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Conserved domains on  [gi|224458288|ref|NP_001138944|]
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lipoxygenase homology domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

PLAT_repeat and PLAT domain-containing protein( domain architecture ID 10205340)

protein containing domains PLAT_repeat, and PLAT

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 ...
 64-184 7.44e-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: 192.00  E-value: 7.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   64 TTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSkTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPG 143
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  144 WFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 184
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 349-469 8.35e-55

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: 186.22  E-value: 8.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  349 VLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCAD 428
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNK-NKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  429 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEK 469
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 774-894 3.08e-54

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: 184.30  E-value: 3.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  774 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 853
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  854 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 894
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 195-321 1.60e-46

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: 162.34  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  195 VPYEITLYTSDVFAAGTDANIFIIIYGcDAVCTQQKYLCTNKREQKqfFERKSASRFIVELEDVGEiIEKIRIGHNNTGM 274
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYG-ENGDTGKRKLKKSNNKNK--FERGQTDKFTVEAVDLGK-LKKIRIGHDNSGL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 224458288  275 NPGWHCSHVDIRRLLPDkdgaETLTFPCDRWLATSEDDKKTIRELVP 321
Cdd:cd01756    77 GAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 647-764 1.36e-45

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: 159.64  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  647 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEW 724
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 224458288  725 FLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 764
Cdd:cd01756    81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1043-1102 4.70e-25

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: 101.09  E-value: 4.70e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224458288 1043 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQK-MRNLFERGSTDRFFLETLEL 1102
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnNKNKFERGQTDKFTVEAVDL 61
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 518-633 1.42e-11

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: 62.68  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwLDYPrGKRGFSRGSVEEFYVAGL-DVGIIKKIELGHDGASPESCW 596
Cdd:cd01752     3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHH-LRDP-EKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224458288  597 -----LVEELclavPTQGTKYMLnCNCWLAKDRGDGITSRVF 633
Cdd:cd01752    81 ylsrvIVRDL----QTGKKWFFL-CNDWLSVEEGDGTVERTF 117
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1-31 1.97e-08

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: 53.71  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 224458288    1 MNNEITYYFPCQRWLAVEEDDGQLSRELLPV 31
Cdd:cd01756    90 PGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 907-1008 4.42e-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: 43.87  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  907 YEIVIETGN--GGETRENVWLILEGR-KNRSKEFLMENSSRqraFRKGTTDTFEFDSiyLGDIASLCVGHLAREDrfiPK 983
Cdd:cd00113     3 YTVTIKTGDkkGAGTDSNISLALYGEnGNSSDIPILDGPGS---FERGSTDTFQIDL--KLDIGDITKVYLRRDG---SG 74

                          90       100
                  ....*....|....*....|....*
gi 224458288  984 RELAWHVKTITITEMEYGNVYFFNC 1008
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 ...
 64-184 7.44e-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: 192.00  E-value: 7.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   64 TTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSkTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPG 143
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  144 WFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 184
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 349-469 8.35e-55

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: 186.22  E-value: 8.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  349 VLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCAD 428
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNK-NKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  429 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEK 469
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 774-894 3.08e-54

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: 184.30  E-value: 3.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  774 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 853
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  854 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 894
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 195-321 1.60e-46

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: 162.34  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  195 VPYEITLYTSDVFAAGTDANIFIIIYGcDAVCTQQKYLCTNKREQKqfFERKSASRFIVELEDVGEiIEKIRIGHNNTGM 274
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYG-ENGDTGKRKLKKSNNKNK--FERGQTDKFTVEAVDLGK-LKKIRIGHDNSGL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 224458288  275 NPGWHCSHVDIRRLLPDkdgaETLTFPCDRWLATSEDDKKTIRELVP 321
Cdd:cd01756    77 GAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 647-764 1.36e-45

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: 159.64  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  647 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEW 724
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 224458288  725 FLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 764
Cdd:cd01756    81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1043-1102 4.70e-25

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: 101.09  E-value: 4.70e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224458288 1043 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQK-MRNLFERGSTDRFFLETLEL 1102
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnNKNKFERGQTDKFTVEAVDL 61
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 776-887 3.60e-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: 89.80  E-value: 3.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   776 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQsaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 855
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 224458288   856 LSYVDVKDNSRDE-TFHFQCDCWLSKSEGDGQT 887
Cdd:pfam01477   79 LKSITVEVPGETGgKYTFPCNSWVYGSKKYKET 111
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 66-173 8.86e-20

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: 85.95  E-value: 8.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    66 FSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKsskTNSDKFERDSIEIFTVET-LDLGDLWKVRLGHDNTGKAPGW 144
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT---LDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 224458288   145 FVDWVEVDAPSL-GKCMTFPCGRWLAKNED 173
Cdd:pfam01477   78 FLKSITVEVPGEtGGKYTFPCNSWVYGSKK 107
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 351-466 2.23e-19

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: 84.79  E-value: 2.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   351 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtnkFERGTADTFII-EAADLGVIYKIKLRHDNSKWCADW 429
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD---FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 224458288   430 YVEKVEIW-NDTNEDEFLFLCGRWLSlKKEDGRLERLF 466
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVY-GSKKYKETRVF 114
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
68-171 8.36e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 8.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288     68 VTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSdkFERDSIEIFTVET-LDLGDLWKVRLGHDNtgKAPGWFV 146
Cdd:smart00308    5 VTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGI--FARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 224458288    147 DWVEVDAPSLGKCMTFPCGRWLAKN 171
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 649-758 2.11e-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: 67.84  E-value: 2.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   649 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLE 727
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEWFLK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 224458288   728 RILL-KNMNTGDLTMFYYGDWLSQ-RKGKKTLV 758
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGsKKYKETRV 113
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 197-315 1.42e-12

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: 1.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   197 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKReqkqfFERKSASRFIVELE-DVGEIIeKIRIGHNNTGMN 275
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD-----FERGAEDSFEIDTDwDVGAIL-KINLHWDNNGLS 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 224458288   276 PGWHCSHVdirRLLPDKDGAETLTFPCDRWLATSEDDKKT 315
Cdd:pfam01477   75 DEWFLKSI---TVEVPGETGGKYTFPCNSWVYGSKKYKET 111
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 518-633 1.42e-11

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: 62.68  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwLDYPrGKRGFSRGSVEEFYVAGL-DVGIIKKIELGHDGASPESCW 596
Cdd:cd01752     3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHH-LRDP-EKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224458288  597 -----LVEELclavPTQGTKYMLnCNCWLAKDRGDGITSRVF 633
Cdd:cd01752    81 ylsrvIVRDL----QTGKKWFFL-CNDWLSVEEGDGTVERTF 117
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 518-633 8.96e-10

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: 57.44  E-value: 8.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKR-IWLDYPRgkrgFSRGSVEEFYV-AGLDVGIIKKIELGHDGASPESC 595
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLeITLDNPD----FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDE 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 224458288   596 WLVEELCLAVP-TQGTKYMLNCNCWLAKDRgDGITSRVF 633
Cdd:pfam01477   77 WFLKSITVEVPgETGGKYTFPCNSWVYGSK-KYKETRVF 114
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
776-880 4.88e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.95  E-value: 4.88e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    776 YTVAVKTSDILGAGTDANVFIIIFGENGDSGtLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKgiFPGWH 855
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGK-ESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEWF 79

                            90       100
                    ....*....|....*....|....*
gi 224458288    856 LSYVDVKDNSRDETFHFQCDCWLSK 880
Cdd:smart00308   80 LKSITVKDLPTGGKYHFPCNSWVYP 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
351-456 7.70e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.18  E-value: 7.70e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    351 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENrtNKFERGTADTFIIE-AADLGVIYKIKLRHDNSKwcADW 429
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFK--GIFARGSTYEFTFDvDEDFGELGAVKIKNEHRH--PEW 78

                            90       100
                    ....*....|....*....|....*..
gi 224458288    430 YVEKVEIWNDTNEDEFLFLCGRWLSLK 456
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1-31 1.97e-08

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: 53.71  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 224458288    1 MNNEITYYFPCQRWLAVEEDDGQLSRELLPV 31
Cdd:cd01756    90 PGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1045-1095 1.51e-07

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: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 224458288  1045 YEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKmRNLFERGSTDRF 1095
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLD-NPDFERGAEDSF 50
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
518-623 4.34e-06

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 46.48  E-value: 4.34e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwlDYPRGKRGFSRGSVEEFYVAG-LDVGIIKKIELGHDGASPEscW 596
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESK--LDYLFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEHRHPE--W 78

                            90       100
                    ....*....|....*....|....*..
gi 224458288    597 LVEELCLAVPTQGTKYMLNCNCWLAKD 623
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
649-749 1.45e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 44.94  E-value: 1.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    649 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDK-KKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGlgSRPEWFL 726
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYlFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|...
gi 224458288    727 ERILLKNMNTGDLTMFYYGDWLS 749
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVY 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1044-1095 2.75e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 44.17  E-value: 2.75e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 224458288   1044 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRF 1095
Cdd:smart00308    2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEF 53
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 907-1008 4.42e-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: 43.87  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  907 YEIVIETGN--GGETRENVWLILEGR-KNRSKEFLMENSSRqraFRKGTTDTFEFDSiyLGDIASLCVGHLAREDrfiPK 983
Cdd:cd00113     3 YTVTIKTGDkkGAGTDSNISLALYGEnGNSSDIPILDGPGS---FERGSTDTFQIDL--KLDIGDITKVYLRRDG---SG 74

                          90       100
                  ....*....|....*....|....*
gi 224458288  984 RELAWHVKTITITEMEYGNVYFFNC 1008
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 ...
 64-184 7.44e-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: 192.00  E-value: 7.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   64 TTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSkTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPG 143
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  144 WFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 184
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 349-469 8.35e-55

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: 186.22  E-value: 8.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  349 VLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCAD 428
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNK-NKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  429 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEK 469
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 774-894 3.08e-54

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: 184.30  E-value: 3.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  774 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 853
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 224458288  854 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 894
Cdd:cd01756    80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 195-321 1.60e-46

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: 162.34  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  195 VPYEITLYTSDVFAAGTDANIFIIIYGcDAVCTQQKYLCTNKREQKqfFERKSASRFIVELEDVGEiIEKIRIGHNNTGM 274
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYG-ENGDTGKRKLKKSNNKNK--FERGQTDKFTVEAVDLGK-LKKIRIGHDNSGL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 224458288  275 NPGWHCSHVDIRRLLPDkdgaETLTFPCDRWLATSEDDKKTIRELVP 321
Cdd:cd01756    77 GAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 647-764 1.36e-45

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: 159.64  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  647 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEW 724
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 224458288  725 FLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 764
Cdd:cd01756    81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 649-759 3.55e-31

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: 118.60  E-value: 3.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  649 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLE 727
Cdd:cd00113     3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGWYCE 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 224458288  728 RILLKNMNTGDLTMFYYGDWLSQRKGKKTLVC 759
Cdd:cd00113    83 SITVQALGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 775-894 3.74e-29

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: 112.75  E-value: 3.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  775 SYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGW 854
Cdd:cd01752     2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDP-EKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 224458288  855 HLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 894
Cdd:cd01752    81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 350-467 5.05e-29

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: 5.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  350 LYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRTnkFERGTADTFIIEAA-DLGVIYKIKLRHDNSKWCAD 428
Cdd:cd01752     2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI--FERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPS 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 224458288  429 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFY 467
Cdd:cd01752    80 WYLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFP 118
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1043-1102 4.70e-25

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: 101.09  E-value: 4.70e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224458288 1043 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQK-MRNLFERGSTDRFFLETLEL 1102
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnNKNKFERGQTDKFTVEAVDL 61
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 68-184 1.11e-23

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: 97.35  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   68 VTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSdkFERDSIEIFTVETL-DLGDLWKVRLGHDNTGKAPGWFV 146
Cdd:cd01752     5 VTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI--FERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSWYL 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 224458288  147 DWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 184
Cdd:cd01752    83 SRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 66-176 1.76e-21

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: 90.86  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   66 FSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSsktNSDKFERDSIEIFTVET-LDLGDLWKVRLGHDNTGKAPGW 144
Cdd:cd00113     3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILD---GPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 224458288  145 FVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGS 176
Cdd:cd00113    80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTS 111
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 776-887 3.60e-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: 89.80  E-value: 3.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   776 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQsaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 855
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 224458288   856 LSYVDVKDNSRDE-TFHFQCDCWLSKSEGDGQT 887
Cdd:pfam01477   79 LKSITVEVPGETGgKYTFPCNSWVYGSKKYKET 111
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 776-889 5.17e-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: 86.62  E-value: 5.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  776 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLalKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 855
Cdd:cd00113     3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDI--PILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 224458288  856 LSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVR 889
Cdd:cd00113    81 CESITVQALGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 66-173 8.86e-20

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: 85.95  E-value: 8.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    66 FSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKsskTNSDKFERDSIEIFTVET-LDLGDLWKVRLGHDNTGKAPGW 144
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT---LDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 224458288   145 FVDWVEVDAPSL-GKCMTFPCGRWLAKNED 173
Cdd:pfam01477   78 FLKSITVEVPGEtGGKYTFPCNSWVYGSKK 107
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 351-466 2.23e-19

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: 84.79  E-value: 2.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   351 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtnkFERGTADTFII-EAADLGVIYKIKLRHDNSKWCADW 429
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD---FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 224458288   430 YVEKVEIW-NDTNEDEFLFLCGRWLSlKKEDGRLERLF 466
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVY-GSKKYKETRVF 114
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 197-319 1.92e-18

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: 82.32  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  197 YEITLYTSDVFAAGTDANIFIIIYGCDAvcTQQKYLCTNkrEQKQFFERKSASRFIVE-LEDVGEIiEKIRIGHNNTGMN 275
Cdd:cd01752     3 YLVTVFTGWRRGAGTTAKVTITLYGAEG--ESEPHHLRD--PEKPIFERGSVDSFLLTtPFPLGEL-QSIRLWHDNSGLS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 224458288  276 PGWHCSHVDIRRLLPDKdgaeTLTFPCDRWLATSEDDKKTIREL 319
Cdd:cd01752    78 PSWYLSRVIVRDLQTGK----KWFFLCNDWLSVEEGDGTVERTF 117
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 351-466 5.84e-16

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: 75.07  E-value: 5.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  351 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGErylGKSENRTNKFERGTADTFIIEAA-DLGVIYKIKLRHDNSKWCADW 429
Cdd:cd00113     3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSD---IPILDGPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 224458288  430 YVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLF 466
Cdd:cd00113    80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTSVRSLK 116
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 648-757 2.04e-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: 73.46  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  648 LYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQL-DKKKARFEREQNDTFIMEildiAPF-----TKMRIRIDGLGSR 721
Cdd:cd01752     2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLrDPEKPIFERGSVDSFLLT----TPFplgelQSIRLWHDNSGLS 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 224458288  722 PEWFLERILLKNMNTGDLTMFYYGDWLSQRKGKKTL 757
Cdd:cd01752    78 PSWYLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTV 113
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 66-175 7.31e-15

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: 71.80  E-value: 7.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   66 FSVTIKTGVK-KNAGTDANVFITLFGTQDDTGMTLLKssktnsdkfeRDSIEiFTVETLDLGDLWKVRLGHDNTGKAPGW 144
Cdd:cd01757     3 YHVVIVPSKKlGGSMFTANPWICVSGELGETPPLQIP----------KNSLE-MTFDCQNLGKLTTVQIGHDNSGLLAKW 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 224458288  145 FVDWVEVDAPSLGKCMTFPCGRWLAKNEDDG 175
Cdd:cd01757    72 LVEYVMVRNEITGHTYKFPCGRWLGEGVDDG 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
68-171 8.36e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 8.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288     68 VTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSdkFERDSIEIFTVET-LDLGDLWKVRLGHDNtgKAPGWFV 146
Cdd:smart00308    5 VTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGI--FARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 224458288    147 DWVEVDAPSLGKCMTFPCGRWLAKN 171
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 649-758 2.11e-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: 67.84  E-value: 2.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   649 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLE 727
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEWFLK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 224458288   728 RILL-KNMNTGDLTMFYYGDWLSQ-RKGKKTLV 758
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGsKKYKETRV 113
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1044-1101 6.02e-13

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: 66.53  E-value: 6.02e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 224458288 1044 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRFFLETLE 1101
Cdd:cd01752     2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPF 59
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 197-315 1.42e-12

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: 1.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   197 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKReqkqfFERKSASRFIVELE-DVGEIIeKIRIGHNNTGMN 275
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD-----FERGAEDSFEIDTDwDVGAIL-KINLHWDNNGLS 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 224458288   276 PGWHCSHVdirRLLPDKDGAETLTFPCDRWLATSEDDKKT 315
Cdd:pfam01477   75 DEWFLKSI---TVEVPGETGGKYTFPCNSWVYGSKKYKET 111
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 776-882 5.94e-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: 64.10  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  776 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQS------ANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKG 849
Cdd:cd01754     3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAwgglmgAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 224458288  850 IFPGWHLSYVDVK---DNSRDETFHFQCDCWLSKSE 882
Cdd:cd01754    83 NHPGWYVNYVEVTqagQHAPCMQHLFAVEQWLATDE 118
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 196-306 9.27e-12

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: 63.13  E-value: 9.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  196 PYEITLYTSDVFAAGTDANIFIIIYGcdAVCTQQKYLCTNKreqKQFFERKSASRFIVELE-DVGeIIEKIRIGHNNTGM 274
Cdd:cd00113     2 RYTVTIKTGDKKGAGTDSNISLALYG--ENGNSSDIPILDG---PGSFERGSTDTFQIDLKlDIG-DITKVYLRRDGSGL 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 224458288  275 NPGWHCSHVDIRRLlpdkDGAETLTFPCDRWL 306
Cdd:cd00113    76 SDGWYCESITVQAL----GTKKVYTFPVNRWV 103
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 518-633 1.42e-11

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: 62.68  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwLDYPrGKRGFSRGSVEEFYVAGL-DVGIIKKIELGHDGASPESCW 596
Cdd:cd01752     3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHH-LRDP-EKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224458288  597 -----LVEELclavPTQGTKYMLnCNCWLAKDRGDGITSRVF 633
Cdd:cd01752    81 ylsrvIVRDL----QTGKKWFFL-CNDWLSVEEGDGTVERTF 117
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 65-178 2.27e-11

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: 61.94  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   65 TFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNsdkFERDSIEIFTVE-TLDLGDLWKVRLGHDNTGKAPG 143
Cdd:cd01753     2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD---FERGAVDEYKVKvPEDLGELLLVRLRKRKYLLFDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 224458288  144 WFVDWVEVDAPSlGKCMTFPCGRWLaknEDDGSII 178
Cdd:cd01753    79 WFCNYITVTGPG-GDEYHFPCYRWI---EGYGTLE 109
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 65-172 1.85e-10

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: 59.86  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   65 TFSVTIKTGVKKNAGTDANVFITLFGTQDDTG-MTLLKS----SKTNSDKFERDSIEIFTVETLDL-GDLWKVRLGHDNT 138
Cdd:cd01754     2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLrIANLEAwgglMGAGHDYFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 224458288  139 GKAPGWFVDWVEVDAPSLGK-CMT--FPCGRWLAKNE 172
Cdd:cd01754    82 GNHPGWYVNYVEVTQAGQHApCMQhlFAVEQWLATDE 118
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 518-633 8.96e-10

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: 57.44  E-value: 8.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKR-IWLDYPRgkrgFSRGSVEEFYV-AGLDVGIIKKIELGHDGASPESC 595
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLeITLDNPD----FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDE 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 224458288   596 WLVEELCLAVP-TQGTKYMLNCNCWLAKDRgDGITSRVF 633
Cdd:pfam01477   77 WFLKSITVEVPgETGGKYTFPCNSWVYGSK-KYKETRVF 114
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 349-465 1.98e-09

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: 56.39  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  349 VLYSVQIFTGN-IPGAGTDAKVYITIYGDLGDTGERYLGKsenrtNKFErgtadtFIIEAADLGVIYKIKLRHDNSKWCA 427
Cdd:cd01757     1 MPYHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQIPK-----NSLE------MTFDCQNLGKLTTVQIGHDNSGLLA 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 224458288  428 DWYVEKVEIWNDTNEDEFLFLCGRWLS-----LKKEDGRLERL 465
Cdd:cd01757    70 KWLVEYVMVRNEITGHTYKFPCGRWLGegvddGNGEDGSLERV 112
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
776-880 4.88e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.95  E-value: 4.88e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    776 YTVAVKTSDILGAGTDANVFIIIFGENGDSGtLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKgiFPGWH 855
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGK-ESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEWF 79

                            90       100
                    ....*....|....*....|....*
gi 224458288    856 LSYVDVKDNSRDETFHFQCDCWLSK 880
Cdd:smart00308   80 LKSITVKDLPTGGKYHFPCNSWVYP 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
351-456 7.70e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.18  E-value: 7.70e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    351 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENrtNKFERGTADTFIIE-AADLGVIYKIKLRHDNSKwcADW 429
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFK--GIFARGSTYEFTFDvDEDFGELGAVKIKNEHRH--PEW 78

                            90       100
                    ....*....|....*....|....*..
gi 224458288    430 YVEKVEIWNDTNEDEFLFLCGRWLSLK 456
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1-31 1.97e-08

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: 53.71  E-value: 1.97e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 224458288    1 MNNEITYYFPCQRWLAVEEDDGQLSRELLPV 31
Cdd:cd01756    90 PGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 350-436 3.88e-08

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: 52.93  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  350 LYSVQIFTGNIPGAGTDAKVYITIYGDLGDTG-----ERYLGKSENRTNKFERGTADTFIIEAADL-GVIYKIKLRHDNS 423
Cdd:cd01754     2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLrianlEAWGGLMGAGHDYFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                          90
                  ....*....|...
gi 224458288  424 KWCADWYVEKVEI 436
Cdd:cd01754    82 GNHPGWYVNYVEV 94
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 778-887 6.04e-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: 52.16  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  778 VAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNtdtfnfpdmlsLGHLCKLRVWHDNKGIFPGWHLS 857
Cdd:cd01757     6 VIVPSKKLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFDCQN-----------LGKLTTVQIGHDNSGLLAKWLVE 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 224458288  858 YVDVKDNSRDETFHFQCDCWLSKSEGDGQT 887
Cdd:cd01757    75 YVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1045-1095 1.51e-07

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: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 224458288  1045 YEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKmRNLFERGSTDRF 1095
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLD-NPDFERGAEDSF 50
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 349-454 3.37e-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: 50.00  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  349 VLYSVQIFTGNIPGAGTDAKVYITIygdLGDTGERYLGKSENRTNKFERGTADTFIIEA-ADLGVIYKIKLRHDNSKWCA 427
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTL---VGTAGESEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFD 77

                          90       100
                  ....*....|....*....|....*..
gi 224458288  428 DWYVEKVEIwNDTNEDEFLFLCGRWLS 454
Cdd:cd01753    78 AWFCNYITV-TGPGGDEYHFPCYRWIE 103
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 775-885 6.33e-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: 49.23  E-value: 6.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  775 SYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALkqsANWNK-FERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPG 853
Cdd:cd01753     2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLL---DRPGYdFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDA 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 224458288  854 WHLSYVDVKDNSRDEtFHFQCDCWLsksEGDG 885
Cdd:cd01753    79 WFCNYITVTGPGGDE-YHFPCYRWI---EGYG 106
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 197-310 7.39e-07

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: 49.46  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  197 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCT---NKREQKQFFERKSASRFIVELEDVGEIIEKIRIGHNNTG 273
Cdd:cd01754     3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAwggLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 224458288  274 MNPGWHCSHVDIRRLLPDKDGAETLtFPCDRWLATSE 310
Cdd:cd01754    83 NHPGWYVNYVEVTQAGQHAPCMQHL-FAVEQWLATDE 118
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 197-317 2.74e-06

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: 47.30  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  197 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKReqkqfFERKSASRFIVEL-EDVGEIIeKIRIGHNNTGMN 275
Cdd:cd01753     3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD-----FERGAVDEYKVKVpEDLGELL-LVRLRKRKYLLF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 224458288  276 PGWHCSHVDIRRLlpdkdGAETLTFPCDRWLatseDDKKTIR 317
Cdd:cd01753    77 DAWFCNYITVTGP-----GGDEYHFPCYRWI----EGYGTLE 109
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1044-1095 3.14e-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: 47.33  E-value: 3.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 224458288 1044 KYEVIVTTGYEPGAGTDANVFVTIFGANgdtGKRELKQKMRNL--FERGSTDRF 1095
Cdd:cd00113     2 RYTVTIKTGDKKGAGTDSNISLALYGEN---GNSSDIPILDGPgsFERGSTDTF 52
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
518-623 4.34e-06

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 46.48  E-value: 4.34e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwlDYPRGKRGFSRGSVEEFYVAG-LDVGIIKKIELGHDGASPEscW 596
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESK--LDYLFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEHRHPE--W 78

                            90       100
                    ....*....|....*....|....*..
gi 224458288    597 LVEELCLAVPTQGTKYMLNCNCWLAKD 623
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 350-453 8.32e-06

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: 45.92  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  350 LYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLgksenrTNKFERGTADTFIIEAADLGVIYKIKLRhdNSKWCADW 429
Cdd:cd02899     2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTL------SQGFYPGSLKRIRFRAADVGDINAIILS--NTALNDPW 73

                          90       100
                  ....*....|....*....|....
gi 224458288  430 YVEKVEIWNDTNEdEFLFLCGRWL 453
Cdd:cd02899    74 YCDYVRIKSEDGK-VFAFNVKRWI 96
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
649-749 1.45e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 44.94  E-value: 1.45e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288    649 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDK-KKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGlgSRPEWFL 726
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYlFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|...
gi 224458288    727 ERILLKNMNTGDLTMFYYGDWLS 749
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVY 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1044-1095 2.75e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 44.17  E-value: 2.75e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 224458288   1044 KYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRF 1095
Cdd:smart00308    2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEF 53
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 647-758 4.39e-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: 43.84  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  647 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWF 725
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFDAWF 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 224458288  726 LERILLKNMNtGDLTMFYYGDWLSqrkGKKTLV 758
Cdd:cd01753    81 CNYITVTGPG-GDEYHFPCYRWIE---GYGTLE 109
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 907-1008 4.42e-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: 43.87  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  907 YEIVIETGN--GGETRENVWLILEGR-KNRSKEFLMENSSRqraFRKGTTDTFEFDSiyLGDIASLCVGHLAREDrfiPK 983
Cdd:cd00113     3 YTVTIKTGDkkGAGTDSNISLALYGEnGNSSDIPILDGPGS---FERGSTDTFQIDL--KLDIGDITKVYLRRDG---SG 74

                          90       100
                  ....*....|....*....|....*
gi 224458288  984 RELAWHVKTITITEMEYGNVYFFNC 1008
Cdd:cd00113    75 LSDGWYCESITVQALGTKKVYTFPV 99
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 907-1010 8.00e-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: 43.42  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  907 YEIVIETG--NGGETRENVWLILEGRKNRSKEFLMENSSRQrAFRKGTTDTF----EFDsiyLGDIASLCVGHLAREDRf 980
Cdd:cd01752     3 YLVTVFTGwrRGAGTTAKVTITLYGAEGESEPHHLRDPEKP-IFERGSVDSFllttPFP---LGELQSIRLWHDNSGLS- 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 224458288  981 iPkrelAWHVKTITITEMEYGNVYFFNCDC 1010
Cdd:cd01752    78 -P----SWYLSRVIVRDLQTGKKWFFLCND 102
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 6-29 1.05e-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: 43.03  E-value: 1.05e-04
                          10        20
                  ....*....|....*....|....
gi 224458288    6 TYYFPCQRWLAVEEDDGQLSRELL 29
Cdd:cd01752    95 KWFFLCNDWLSVEEGDGTVERTFP 118
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 197-308 5.25e-04

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: 40.52  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  197 YEITLYTSDVFAAGTDANIFIIIYGCDAVctqqkylcTNKREQKQFFERKSASRFIVELEDVGEIIEKIRIghnNTGMNP 276
Cdd:cd02899     3 YTASVQTGKDKEAGTNGTIEITLLGSSGR--------SNPKTLSQGFYPGSLKRIRFRAADVGDINAIILS---NTALND 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 224458288  277 GWHCSHVDIRrllpdKDGAETLTFPCDRWLAT 308
Cdd:cd02899    72 PWYCDYVRIK-----SEDGKVFAFNVKRWIGY 98
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 518-620 1.07e-03

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: 39.98  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  518 YYVSVTTGKHKDAATDSRAFIFLIGEDDErSKRIWLDYPrgKRGFSRGSVEEFYV-AGLDVGIIKKIELGHDGASPESCW 596
Cdd:cd01753     3 YKVTVATGSSLFAGTDDYIYLTLVGTAGE-SEKQLLDRP--GYDFERGAVDEYKVkVPEDLGELLLVRLRKRKYLLFDAW 79

                          90       100
                  ....*....|....*....|....
gi 224458288  597 LVEELCLAVPtQGTKYMLNCNCWL 620
Cdd:cd01753    80 FCNYITVTGP-GGDEYHFPCYRWI 102
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 1045-1095 1.45e-03

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: 39.83  E-value: 1.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 224458288 1045 YEVIVTTGYEPGAGTDANVFVTIFGANGDTGK-------RELKQKMRNLFERGSTDRF 1095
Cdd:cd01754     3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRianleawGGLMGAGHDYFERGNLDRF 60
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 65-170 1.50e-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: 39.37  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288   65 TFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSktnsdkFERDSIEIFTVETLDLGDLWKVRLGhdNTGKAPGW 144
Cdd:cd02899     2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG------FYPGSLKRIRFRAADVGDINAIILS--NTALNDPW 73

                          90       100
                  ....*....|....*....|....*.
gi 224458288  145 FVDWVEVDAPSlGKCMTFPCGRWLAK 170
Cdd:cd02899    74 YCDYVRIKSED-GKVFAFNVKRWIGY 98
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1043-1095 1.58e-03

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: 39.21  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224458288 1043 VKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNlFERGSTDRF 1095
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD-FERGAVDEY 52
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 516-629 2.37e-03

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: 39.06  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  516 IPYYVSVTTGKHKDAA-TDSRAFIFLIGEDDErSKRIWLdyPRGkrgfsrgsVEEFYVAGLDVGIIKKIELGHDGASPES 594
Cdd:cd01757     1 MPYHVVIVPSKKLGGSmFTANPWICVSGELGE-TPPLQI--PKN--------SLEMTFDCQNLGKLTTVQIGHDNSGLLA 69

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 224458288  595 CWLVEELCLAVPTQGTKYMLNCNCWLAKDRGDGIT 629
Cdd:cd01757    70 KWLVEYVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 195-312 5.13e-03

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: 37.90  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  195 VPYEITLYTSD-VFAAGTDANIFIIIYGcdavctqqkYLCTNKREQkqfFERKSASrFIVELEDVGeIIEKIRIGHNNTG 273
Cdd:cd01757     1 MPYHVVIVPSKkLGGSMFTANPWICVSG---------ELGETPPLQ---IPKNSLE-MTFDCQNLG-KLTTVQIGHDNSG 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 224458288  274 MNPGWHCSHVDIRRLLPDKdgaeTLTFPCDRWLATSEDD 312
Cdd:cd01757    67 LLAKWLVEYVMVRNEITGH----TYKFPCGRWLGEGVDD 101
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 647-748 6.47e-03

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: 37.52  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224458288  647 VLYEMTVWTGDVVGG-GTDSNIFMTLYGINGSTEEMQLdkKKARFEreqndtFIMEILDIAPFTKMRIRIDGLGSRPEWF 725
Cdd:cd01757     1 MPYHVVIVPSKKLGGsMFTANPWICVSGELGETPPLQI--PKNSLE------MTFDCQNLGKLTTVQIGHDNSGLLAKWL 72

                          90       100
                  ....*....|....*....|...
gi 224458288  726 LERILLKNMNTGDLTMFYYGDWL 748
Cdd:cd01757    73 VEYVMVRNEITGHTYKFPCGRWL 95
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 518-588 8.41e-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: 8.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224458288  518 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIWldyprgKRGFSRGSVEEFYVAGLDVGIIKKIELGHD 588
Cdd:cd02899     3 YTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTL------SQGFYPGSLKRIRFRAADVGDINAIILSNT 67
 
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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