 LLKNMNTGDLTMFYYGDWLS 99
Cdd:smart00308  84 TVKDLPTGGKYHFPCNSWVY 103
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 2-108 1.09e-04

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 41.53  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290542348   2 TVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLERIL 80
Cdd:cd01753    6 TVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFDAWFCNYIT 85

                         90       100
                 ....*....|....*....|....*...
gi 290542348  81 LKNMNtGDLTMFYYGDWLSqrkGKKTLV 108
Cdd:cd01753   86 VTGPG-GDEYHFPCYRWIE---GYGTLE 109
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 395-445 4.29e-04

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: 40.22  E-value: 4.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 290542348 395 YEVIVTTGYEPGAGTDANVFVTIFGANGDTGK-------RELKQKMRNLFERGSTDRF 445
Cdd:cd01754    3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRianleawGGLMGAGHDYFERGNLDRF 60
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 394-455 3.24e-03

Scavenger receptor protein. A subfamily of 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. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1.


Pssm-ID: 239228  Cd Length: 109  Bit Score: 37.06  E-value: 3.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290542348 394 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKmrnlFERGSTDRFFLETLELGEL 455
Cdd:cd02899    2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG----FYPGSLKRIRFRAADVGDI 59
 
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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