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Conserved domains on  [gi|2217316121|ref|XP_047293247|]
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lipoxygenase homology domain-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

phospholipase C( domain architecture ID 10109880)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 744-864 2.78e-62

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: 208.18  E-value: 2.78e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  744 NTYEVQVVTGNVPKAGTDANVYLTIYGEeYGDTGERPLKKSDKSNKFEQGQTDTFTIYAIDLGALTKIRIRHDNTGNRAG 823
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGE-NGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  824 WFLDRIDITDMNNEITYYFPCQRWLAVEEDDGQLSRELLPV 864
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 897-1017 8.99e-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: 192.38  E-value: 8.99e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  897 TTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSkTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPG 976
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  977 WFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 1017
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 276-397 3.05e-56

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: 190.84  E-value: 3.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  276 RYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCrNNTDLFEKGNADEFTIESVTMRNVRRVRIRHDGKGSGSGW 355
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  356 YLDRVLVREEGQpeSDNVEFPCLRWLDKDKDDGQLVRELLPS 397
Cdd:cd01756     81 FLDKVEIREPGT--GDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1182-1302 9.25e-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: 186.61  E-value: 9.25e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1182 VLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCAD 1261
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNK-NKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121 1262 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEK 1302
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1607-1727 3.66e-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: 184.68  E-value: 3.66e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1607 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 1686
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121 1687 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 1727
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 406-527 3.42e-52

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: 179.29  E-value: 3.42e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  406 FRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNnlKDYFERGRVDEFTLETLNIGNINRLVIGHDSTGMHA 485
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNN--KNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  486 SWFLGSVQIRVPRQGKQYTFPANRWLDKNQADGRLEVELYPS 527
Cdd:cd01756     79 GWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 147-264 1.06e-48

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: 169.27  E-value: 1.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  147 FPWSLWVWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNK--WFKPGIIEKFRIELPDLGRFYKIRVWHDKRSSGSGW 224
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNknKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121  225 HLERMTLMNTLNKDKYNFNCNRWLDANEDDNEIVREMTAE 264
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1028-1154 1.79e-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: 162.72  E-value: 1.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1028 VPYEITLYTSDVFAAGTDANIFIIIYGcDAVCTQQKYLCTNKREQKqfFERKSASRFIVELEDVGEiIEKIRIGHNNTGM 1107
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYG-ENGDTGKRKLKKSNNKNK--FERGQTDKFTVEAVDLGK-LKKIRIGHDNSGL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217316121 1108 NPGWHCSHVDIRRLLPDkdgaETLTFPCDRWLATSEDDKKTIRELVP 1154
Cdd:cd01756     77 GAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 18-136 2.90e-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: 2.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   18 ITYIVTVFTGDVRGAGTKSKIYLVMYGARGNknSGKIFLE----GGVFDRGRTDIFHIElAVLLSPLSRVSVGHGNVGVN 93
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGD--TGKRKLKksnnKNKFERGQTDKFTVE-AVDLGKLKKIRIGHDNSGLG 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217316121   94 RGWFCEKVVILCPFTGIQQTFPCSNWLDEKKADGLIERQLYEM 136
Cdd:cd01756     78 AGWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1480-1597 1.63e-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: 160.03  E-value: 1.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1480 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEW 1557
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121 1558 FLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 1597
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 538-618 3.67e-28

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


The actual alignment was detected with superfamily member cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 110.72  E-value: 3.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFL--SSRSKVFERASKDTFQLEAADVGEVYKLRLGHTGEGFGPSWFV 615
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLkkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82


                   ...
gi 2217316121  616 DTV 618
Cdd:cd01756     83 DKV 85
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1351-1466 3.15e-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: 62.29  E-value: 3.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwLDYPrGKRGFSRGSVEEFYVAGL-DVGIIKKIELGHDGASPESCW 1429
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHH-LRDP-EKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121 1430 -----LVEELclavPTQGTKYMLnCNCWLAKDRGDGITSRVF 1466
Cdd:cd01752     81 ylsrvIVRDL----QTGKKWFFL-CNDWLSVEEGDGTVERTF 117
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 744-864 2.78e-62

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: 208.18  E-value: 2.78e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  744 NTYEVQVVTGNVPKAGTDANVYLTIYGEeYGDTGERPLKKSDKSNKFEQGQTDTFTIYAIDLGALTKIRIRHDNTGNRAG 823
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGE-NGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  824 WFLDRIDITDMNNEITYYFPCQRWLAVEEDDGQLSRELLPV 864
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 897-1017 8.99e-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: 192.38  E-value: 8.99e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  897 TTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSkTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPG 976
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  977 WFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 1017
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 276-397 3.05e-56

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: 190.84  E-value: 3.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  276 RYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCrNNTDLFEKGNADEFTIESVTMRNVRRVRIRHDGKGSGSGW 355
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  356 YLDRVLVREEGQpeSDNVEFPCLRWLDKDKDDGQLVRELLPS 397
Cdd:cd01756     81 FLDKVEIREPGT--GDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1182-1302 9.25e-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: 186.61  E-value: 9.25e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1182 VLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCAD 1261
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNK-NKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121 1262 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEK 1302
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1607-1727 3.66e-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: 184.68  E-value: 3.66e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1607 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 1686
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121 1687 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 1727
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 406-527 3.42e-52

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: 179.29  E-value: 3.42e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  406 FRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNnlKDYFERGRVDEFTLETLNIGNINRLVIGHDSTGMHA 485
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNN--KNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  486 SWFLGSVQIRVPRQGKQYTFPANRWLDKNQADGRLEVELYPS 527
Cdd:cd01756     79 GWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 147-264 1.06e-48

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: 169.27  E-value: 1.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  147 FPWSLWVWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNK--WFKPGIIEKFRIELPDLGRFYKIRVWHDKRSSGSGW 224
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNknKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121  225 HLERMTLMNTLNKDKYNFNCNRWLDANEDDNEIVREMTAE 264
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1028-1154 1.79e-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: 162.72  E-value: 1.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1028 VPYEITLYTSDVFAAGTDANIFIIIYGcDAVCTQQKYLCTNKREQKqfFERKSASRFIVELEDVGEiIEKIRIGHNNTGM 1107
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYG-ENGDTGKRKLKKSNNKNK--FERGQTDKFTVEAVDLGK-LKKIRIGHDNSGL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217316121 1108 NPGWHCSHVDIRRLLPDkdgaETLTFPCDRWLATSEDDKKTIRELVP 1154
Cdd:cd01756     77 GAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 18-136 2.90e-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: 2.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   18 ITYIVTVFTGDVRGAGTKSKIYLVMYGARGNknSGKIFLE----GGVFDRGRTDIFHIElAVLLSPLSRVSVGHGNVGVN 93
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGD--TGKRKLKksnnKNKFERGQTDKFTVE-AVDLGKLKKIRIGHDNSGLG 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217316121   94 RGWFCEKVVILCPFTGIQQTFPCSNWLDEKKADGLIERQLYEM 136
Cdd:cd01756     78 AGWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1480-1597 1.63e-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: 160.03  E-value: 1.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1480 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEW 1557
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121 1558 FLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 1597
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 538-618 3.67e-28

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


Pssm-ID: 238854  Cd Length: 120  Bit Score: 110.72  E-value: 3.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFL--SSRSKVFERASKDTFQLEAADVGEVYKLRLGHTGEGFGPSWFV 615
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLkkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82


                   ...
gi 2217316121  616 DTV 618
Cdd:cd01756     83 DKV 85
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 746-853 1.04e-23

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: 97.50  E-value: 1.04e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  746 YEVQVVTGNVPKAGTDANVYLTIYGEEyGDTGERPLKKSDKSnkFEQGQTDTFTIYA-IDLGALTKIRIRHDNTGNRAGW 824
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKV-GESAQLEITLDNPD--FERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121  825 FLDRIDIT-DMNNEITYYFPCQRWLAVEED 853
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSKK 107
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1609-1720 5.12e-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: 5.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1609 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQsaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 1688
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217316121 1689 LSYVDVKDNSRDE-TFHFQCDCWLSKSEGDGQT 1720
Cdd:pfam01477   79 LKSITVEVPGETGgKYTFPCNSWVYGSKKYKET 111
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 899-1006 1.30e-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: 85.95  E-value: 1.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  899 FSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKsskTNSDKFERDSIEIFTVET-LDLGDLWKVRLGHDNTGKAPGW 977
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT---LDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121  978 FVDWVEVDAPSL-GKCMTFPCGRWLAKNED 1006
Cdd:pfam01477   78 FLKSITVEVPGEtGGKYTFPCNSWVYGSKK 107
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1184-1299 3.30e-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: 3.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1184 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtnkFERGTADTFII-EAADLGVIYKIKLRHDNSKWCADW 1262
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD---FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217316121 1263 YVEKVEIW-NDTNEDEFLFLCGRWLSlKKEDGRLERLF 1299
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVY-GSKKYKETRVF 114
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 20-124 1.36e-18

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


Pssm-ID: 396180  Cd Length: 115  Bit Score: 83.25  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   20 YIVTVFTGDVRGAGTKSKIYLVMYGARGNKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGVNRGWFCE 99
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80

                           90       100
                   ....*....|....*....|....*.
gi 2217316121  100 KVVILCP-FTGIQQTFPCSNWLDEKK 124
Cdd:pfam01477   81 SITVEVPgETGGKYTFPCNSWVYGSK 106
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 408-515 3.30e-17

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: 79.01  E-value: 3.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  408 YHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNNlkdyFERGRVDEFTLET-LNIGNINRLVIGHDSTGMHAS 486
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD----FERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDE 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121  487 WFLGSVQIRVPRQ-GKQYTFPANRWLDKNQ 515
Cdd:pfam01477   77 WFLKSITVEVPGEtGGKYTFPCNSWVYGSK 106
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 149-256 6.89e-16

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: 75.16  E-value: 6.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  149 WSLWVWTTDLKKAGTNSPIFIQIYGQKGRT--DEILLNPNNkwFKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGSGWH 225
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121  226 LERMTLM-NTLNKDKYNFNCNRWLDANEDDNE 256
Cdd:pfam01477   79 LKSITVEvPGETGGKYTFPCNSWVYGSKKYKE 110
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 277-386 8.54e-16

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: 75.16  E-value: 8.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  277 YHVTVCTGELEGAGTDANVYLCLFGDVGDTGerLLYNCRNNTDlFEKGNADEFTI-ESVTMRNVRRVRIRHDGKGSGSGW 355
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESA--QLEITLDNPD-FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217316121  356 YLDRVLVREEGQPESdNVEFPCLRWLDKDKD 386
Cdd:pfam01477   78 FLKSITVEVPGETGG-KYTFPCNSWVYGSKK 107
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
901-1004 1.33e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 1.33e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   901 VTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSdkFERDSIEIFTVET-LDLGDLWKVRLGHDNtgKAPGWFV 979
Cdd:smart00308    5 VTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGI--FARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 2217316121   980 DWVEVDAPSLGKCMTFPCGRWLAKN 1004
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 538-621 1.84e-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: 68.61  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFLSSRSKVFERASKDTFQL-EAADVGEVYKLRLGHTGEGFGPSWFVD 616
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWFLK 80


                   ....*
gi 2217316121  617 TVWLR 621
Cdd:pfam01477   81 SITVE 85
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1482-1591 3.07e-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: 3.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1482 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLE 1560
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEWFLK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217316121 1561 RILL-KNMNTGDLTMFYYGDWLSQ-RKGKKTLV 1591
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGsKKYKETRV 113
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
153-249 7.47e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 66.51  E-value: 7.47e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   153 VWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNKW-FKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGsgWHLERMT 230
Cdd:smart00308    7 VTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGiFARGSTYEFTFDVDeDFGELGAVKIKNEHRHPE--WFLKSIT 84

                            90
                    ....*....|....*....
gi 2217316121   231 LMNTLNKDKYNFNCNRWLD 249
Cdd:smart00308   85 VKDLPTGGKYHFPCNSWVY 103
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1030-1148 2.04e-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: 65.53  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1030 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKReqkqfFERKSASRFIVELE-DVGEIIeKIRIGHNNTGMN 1108
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD-----FERGAEDSFEIDTDwDVGAIL-KINLHWDNNGLS 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121 1109 PGWHCSHVdirRLLPDKDGAETLTFPCDRWLATSEDDKKT 1148
Cdd:pfam01477   75 DEWFLKSI---TVEVPGETGGKYTFPCNSWVYGSKKYKET 111
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
746-848 9.01e-12

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 63.43  E-value: 9.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   746 YEVQVVTGNVPKAGTDANVYLTIYGEEyGDTGERPLKKSDKsNKFEQGQTDTFTI-YAIDLGALTKIRIRHDNtgNRAGW 824
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAE-GDGKESKLDYLFK-GIFARGSTYEFTFdVDEDFGELGAVKIKNEH--RHPEW 78

                            90       100
                    ....*....|....*....|....
gi 2217316121   825 FLDRIDITDMNNEITYYFPCQRWL 848
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWV 102
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1351-1466 3.15e-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: 62.29  E-value: 3.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwLDYPrGKRGFSRGSVEEFYVAGL-DVGIIKKIELGHDGASPESCW 1429
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHH-LRDP-EKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121 1430 -----LVEELclavPTQGTKYMLnCNCWLAKDRGDGITSRVF 1466
Cdd:cd01752     81 ylsrvIVRDL----QTGKKWFFL-CNDWLSVEEGDGTVERTF 117
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
275-384 1.12e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 59.96  E-value: 1.12e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   275 ARYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCRNNtdLFEKGNADEFTIE-SVTMRNVRRVRIRHDGKgsGS 353
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKG--IFARGSTYEFTFDvDEDFGELGAVKIKNEHR--HP 76

                            90       100       110
                    ....*....|....*....|....*....|.
gi 2217316121   354 GWYLDRVLVreEGQPESDNVEFPCLRWLDKD 384
Cdd:smart00308   77 EWFLKSITV--KDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1351-1466 1.37e-09

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: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKR-IWLDYPRgkrgFSRGSVEEFYV-AGLDVGIIKKIELGHDGASPESC 1428
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLeITLDNPD----FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDE 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217316121 1429 WLVEELCLAVP-TQGTKYMLNCNCWLAKDRgDGITSRVF 1466
Cdd:pfam01477   77 WFLKSITVEVPgETGGKYTFPCNSWVYGSK-KYKETRVF 114
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1609-1713 7.79e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.95  E-value: 7.79e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1609 YTVAVKTSDILGAGTDANVFIIIFGENGDSGtLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKgiFPGWH 1688
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGK-ESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEWF 79

                            90       100
                    ....*....|....*....|....*
gi 2217316121  1689 LSYVDVKDNSRDETFHFQCDCWLSK 1713
Cdd:smart00308   80 LKSITVKDLPTGGKYHFPCNSWVYP 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1184-1289 1.23e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.18  E-value: 1.23e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1184 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENrtNKFERGTADTFIIE-AADLGVIYKIKLRHDNSKwcADW 1262
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFK--GIFARGSTYEFTFDvDEDFGELGAVKIKNEHRH--PEW 78

                            90       100
                    ....*....|....*....|....*..
gi 2217316121  1263 YVEKVEIWNDTNEDEFLFLCGRWLSLK 1289
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
20-123 3.95e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 53.03  E-value: 3.95e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121    20 YIVTVFTGDVRGAGTKSKIYLVMYGARG-NKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGvnRGWFC 98
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGdGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHRH--PEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 2217316121    99 EKVVILCPFTGIQQTFPCSNWLDEK 123
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
406-514 6.62e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 52.26  E-value: 6.62e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   406 FRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLlvsDNNLKDYFERGRVDEFTLET-LNIGNINRLVIGHDSTgmH 484
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKL---DYLFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEHR--H 75

                            90       100       110
                    ....*....|....*....|....*....|
gi 2217316121   485 ASWFLGSVQIRVPRQGKQYTFPANRWLDKN 514
Cdd:smart00308   76 PEWFLKSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1351-1456 6.86e-06

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 46.48  E-value: 6.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwlDYPRGKRGFSRGSVEEFYVAG-LDVGIIKKIELGHDGASPEscW 1429
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESK--LDYLFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEHRHPE--W 78

                            90       100
                    ....*....|....*....|....*..
gi 2217316121  1430 LVEELCLAVPTQGTKYMLNCNCWLAKD 1456
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1482-1582 2.31e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 44.94  E-value: 2.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1482 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDK-KKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGlgSRPEWFL 1559
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYlFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|...
gi 2217316121  1560 ERILLKNMNTGDLTMFYYGDWLS 1582
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVY 103
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 744-864 2.78e-62

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: 208.18  E-value: 2.78e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  744 NTYEVQVVTGNVPKAGTDANVYLTIYGEeYGDTGERPLKKSDKSNKFEQGQTDTFTIYAIDLGALTKIRIRHDNTGNRAG 823
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGE-NGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  824 WFLDRIDITDMNNEITYYFPCQRWLAVEEDDGQLSRELLPV 864
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 897-1017 8.99e-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: 192.38  E-value: 8.99e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  897 TTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSkTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPG 976
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  977 WFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 1017
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 276-397 3.05e-56

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: 190.84  E-value: 3.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  276 RYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCrNNTDLFEKGNADEFTIESVTMRNVRRVRIRHDGKGSGSGW 355
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  356 YLDRVLVREEGQpeSDNVEFPCLRWLDKDKDDGQLVRELLPS 397
Cdd:cd01756     81 FLDKVEIREPGT--GDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1182-1302 9.25e-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: 186.61  E-value: 9.25e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1182 VLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCAD 1261
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNK-NKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121 1262 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEK 1302
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1607-1727 3.66e-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: 184.68  E-value: 3.66e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1607 TSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFpDMLSLGHLCKLRVWHDNKGIFPG 1686
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTV-EAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121 1687 WHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 1727
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 406-527 3.42e-52

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: 179.29  E-value: 3.42e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  406 FRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNnlKDYFERGRVDEFTLETLNIGNINRLVIGHDSTGMHA 485
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNN--KNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  486 SWFLGSVQIRVPRQGKQYTFPANRWLDKNQADGRLEVELYPS 527
Cdd:cd01756     79 GWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 147-264 1.06e-48

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: 169.27  E-value: 1.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  147 FPWSLWVWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNK--WFKPGIIEKFRIELPDLGRFYKIRVWHDKRSSGSGW 224
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNknKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121  225 HLERMTLMNTLNKDKYNFNCNRWLDANEDDNEIVREMTAE 264
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1028-1154 1.79e-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: 162.72  E-value: 1.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1028 VPYEITLYTSDVFAAGTDANIFIIIYGcDAVCTQQKYLCTNKREQKqfFERKSASRFIVELEDVGEiIEKIRIGHNNTGM 1107
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYG-ENGDTGKRKLKKSNNKNK--FERGQTDKFTVEAVDLGK-LKKIRIGHDNSGL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217316121 1108 NPGWHCSHVDIRRLLPDkdgaETLTFPCDRWLATSEDDKKTIRELVP 1154
Cdd:cd01756     77 GAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 18-136 2.90e-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: 2.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   18 ITYIVTVFTGDVRGAGTKSKIYLVMYGARGNknSGKIFLE----GGVFDRGRTDIFHIElAVLLSPLSRVSVGHGNVGVN 93
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGD--TGKRKLKksnnKNKFERGQTDKFTVE-AVDLGKLKKIRIGHDNSGLG 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217316121   94 RGWFCEKVVILCPFTGIQQTFPCSNWLDEKKADGLIERQLYEM 136
Cdd:cd01756     78 AGWFLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1480-1597 1.63e-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: 160.03  E-value: 1.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1480 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKK--KARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEW 1557
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSnnKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121 1558 FLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAV 1597
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1482-1592 4.96e-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: 4.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1482 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLE 1560
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGWYCE 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121 1561 RILLKNMNTGDLTMFYYGDWLSQRKGKKTLVC 1592
Cdd:cd00113     83 SITVQALGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 746-862 5.04e-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: 113.14  E-value: 5.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  746 YEVQVVTGNVPKAGTDANVYLTIYGEEyGDTGERPLKKSDKSnKFEQGQTDTFTI-YAIDLGALTKIRIRHDNTGNRAGW 824
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAE-GESEPHHLRDPEKP-IFERGSVDSFLLtTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217316121  825 FLDRIDITDMNNEITYYFPCQRWLAVEEDDGQLSRELL 862
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFP 118
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1608-1727 8.50e-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: 8.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1608 SYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGW 1687
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDP-EKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121 1688 HLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACA 1727
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1183-1300 1.28e-28

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: 111.98  E-value: 1.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1183 LYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRTnkFERGTADTFIIEAA-DLGVIYKIKLRHDNSKWCAD 1261
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI--FERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPS 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217316121 1262 WYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFY 1300
Cdd:cd01752     80 WYLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFP 118
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 538-618 3.67e-28

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


Pssm-ID: 238854  Cd Length: 120  Bit Score: 110.72  E-value: 3.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFL--SSRSKVFERASKDTFQLEAADVGEVYKLRLGHTGEGFGPSWFV 615
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLkkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82


                   ...
gi 2217316121  616 DTV 618
Cdd:cd01756     83 DKV 85
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 746-853 1.04e-23

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: 97.50  E-value: 1.04e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  746 YEVQVVTGNVPKAGTDANVYLTIYGEEyGDTGERPLKKSDKSnkFEQGQTDTFTIYA-IDLGALTKIRIRHDNTGNRAGW 824
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKV-GESAQLEITLDNPD--FERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121  825 FLDRIDIT-DMNNEITYYFPCQRWLAVEED 853
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSKK 107
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 901-1017 2.44e-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: 96.96  E-value: 2.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  901 VTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSdkFERDSIEIFTVETL-DLGDLWKVRLGHDNTGKAPGWFV 979
Cdd:cd01752      5 VTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI--FERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSWYL 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217316121  980 DWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHA 1017
Cdd:cd01752     83 SRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 899-1009 2.54e-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: 2.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  899 FSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSsktNSDKFERDSIEIFTVET-LDLGDLWKVRLGHDNTGKAPGW 977
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILD---GPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121  978 FVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGS 1009
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTS 111
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1609-1720 5.12e-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: 5.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1609 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQsaNWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 1688
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITL--DNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217316121 1689 LSYVDVKDNSRDE-TFHFQCDCWLSKSEGDGQT 1720
Cdd:pfam01477   79 LKSITVEVPGETGgKYTFPCNSWVYGSKKYKET 111
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 746-848 4.76e-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: 87.39  E-value: 4.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  746 YEVQVVTGNVPKAGTDANVYLTIYGEeYGDTGERPLkkSDKSNKFEQGQTDTFTIYA-IDLGALTKIRIRHDNTGNRAGW 824
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGE-NGNSSDIPI--LDGPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....
gi 2217316121  825 FLDRIDITDMNNEITYYFPCQRWL 848
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWV 103
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 406-525 6.16e-20

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: 86.95  E-value: 6.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  406 FRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDnnlKDYFERGRVDEFTLETL-NIGNINRLVIGHDSTGMH 484
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPE---KPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLS 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  485 ASWFLGSVQIRVPRQGKQYTFPANRWLDKNQADGRLEVELY 525
Cdd:cd01752     78 PSWYLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFP 118
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1609-1722 7.66e-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: 7.66e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1609 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLalKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWH 1688
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDI--PILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2217316121 1689 LSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVR 1722
Cdd:cd00113     81 CESITVQALGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 899-1006 1.30e-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: 85.95  E-value: 1.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  899 FSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKsskTNSDKFERDSIEIFTVET-LDLGDLWKVRLGHDNTGKAPGW 977
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT---LDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121  978 FVDWVEVDAPSL-GKCMTFPCGRWLAKNED 1006
Cdd:pfam01477   78 FLKSITVEVPGEtGGKYTFPCNSWVYGSKK 107
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1184-1299 3.30e-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: 3.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1184 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRtnkFERGTADTFII-EAADLGVIYKIKLRHDNSKWCADW 1262
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD---FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217316121 1263 YVEKVEIW-NDTNEDEFLFLCGRWLSlKKEDGRLERLF 1299
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVY-GSKKYKETRVF 114
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 20-124 1.36e-18

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


Pssm-ID: 396180  Cd Length: 115  Bit Score: 83.25  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   20 YIVTVFTGDVRGAGTKSKIYLVMYGARGNKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGVNRGWFCE 99
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80

                           90       100
                   ....*....|....*....|....*.
gi 2217316121  100 KVVILCP-FTGIQQTFPCSNWLDEKK 124
Cdd:pfam01477   81 SITVEVPgETGGKYTFPCNSWVYGSK 106
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1030-1152 4.41e-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: 81.94  E-value: 4.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1030 YEITLYTSDVFAAGTDANIFIIIYGCDAvcTQQKYLCTNkrEQKQFFERKSASRFIVE-LEDVGEIiEKIRIGHNNTGMN 1108
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAEG--ESEPHHLRD--PEKPIFERGSVDSFLLTtPFPLGEL-QSIRLWHDNSGLS 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217316121 1109 PGWHCSHVDIRRLLPDKdgaeTLTFPCDRWLATSEDDKKTIREL 1152
Cdd:cd01752     78 PSWYLSRVIVRDLQTGK----KWFFLCNDWLSVEEGDGTVERTF 117
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 20-122 8.85e-18

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: 80.85  E-value: 8.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   20 YIVTVFTGDVRGAGTKSKIYLVMYGARGNKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGVNRGWFCE 99
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYCE 82

                           90       100
                   ....*....|....*....|...
gi 2217316121  100 KVVILCPFTGIQQTFPCSNWLDE 122
Cdd:cd00113     83 SITVQALGTKKVYTFPVNRWVLG 105
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 276-395 2.50e-17

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: 79.63  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  276 RYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNcrNNTDLFEKGNADEFTIESV-TMRNVRRVRIRHDGKGSGSG 354
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRD--PEKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  355 WYLDRVLVREegqPESDNV-EFPCLRWLDKDKDDGQLVRELL 395
Cdd:cd01752     80 WYLSRVIVRD---LQTGKKwFFLCNDWLSVEEGDGTVERTFP 118
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 408-515 3.30e-17

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: 79.01  E-value: 3.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  408 YHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNNlkdyFERGRVDEFTLET-LNIGNINRLVIGHDSTGMHAS 486
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD----FERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDE 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121  487 WFLGSVQIRVPRQ-GKQYTFPANRWLDKNQ 515
Cdd:pfam01477   77 WFLKSITVEVPGEtGGKYTFPCNSWVYGSK 106
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 276-392 9.28e-17

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


Pssm-ID: 238061  Cd Length: 116  Bit Score: 77.76  E-value: 9.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  276 RYHVTVCTGELEGAGTDANVYLCLFGDVGDTGErllYNCRNNTDLFEKGNADEFTIE-SVTMRNVRRVRIRHDGKGSGSG 354
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSD---IPILDGPGSFERGSTDTFQIDlKLDIGDITKVYLRRDGSGLSDG 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217316121  355 WYLDRVLVREEGqpESDNVEFPCLRWLDKDKDDGQLVR 392
Cdd:cd00113     79 WYCESITVQALG--TKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 20-134 1.12e-16

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: 77.70  E-value: 1.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   20 YIVTVFTGDVRGAGTKSKIYLVMYGArgNKNSGKIFLEGG---VFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGVNRGW 96
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGA--EGESEPHHLRDPekpIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217316121   97 FCEKVVILCPFTGIQQTFPCSNWLDEKKADGLIERQLY 134
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFP 118
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 148-255 1.27e-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: 77.38  E-value: 1.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  148 PWSLWVWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNKWFKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGSGWHL 226
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGWYC 81

                           90       100
                   ....*....|....*....|....*....
gi 2217316121  227 ERMTLMNTLNKDKYNFNCNRWLDANEDDN 255
Cdd:cd00113     82 ESITVQALGTKKVYTFPVNRWVLGGKWYT 110
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 149-256 6.89e-16

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: 75.16  E-value: 6.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  149 WSLWVWTTDLKKAGTNSPIFIQIYGQKGRT--DEILLNPNNkwFKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGSGWH 225
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121  226 LERMTLM-NTLNKDKYNFNCNRWLDANEDDNE 256
Cdd:pfam01477   79 LKSITVEvPGETGGKYTFPCNSWVYGSKKYKE 110
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 277-386 8.54e-16

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: 75.16  E-value: 8.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  277 YHVTVCTGELEGAGTDANVYLCLFGDVGDTGerLLYNCRNNTDlFEKGNADEFTI-ESVTMRNVRRVRIRHDGKGSGSGW 355
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESA--QLEITLDNPD-FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217316121  356 YLDRVLVREEGQPESdNVEFPCLRWLDKDKD 386
Cdd:pfam01477   78 FLKSITVEVPGETGG-KYTFPCNSWVYGSKK 107
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1184-1299 8.57e-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: 8.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1184 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGErylGKSENRTNKFERGTADTFIIEAA-DLGVIYKIKLRHDNSKWCADW 1262
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSD---IPILDGPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217316121 1263 YVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLF 1299
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTSVRSLK 116
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 537-628 1.02e-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: 75.00  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  537 HYEVEIWTGDVGGAGTSARVYMQIYGEKGKTEV-LFLSSRSKVFERASKDTFQLEAA-DVGEVYKLRLGHTGEGFGPSWF 614
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPhHLRDPEKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSWY 81

                           90
                   ....*....|....
gi 2217316121  615 VDTVWLRHLVVREV 628
Cdd:cd01752     82 LSRVIVRDLQTGKK 95
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 407-514 1.02e-15

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: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  407 RYHISLKTGDVSGASTDSRVYIKLYGDKSDTiKQVLLVSDNnlkDYFERGRVDEFTLET-LNIGNINRLVIGHDSTGMHA 485
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNS-SDIPILDGP---GSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSD 77

                           90       100
                   ....*....|....*....|....*....
gi 2217316121  486 SWFLGSVQIRVPRQGKQYTFPANRWLDKN 514
Cdd:cd00113     78 GWYCESITVQALGTKKVYTFPVNRWVLGG 106
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 159-264 1.66e-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: 74.23  E-value: 1.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  159 KKAGTNSPIFIQIYGQKGRTD-EILLNPNNKWFKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGSGWHLERMTLMNTLN 236
Cdd:cd01752     13 RGAGTTAKVTITLYGAEGESEpHHLRDPEKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSWYLSRVIVRDLQT 92

                           90       100
                   ....*....|....*....|....*...
gi 2217316121  237 KDKYNFNCNRWLDANEDDNEIVREMTAE 264
Cdd:cd01752     93 GKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 537-628 3.51e-15

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: 73.53  E-value: 3.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  537 HYEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFLSSRSKVFERASKDTFQLEAA-DVGEVYKLRLGHTGEGFGPSWFV 615
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGWYC 81

                           90
                   ....*....|...
gi 2217316121  616 DTVWLRHLVVREV 628
Cdd:cd00113     82 ESITVQALGTKKV 94
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1481-1590 4.60e-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: 73.08  E-value: 4.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1481 LYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQL-DKKKARFEREQNDTFIMEildiAPF-----TKMRIRIDGLGSR 1554
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLrDPEKPIFERGSVDSFLLT----TPFplgelQSIRLWHDNSGLS 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217316121 1555 PEWFLERILLKNMNTGDLTMFYYGDWLSQRKGKKTL 1590
Cdd:cd01752     78 PSWYLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTV 113
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 899-1008 1.58e-14

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: 71.42  E-value: 1.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  899 FSVTIKTGVK-KNAGTDANVFITLFGTQDDTGMTLLKssktnsdkfeRDSIEiFTVETLDLGDLWKVRLGHDNTGKAPGW 977
Cdd:cd01757      3 YHVVIVPSKKlGGSMFTANPWICVSGELGETPPLQIP----------KNSLE-MTFDCQNLGKLTTVQIGHDNSGLLAKW 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217316121  978 FVDWVEVDAPSLGKCMTFPCGRWLAKNEDDG 1008
Cdd:cd01757     72 LVEYVMVRNEITGHTYKFPCGRWLGEGVDDG 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
901-1004 1.33e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 1.33e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   901 VTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSdkFERDSIEIFTVET-LDLGDLWKVRLGHDNtgKAPGWFV 979
Cdd:smart00308    5 VTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGI--FARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 2217316121   980 DWVEVDAPSLGKCMTFPCGRWLAKN 1004
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 538-621 1.84e-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: 68.61  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFLSSRSKVFERASKDTFQL-EAADVGEVYKLRLGHTGEGFGPSWFVD 616
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWFLK 80


                   ....*
gi 2217316121  617 TVWLR 621
Cdd:pfam01477   81 SITVE 85
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1482-1591 3.07e-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: 3.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1482 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWFLE 1560
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEWFLK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217316121 1561 RILL-KNMNTGDLTMFYYGDWLSQ-RKGKKTLV 1591
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGsKKYKETRV 113
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
153-249 7.47e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 66.51  E-value: 7.47e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   153 VWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNKW-FKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGsgWHLERMT 230
Cdd:smart00308    7 VTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGiFARGSTYEFTFDVDeDFGELGAVKIKNEHRHPE--WFLKSIT 84

                            90
                    ....*....|....*....
gi 2217316121   231 LMNTLNKDKYNFNCNRWLD 249
Cdd:smart00308   85 VKDLPTGGKYHFPCNSWVY 103
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1030-1148 2.04e-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: 65.53  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1030 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKReqkqfFERKSASRFIVELE-DVGEIIeKIRIGHNNTGMN 1108
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD-----FERGAEDSFEIDTDwDVGAIL-KINLHWDNNGLS 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121 1109 PGWHCSHVdirRLLPDKDGAETLTFPCDRWLATSEDDKKT 1148
Cdd:pfam01477   75 DEWFLKSI---TVEVPGETGGKYTFPCNSWVYGSKKYKET 111
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 746-862 4.25e-12

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: 64.48  E-value: 4.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  746 YEVQVVTGN-VPKAGTDANVYLTIYGEeYGDTGERPLKKsdksNKFEqgqtdtFTIYAIDLGALTKIRIRHDNTGNRAGW 824
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGE-LGETPPLQIPK----NSLE------MTFDCQNLGKLTTVQIGHDNSGLLAKW 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217316121  825 FLDRIditDMNNEI---TYYFPCQRWLA-----VEEDDGQLSRELL 862
Cdd:cd01757     72 LVEYV---MVRNEItghTYKFPCGRWLGegvddGNGEDGSLERVLV 114
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
746-848 9.01e-12

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 63.43  E-value: 9.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   746 YEVQVVTGNVPKAGTDANVYLTIYGEEyGDTGERPLKKSDKsNKFEQGQTDTFTI-YAIDLGALTKIRIRHDNtgNRAGW 824
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAE-GDGKESKLDYLFK-GIFARGSTYEFTFdVDEDFGELGAVKIKNEH--RHPEW 78

                            90       100
                    ....*....|....*....|....
gi 2217316121   825 FLDRIDITDMNNEITYYFPCQRWL 848
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWV 102
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 1609-1715 1.25e-11

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: 63.71  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1609 YTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQS------ANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKG 1682
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAwgglmgAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217316121 1683 IFPGWHLSYVDVK---DNSRDETFHFQCDCWLSKSE 1715
Cdd:cd01754     83 NHPGWYVNYVEVTqagQHAPCMQHLFAVEQWLATDE 118
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1029-1139 1.36e-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.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 63.13  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1029 PYEITLYTSDVFAAGTDANIFIIIYGcdAVCTQQKYLCTNKreqKQFFERKSASRFIVELE-DVGeIIEKIRIGHNNTGM 1107
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYG--ENGNSSDIPILDG---PGSFERGSTDTFQIDLKlDIG-DITKVYLRRDGSGL 75

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121 1108 NPGWHCSHVDIRRLlpdkDGAETLTFPCDRWL 1139
Cdd:cd00113     76 SDGWYCESITVQAL----GTKKVYTFPVNRWV 103
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 407-512 2.37e-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: 62.33  E-value: 2.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  407 RYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLvsdnNLKDYFERGRVDEFTLE-TLNIGNINRLVIGHDSTGMHA 485
Cdd:cd01753      2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLD----RPGYDFERGAVDEYKVKvPEDLGELLLVRLRKRKYLLFD 77

                           90       100
                   ....*....|....*....|....*..
gi 2217316121  486 SWFLGSVQIRVPRQGKqYTFPANRWLD 512
Cdd:cd01753     78 AWFCNYITVTGPGGDE-YHFPCYRWIE 103
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 275-385 2.46e-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: 62.33  E-value: 2.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  275 ARYHVTVCTGELEGAGTDANVYLCLfgdVGDTGERLLYNCRNNTDLFEKGNADEFTIESVT-MRNVRRVRIRHDGKGSGS 353
Cdd:cd01753      1 AEYKVTVATGSSLFAGTDDYIYLTL---VGTAGESEKQLLDRPGYDFERGAVDEYKVKVPEdLGELLLVRLRKRKYLLFD 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121  354 GWYLDRVLVREegqPESDNVEFPCLRWLDKDK 385
Cdd:cd01753     78 AWFCNYITVTG---PGGDEYHFPCYRWIEGYG 106
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1351-1466 3.15e-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: 62.29  E-value: 3.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwLDYPrGKRGFSRGSVEEFYVAGL-DVGIIKKIELGHDGASPESCW 1429
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHH-LRDP-EKPIFERGSVDSFLLTTPfPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121 1430 -----LVEELclavPTQGTKYMLnCNCWLAKDRGDGITSRVF 1466
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 ...
 745-858 3.33e-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: 3.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  745 TYEVQVVTGNVPKAGTDANVYLTIYGEEygdtGERPLKKSDKSNK-FEQGQTDTFTIYA-IDLGALTKIRIRHDNTGNRA 822
Cdd:cd01753      2 EYKVTVATGSSLFAGTDDYIYLTLVGTA----GESEKQLLDRPGYdFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFD 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217316121  823 GWFLDRIDITDMNNEiTYYFPCQRWLaveEDDGQLS 858
Cdd:cd01753     78 AWFCNYITVTGPGGD-EYHFPCYRWI---EGYGTLE 109
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 898-1011 4.54e-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: 61.56  E-value: 4.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  898 TFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNsdkFERDSIEIFTVE-TLDLGDLWKVRLGHDNTGKAPG 976
Cdd:cd01753      2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD---FERGAVDEYKVKvPEDLGELLLVRLRKRKYLLFDA 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217316121  977 WFVDWVEVDAPSlGKCMTFPCGRWLaknEDDGSII 1011
Cdd:cd01753     79 WFCNYITVTGPG-GDEYHFPCYRWI---EGYGTLE 109
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
275-384 1.12e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 59.96  E-value: 1.12e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   275 ARYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCRNNtdLFEKGNADEFTIE-SVTMRNVRRVRIRHDGKgsGS 353
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKG--IFARGSTYEFTFDvDEDFGELGAVKIKNEHR--HP 76

                            90       100       110
                    ....*....|....*....|....*....|.
gi 2217316121   354 GWYLDRVLVreEGQPESDNVEFPCLRWLDKD 384
Cdd:smart00308   77 EWFLKSITV--KDLPTGGKYHFPCNSWVYPD 105
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 408-520 2.29e-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: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  408 YHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNNLK----DYFERGRVDEFT--LETLNiGNINRLVIGHDST 481
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMgaghDYFERGNLDRFSgrGPCLP-SPPCWMNLTSDGT 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121  482 GMHASWFLGSVQIRVPRQGK---QYTFPANRWLDKNQADGRL 520
Cdd:cd01754     82 GNHPGWYVNYVEVTQAGQHApcmQHLFAVEQWLATDESPYML 123
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 898-1005 4.09e-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: 59.48  E-value: 4.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  898 TFSVTIKTGVKKNAGTDANVFITLFGTQDDTG-MTLLKS----SKTNSDKFERDSIEIFTVETLDL-GDLWKVRLGHDNT 971
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLrIANLEAwgglMGAGHDYFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217316121  972 GKAPGWFVDWVEVDAPSLGK-CMT--FPCGRWLAKNE 1005
Cdd:cd01754     82 GNHPGWYVNYVEVTQAGQHApCMQhlFAVEQWLATDE 118
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 277-388 7.39e-10

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: 57.93  E-value: 7.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  277 YHVTVCTGE-LEGAGTDANVYLCLFGDVGDTGERLLyncrnntdlfeKGNADEFTIESVTMRNVRRVRIRHDGKGSGSGW 355
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQI-----------PKNSLEMTFDCQNLGKLTTVQIGHDNSGLLAKW 71

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217316121  356 YLDRVLVREEgqPESDNVEFPCLRWLDKDKDDG 388
Cdd:cd01757     72 LVEYVMVRNE--ITGHTYKFPCGRWLGEGVDDG 102
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 408-521 1.29e-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: 57.55  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  408 YHISLKTGD-VSGASTDSRVYIKLYGDKSDTikQVLLVSDNNLkdyfergrvdEFTLETLNIGNINRLVIGHDSTGMHAS 486
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGET--PPLQIPKNSL----------EMTFDCQNLGKLTTVQIGHDNSGLLAK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217316121  487 WFLGSVQIRVPRQGKQYTFPANRWL-----DKNQADGRLE 521
Cdd:cd01757     71 WLVEYVMVRNEITGHTYKFPCGRWLgegvdDGNGEDGSLE 110
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1351-1466 1.37e-09

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: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKR-IWLDYPRgkrgFSRGSVEEFYV-AGLDVGIIKKIELGHDGASPESC 1428
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLeITLDNPD----FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDE 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217316121 1429 WLVEELCLAVP-TQGTKYMLNCNCWLAKDRgDGITSRVF 1466
Cdd:pfam01477   77 WFLKSITVEVPgETGGKYTFPCNSWVYGSK-KYKETRVF 114
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 19-121 1.59e-09

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: 56.93  E-value: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   19 TYIVTVFTGDVRGAGTKSKIYLVMYGARGNKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGVNRGWFC 98
Cdd:cd01753      2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDAWFC 81

                           90       100
                   ....*....|....*....|...
gi 2217316121   99 EKVVILCPFTGIqQTFPCSNWLD 121
Cdd:cd01753     82 NYITVTGPGGDE-YHFPCYRWIE 103
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 745-858 3.09e-09

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: 56.78  E-value: 3.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  745 TYEVQVVTGNVPKAGTDANVYLTIYGEEyGDTG-----ER--PLKKSDkSNKFEQGQTDTFTIYAIDL-GALTKIRIRHD 816
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDAD-GPGLrianlEAwgGLMGAG-HDYFERGNLDRFSGRGPCLpSPPCWMNLTSD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217316121  817 NTGNRAGWFLDRIDITDMNNEI---TYYFPCQRWLAVEEDDGQLS 858
Cdd:cd01754     80 GTGNHPGWYVNYVEVTQAGQHApcmQHLFAVEQWLATDESPYMLT 124
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 1182-1298 4.59e-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: 56.01  E-value: 4.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1182 VLYSVQIFTGN-IPGAGTDAKVYITIYGDLGDTGERYLGKsenrtNKFErgtadtFIIEAADLGVIYKIKLRHDNSKWCA 1260
Cdd:cd01757      1 MPYHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQIPK-----NSLE------MTFDCQNLGKLTTVQIGHDNSGLLA 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217316121 1261 DWYVEKVEIWNDTNEDEFLFLCGRWLS-----LKKEDGRLERL 1298
Cdd:cd01757     70 KWLVEYVMVRNEITGHTYKFPCGRWLGegvddGNGEDGSLERV 112
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1609-1713 7.79e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.95  E-value: 7.79e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1609 YTVAVKTSDILGAGTDANVFIIIFGENGDSGtLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKgiFPGWH 1688
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGK-ESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEWF 79

                            90       100
                    ....*....|....*....|....*
gi 2217316121  1689 LSYVDVKDNSRDETFHFQCDCWLSK 1713
Cdd:smart00308   80 LKSITVKDLPTGGKYHFPCNSWVYP 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1184-1289 1.23e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.18  E-value: 1.23e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1184 YSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENrtNKFERGTADTFIIE-AADLGVIYKIKLRHDNSKwcADW 1262
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFK--GIFARGSTYEFTFDvDEDFGELGAVKIKNEHRH--PEW 78

                            90       100
                    ....*....|....*....|....*..
gi 2217316121  1263 YVEKVEIWNDTNEDEFLFLCGRWLSLK 1289
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
20-123 3.95e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 53.03  E-value: 3.95e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121    20 YIVTVFTGDVRGAGTKSKIYLVMYGARG-NKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGvnRGWFC 98
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGdGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHRH--PEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 2217316121    99 EKVVILCPFTGIQQTFPCSNWLDEK 123
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
406-514 6.62e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 52.26  E-value: 6.62e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   406 FRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLlvsDNNLKDYFERGRVDEFTLET-LNIGNINRLVIGHDSTgmH 484
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKL---DYLFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEHR--H 75

                            90       100       110
                    ....*....|....*....|....*....|
gi 2217316121   485 ASWFLGSVQIRVPRQGKQYTFPANRWLDKN 514
Cdd:smart00308   76 PEWFLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 1183-1269 7.88e-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: 7.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1183 LYSVQIFTGNIPGAGTDAKVYITIYGDLGDTG-----ERYLGKSENRTNKFERGTADTFIIEAADL-GVIYKIKLRHDNS 1256
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLrianlEAWGGLMGAGHDYFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                           90
                   ....*....|...
gi 2217316121 1257 KWCADWYVEKVEI 1269
Cdd:cd01754     82 GNHPGWYVNYVEV 94
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 19-120 1.03e-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: 52.54  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121   19 TYIVTVFTGDVRGAGTKSKIYLVMYGARGNKNSGKiFLE--GGV-------FDRGRTDIFHIELAVLLSPLSRVSVGHGN 89
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIA-NLEawGGLmgaghdyFERGNLDRFSGRGPCLPSPPCWMNLTSDG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217316121   90 VGVNRGWFCEKVVILCpfTGI-----QQTFPCSNWL 120
Cdd:cd01754     81 TGNHPGWYVNYVEVTQ--AGQhapcmQHLFAVEQWL 114
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 1611-1720 1.23e-07

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


Pssm-ID: 238855  Cd Length: 114  Bit Score: 51.77  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1611 VAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNtdtfnfpdmlsLGHLCKLRVWHDNKGIFPGWHLS 1690
Cdd:cd01757      6 VIVPSKKLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFDCQN-----------LGKLTTVQIGHDNSGLLAKWLVE 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217316121 1691 YVDVKDNSRDETFHFQCDCWLSKSEGDGQT 1720
Cdd:cd01757     75 YVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 153-252 2.02e-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: 51.16  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  153 VWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNKWFKPGIIEKFRIELP-DLGRFYKIRVWHDKRSSGSGWHLERMTL 231
Cdd:cd01753      7 VATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVPeDLGELLLVRLRKRKYLLFDAWFCNYITV 86

                           90       100
                   ....*....|....*....|.
gi 2217316121  232 mNTLNKDKYNFNCNRWLDANE 252
Cdd:cd01753     87 -TGPGGDEYHFPCYRWIEGYG 106
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 277-390 5.87e-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: 50.23  E-value: 5.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  277 YHVTVCTGELEGAGTDANVYLCLFGDVGDTG-----ERLLYNCRNNTDLFEKGNADEFTIESVTMRN-VRRVRIRHDGKG 350
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLrianlEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSpPCWMNLTSDGTG 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217316121  351 SGSGWYLDRVLVREEGQPESDNVE-FPCLRWLDKDKDDGQL 390
Cdd:cd01754     83 NHPGWYVNYVEVTQAGQHAPCMQHlFAVEQWLATDESPYML 123
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1182-1287 5.94e-07

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


Pssm-ID: 238851  Cd Length: 113  Bit Score: 49.61  E-value: 5.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1182 VLYSVQIFTGNIPGAGTDAKVYITIygdLGDTGERYLGKSENRTNKFERGTADTFIIEA-ADLGVIYKIKLRHDNSKWCA 1260
Cdd:cd01753      1 AEYKVTVATGSSLFAGTDDYIYLTL---VGTAGESEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFD 77

                           90       100
                   ....*....|....*....|....*..
gi 2217316121 1261 DWYVEKVEIwNDTNEDEFLFLCGRWLS 1287
Cdd:cd01753     78 AWFCNYITV-TGPGGDEYHFPCYRWIE 103
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 745-848 8.02e-07

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: 49.38  E-value: 8.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  745 TYEVQVVTGNVPKAGTDANVYLTIYGEEyGDTGERPLKKSdksnkFEQGQTDTFTIYAIDLGALTKIRIRhdNTGNRAGW 824
Cdd:cd02899      2 TYTASVQTGKDKEAGTNGTIEITLLGSS-GRSNPKTLSQG-----FYPGSLKRIRFRAADVGDINAIILS--NTALNDPW 73

                           90       100
                   ....*....|....*....|....
gi 2217316121  825 FLDRIDITDMNNEItYYFPCQRWL 848
Cdd:cd02899     74 YCDYVRIKSEDGKV-FAFNVKRWI 96
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1608-1718 1.22e-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: 48.84  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1608 SYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKqsaNWNK-FERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPG 1686
Cdd:cd01753      2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLD---RPGYdFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDA 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121 1687 WHLSYVDVKDNSRDEtFHFQCDCWLsksEGDG 1718
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 ...
 1030-1143 1.36e-06

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: 49.08  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1030 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCT---NKREQKQFFERKSASRFIVELEDVGEIIEKIRIGHNNTG 1106
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAwggLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217316121 1107 MNPGWHCSHVDIRRLLPDKDGAETLtFPCDRWLATSE 1143
Cdd:cd01754     83 NHPGWYVNYVEVTQAGQHAPCMQHL-FAVEQWLATDE 118
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1030-1150 5.37e-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: 46.92  E-value: 5.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1030 YEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKReqkqfFERKSASRFIVEL-EDVGEIIeKIRIGHNNTGMN 1108
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD-----FERGAVDEYKVKVpEDLGELL-LVRLRKRKYLLF 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217316121 1109 PGWHCSHVDIRRLlpdkdGAETLTFPCDRWLatseDDKKTIR 1150
Cdd:cd01753     77 DAWFCNYITVTGP-----GGDEYHFPCYRWI----EGYGTLE 109
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1351-1456 6.86e-06

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 46.48  E-value: 6.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIwlDYPRGKRGFSRGSVEEFYVAG-LDVGIIKKIELGHDGASPEscW 1429
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESK--LDYLFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEHRHPE--W 78

                            90       100
                    ....*....|....*....|....*..
gi 2217316121  1430 LVEELCLAVPTQGTKYMLNCNCWLAKD 1456
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 1183-1286 1.28e-05

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: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1183 LYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLgksenrTNKFERGTADTFIIEAADLGVIYKIKLRhdNSKWCADW 1262
Cdd:cd02899      2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTL------SQGFYPGSLKRIRFRAADVGDINAIILS--NTALNDPW 73

                           90       100
                   ....*....|....*....|....
gi 2217316121 1263 YVEKVEIWNDTNEdEFLFLCGRWL 1286
Cdd:cd02899     74 YCDYVRIKSEDGK-VFAFNVKRWI 96
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 538-614 2.05e-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: 45.38  E-value: 2.05e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFLSSRSKVFERASKDTFQLEA-ADVGEVYKLRLGHTGEGFGPSWF 614
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFDAWF 80
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1482-1582 2.31e-05

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 44.94  E-value: 2.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  1482 YEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDK-KKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGlgSRPEWFL 1559
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYlFKGIFARGSTYEFTFDVdEDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|...
gi 2217316121  1560 ERILLKNMNTGDLTMFYYGDWLS 1582
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVY 103
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1480-1591 8.78e-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: 43.45  E-value: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1480 VLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEI-LDIAPFTKMRIRIDGLGSRPEWF 1558
Cdd:cd01753      1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFDAWF 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217316121 1559 LERILLKNMNtGDLTMFYYGDWLSqrkGKKTLV 1591
Cdd:cd01753     81 CNYITVTGPG-GDEYHFPCYRWIE---GYGTLE 109
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 538-618 1.03e-04

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


Pssm-ID: 238852  Cd Length: 129  Bit Score: 43.68  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKT-EVLFLSSRSKV-------FERASKDTFQLEAADV-GEVYKLRLGHTGEG 608
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGlRIANLEAWGGLmgaghdyFERGNLDRFSGRGPCLpSPPCWMNLTSDGTG 82

                           90
                   ....*....|
gi 2217316121  609 FGPSWFVDTV 618
Cdd:cd01754     83 NHPGWYVNYV 92
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 77-133 2.47e-04

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: 42.53  E-value: 2.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316121   77 LSPLSRVSVGHGNVGVNRGWFCEKVVILCPFTGIQQTFPCSNWL-----DEKKADGLIERQL 133
Cdd:cd01757     52 LGKLTTVQIGHDNSGLLAKWLVEYVMVRNEITGHTYKFPCGRWLgegvdDGNGEDGSLERVL 113
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 1030-1141 8.40e-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: 8.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1030 YEITLYTSDVFAAGTDANIFIIIYGCDAVctqqkylcTNKREQKQFFERKSASRFIVELEDVGEIIEKIRIghnNTGMNP 1109
Cdd:cd02899      3 YTASVQTGKDKEAGTNGTIEITLLGSSGR--------SNPKTLSQGFYPGSLKRIRFRAADVGDINAIILS---NTALND 71

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217316121 1110 GWHCSHVDIRrllpdKDGAETLTFPCDRWLAT 1141
Cdd:cd02899     72 PWYCDYVRIK-----SEDGKVFAFNVKRWIGY 98
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1351-1453 2.05e-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: 39.60  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1351 YYVSVTTGKHKDAATDSRAFIFLIGEDDErSKRIWLDYPrgKRGFSRGSVEEFYV-AGLDVGIIKKIELGHDGASPESCW 1429
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGE-SEKQLLDRP--GYDFERGAVDEYKVkVPEDLGELLLVRLRKRKYLLFDAW 79

                           90       100
                   ....*....|....*....|....
gi 2217316121 1430 LVEELCLAVPtQGTKYMLNCNCWL 1453
Cdd:cd01753     80 FCNYITVTGP-GGDEYHFPCYRWI 102
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 898-1003 2.37e-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: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  898 TFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSktnsdkFERDSIEIFTVETLDLGDLWKVRLGhdNTGKAPGW 977
Cdd:cd02899      2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG------FYPGSLKRIRFRAADVGDINAIILS--NTALNDPW 73

                           90       100
                   ....*....|....*....|....*.
gi 2217316121  978 FVDWVEVDAPSlGKCMTFPCGRWLAK 1003
Cdd:cd02899     74 YCDYVRIKSED-GKVFAFNVKRWIGY 98
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 538-618 4.41e-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: 38.60  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFLSsrsKVFERASKDTFQLEAADVGEVYKLRLGHTGEgfGPSWFVDT 617
Cdd:cd02899      3 YTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLS---QGFYPGSLKRIRFRAADVGDINAIILSNTAL--NDPWYCDY 77


                   .
gi 2217316121  618 V 618
Cdd:cd02899     78 V 78
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 1349-1462 4.73e-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: 38.67  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121 1349 IPYYVSVTTGKHKDAA-TDSRAFIFLIGEDDErSKRIWLdyPRGkrgfsrgsVEEFYVAGLDVGIIKKIELGHDGASPES 1427
Cdd:cd01757      1 MPYHVVIVPSKKLGGSmFTANPWICVSGELGE-TPPLQI--PKN--------SLEMTFDCQNLGKLTTVQIGHDNSGLLA 69

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217316121 1428 CWLVEELCLAVPTQGTKYMLNCNCWLAKDRGDGIT 1462
Cdd:cd01757     70 KWLVEYVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 538-621 6.02e-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: 38.29  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316121  538 YEVEIWTGD-VGGAGTSARVYMQIYGEKGKTEVLFLssRSKVFEraskdtFQLEAADVGEVYKLRLGHTGEGFGPSWFVD 616
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQI--PKNSLE------MTFDCQNLGKLTTVQIGHDNSGLLAKWLVE 74


                   ....*
gi 2217316121  617 TVWLR 621
Cdd:cd01757     75 YVMVR 79
 
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.
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