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Conserved domains on  [gi|1034662933|ref|XP_016869647|]
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oxygen-regulated protein 1 isoform X7 [Homo sapiens]

Protein Classification

phospholipase C( domain architecture ID 10205339)

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 ...
 707-829 6.46e-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: 176.98  E-value: 6.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 707 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSkNNEIKFQRGQVDIFSIKAVSLGKLKKVLISHDGTGPGNG 786
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034662933 787 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 829
Cdd:cd01756    80 WFLDKVEIR--EPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 442-561 4.35e-49

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: 168.89  E-value: 4.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 442 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSQYW 521
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034662933 522 YCEQVIVREPGTTSESIFTCQRWLPFmSQGIIHSEIELYL 561
Cdd:cd01756    81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 134-255 7.90e-44

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 466998  Cd Length: 128  Bit Score: 154.66  E-value: 7.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 134 VVLLATSL-CQALCLQPDGSCTGVGSQSEK-SYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKIKKN 211
Cdd:cd23312     5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034662933 212 lKNASISLESTKSPGLFVGLQSDGQAKPMIYTKDE-NVCFYPQVI 255
Cdd:cd23312    85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 581-695 9.23e-34

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: 125.75  E-value: 9.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 581 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILG-SGKHQLFNPNTADIFKINLKDIGEIYKIRIGHDNTGKNPRWYL 659
Cdd:cd01756     3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034662933 660 EEVRLENIATYELFCLPVDSWIAENENDGDLWKEIP 695
Cdd:cd01756    83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
beta-trefoil_FGF super family cl00060
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 31-126 1.16e-29

FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily; The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


The actual alignment was detected with superfamily member cd23312:

Pssm-ID: 469595  Cd Length: 128  Bit Score: 114.21  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  31 KEGVFDVIFNKRNICIFQSHEMRHLSLALDNGIVTGMVSGEATTELRVLYQPNRCALLESALVPGHTVVFDRHGKIADAS 110
Cdd:cd23312    34 KFAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQPDRSVTLESVKNPGQFVGFNPDGKPRDPR 113

                          90
                  ....*....|....*.
gi 1034662933 111 SAGYAnLSKEFVIFVK 126
Cdd:cd23312   114 GTGDG-PNAQFYVYVK 128
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 318-432 1.36e-25

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


The actual alignment was detected with superfamily member cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 102.25  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 318 WKVLVLTG---NTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFLPGHEDEFQVEIRNTGNIYKIRIGHDGTSEQPEWNL 394
Cdd:cd01756     3 YEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034662933 395 QRVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPVV 432
Cdd:cd01756    83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 707-829 6.46e-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: 176.98  E-value: 6.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 707 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSkNNEIKFQRGQVDIFSIKAVSLGKLKKVLISHDGTGPGNG 786
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034662933 787 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 829
Cdd:cd01756    80 WFLDKVEIR--EPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 442-561 4.35e-49

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: 168.89  E-value: 4.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 442 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSQYW 521
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034662933 522 YCEQVIVREPGTTSESIFTCQRWLPFmSQGIIHSEIELYL 561
Cdd:cd01756    81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 134-255 7.90e-44

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 154.66  E-value: 7.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 134 VVLLATSL-CQALCLQPDGSCTGVGSQSEK-SYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKIKKN 211
Cdd:cd23312     5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034662933 212 lKNASISLESTKSPGLFVGLQSDGQAKPMIYTKDE-NVCFYPQVI 255
Cdd:cd23312    85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 581-695 9.23e-34

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: 125.75  E-value: 9.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 581 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILG-SGKHQLFNPNTADIFKINLKDIGEIYKIRIGHDNTGKNPRWYL 659
Cdd:cd01756     3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034662933 660 EEVRLENIATYELFCLPVDSWIAENENDGDLWKEIP 695
Cdd:cd01756    83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 31-126 1.16e-29

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 114.21  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  31 KEGVFDVIFNKRNICIFQSHEMRHLSLALDNGIVTGMVSGEATTELRVLYQPNRCALLESALVPGHTVVFDRHGKIADAS 110
Cdd:cd23312    34 KFAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQPDRSVTLESVKNPGQFVGFNPDGKPRDPR 113

                          90
                  ....*....|....*.
gi 1034662933 111 SAGYAnLSKEFVIFVK 126
Cdd:cd23312   114 GTGDG-PNAQFYVYVK 128
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 318-432 1.36e-25

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


Pssm-ID: 238854  Cd Length: 120  Bit Score: 102.25  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 318 WKVLVLTG---NTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFLPGHEDEFQVEIRNTGNIYKIRIGHDGTSEQPEWNL 394
Cdd:cd01756     3 YEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034662933 395 QRVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPVV 432
Cdd:cd01756    83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 709-823 1.06e-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: 85.18  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 709 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNneiKFQRGQVDIFSIKA-VSLGKLKKVLISHDGTGPGNGW 787
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP---DFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034662933 788 FLGSIVVKSEDEDSSeEVLFLCNRWLDEYQDDGKTQ 823
Cdd:pfam01477  78 FLKSITVEVPGETGG-KYTFPCNSWVYGSKKYKETR 112
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 444-545 7.09e-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: 74.39  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 444 YQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMqvKFQRGQIDKFQV-AAVSLGKLQKVLLRCEASDKSQYWY 522
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP--DFERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWF 78

                          90       100
                  ....*....|....*....|....
gi 1034662933 523 CEQVIVREPGTT-SESIFTCQRWL 545
Cdd:pfam01477  79 LKSITVEVPGETgGKYTFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
581-684 3.76e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 69.21  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  581 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILGSGKHQLFNPNTADIFKINLK-DIGEIYKIRIGHDNtgKNPRWYL 659
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDeDFGELGAVKIKNEH--RHPEWFL 80

                           90       100
                   ....*....|....*....|....*
gi 1034662933  660 EEVRLENIATYELFCLPVDSWIAEN 684
Cdd:smart00308  81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 581-689 4.80e-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: 66.30  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 581 WKVTIVTGDLENAGTTATVFLYVYGE--TKCSGPIILGSGKhqlFNPNTADIFKINLK-DIGEIYKIRIGHDNTGKNPRW 657
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKvgESAQLEITLDNPD---FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEW 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034662933 658 YLEEVRLENIATYE---LFClpVDSWIAENENDGD 689
Cdd:pfam01477  78 FLKSITVEVPGETGgkyTFP--CNSWVYGSKKYKE 110
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
709-816 5.45e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 57.27  E-value: 5.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  709 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRrlHQSKNNEIKFQRGQVDIFSIK-AVSLGKLKKVLISHDGTGPgnGW 787
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKES--KLDYLFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHP--EW 78

                           90       100
                   ....*....|....*....|....*....
gi 1034662933  788 FLGSIVVKSEDEDSseEVLFLCNRWLDEY 816
Cdd:smart00308  79 FLKSITVKDLPTGG--KYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 318-418 1.33e-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: 56.29  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 318 WKVLVLTGNT---GTQANVTLWVYGDKGVTGPISLRKDSSEqlFLPGHEDEFQVEIR-NTGNIYKIRIGHDGTSEQPEWN 393
Cdd:pfam01477   1 YQVKVVTGDElgaGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                          90       100
                  ....*....|....*....|....*.
gi 1034662933 394 LQRVT-MQHMKSKKILDFAANVWLSR 418
Cdd:pfam01477  79 LKSITvEVPGETGGKYTFPCNSWVYG 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
443-545 2.52e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 52.64  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  443 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKsNMQVKFQRGQIDKFQVA-AVSLGKLQKVLLRCEASDKSqyW 521
Cdd:smart00308   2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDY-LFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHPE--W 78

                           90       100
                   ....*....|....*....|....
gi 1034662933  522 YCEQVIVREPGTTSESIFTCQRWL 545
Cdd:smart00308  79 FLKSITVKDLPTGGKYHFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
318-417 2.06e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 41.47  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  318 WKVLVLTGN---TGTQANVTLWVYG---DKGVTGPISLRKdsseQLFLPG--HEDEFQVEIrNTGNIYKIRIGHDGTseQ 389
Cdd:smart00308   3 YKVTVTTGGldfAGTTASVSLSLVGaegDGKESKLDYLFK----GIFARGstYEFTFDVDE-DFGELGAVKIKNEHR--H 75

                           90       100
                   ....*....|....*....|....*...
gi 1034662933  390 PEWNLQRVTMQHMKSKKILDFAANVWLS 417
Cdd:smart00308  76 PEWFLKSITVKDLPTGGKYHFPCNSWVY 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 ...
 707-829 6.46e-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: 176.98  E-value: 6.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 707 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSkNNEIKFQRGQVDIFSIKAVSLGKLKKVLISHDGTGPGNG 786
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034662933 787 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 829
Cdd:cd01756    80 WFLDKVEIR--EPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 442-561 4.35e-49

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: 168.89  E-value: 4.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 442 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSQYW 521
Cdd:cd01756     1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034662933 522 YCEQVIVREPGTTSESIFTCQRWLPFmSQGIIHSEIELYL 561
Cdd:cd01756    81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 134-255 7.90e-44

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 154.66  E-value: 7.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 134 VVLLATSL-CQALCLQPDGSCTGVGSQSEK-SYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKIKKN 211
Cdd:cd23312     5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034662933 212 lKNASISLESTKSPGLFVGLQSDGQAKPMIYTKDE-NVCFYPQVI 255
Cdd:cd23312    85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 581-695 9.23e-34

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: 125.75  E-value: 9.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 581 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILG-SGKHQLFNPNTADIFKINLKDIGEIYKIRIGHDNTGKNPRWYL 659
Cdd:cd01756     3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034662933 660 EEVRLENIATYELFCLPVDSWIAENENDGDLWKEIP 695
Cdd:cd01756    83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 31-126 1.16e-29

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 114.21  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  31 KEGVFDVIFNKRNICIFQSHEMRHLSLALDNGIVTGMVSGEATTELRVLYQPNRCALLESALVPGHTVVFDRHGKIADAS 110
Cdd:cd23312    34 KFAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQPDRSVTLESVKNPGQFVGFNPDGKPRDPR 113

                          90
                  ....*....|....*.
gi 1034662933 111 SAGYAnLSKEFVIFVK 126
Cdd:cd23312   114 GTGDG-PNAQFYVYVK 128
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 318-432 1.36e-25

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


Pssm-ID: 238854  Cd Length: 120  Bit Score: 102.25  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 318 WKVLVLTG---NTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFLPGHEDEFQVEIRNTGNIYKIRIGHDGTSEQPEWNL 394
Cdd:cd01756     3 YEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034662933 395 QRVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPVV 432
Cdd:cd01756    83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 708-829 9.56e-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: 94.26  E-value: 9.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 708 LYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNNeiKFQRGQVDIFSIK-AVSLGKLKKVLISHDGTGPGNG 786
Cdd:cd01752     2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKP--IFERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034662933 787 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 829
Cdd:cd01752    80 WYLSRVIVR--DLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 583-696 7.34e-22

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: 91.57  E-value: 7.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 583 VTIVTGDLENAGTTATVFLYVYGETKCSGPIILGSGKHQLFNPNTADIFKIN-LKDIGEIYKIRIGHDNTGKNPRWYLEE 661
Cdd:cd01752     5 VTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSWYLSR 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034662933 662 VRLENIATYELFCLPVDSWIAENENDGDLWKEIPI 696
Cdd:cd01752    85 VIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 709-823 1.06e-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: 85.18  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 709 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNneiKFQRGQVDIFSIKA-VSLGKLKKVLISHDGTGPGNGW 787
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP---DFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034662933 788 FLGSIVVKSEDEDSSeEVLFLCNRWLDEYQDDGKTQ 823
Cdd:pfam01477  78 FLKSITVEVPGETGG-KYTFPCNSWVYGSKKYKETR 112
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 579-681 1.06e-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: 79.69  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 579 GDWKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILgSGKHQLFNPNTADIFKINLK-DIGEIYKIRIGHDNTGKNPRW 657
Cdd:cd00113     1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPI-LDGPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                          90       100
                  ....*....|....*....|....
gi 1034662933 658 YLEEVRLENIATYELFCLPVDSWI 681
Cdd:cd00113    80 YCESITVQALGTKKVYTFPVNRWV 103
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 443-545 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: 76.93  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 443 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVkFQRGQIDKFQVA-AVSLGKLQKVLLRCEASDKSQYW 521
Cdd:cd01752     2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI-FERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSW 80

                          90       100
                  ....*....|....*....|....
gi 1034662933 522 YCEQVIVREPGTTSESIFTCQRWL 545
Cdd:cd01752    81 YLSRVIVRDLQTGKKWFFLCNDWL 104
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 444-545 7.09e-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: 74.39  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 444 YQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMqvKFQRGQIDKFQV-AAVSLGKLQKVLLRCEASDKSQYWY 522
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP--DFERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWF 78

                          90       100
                  ....*....|....*....|....
gi 1034662933 523 CEQVIVREPGTT-SESIFTCQRWL 545
Cdd:pfam01477  79 LKSITVEVPGETgGKYTFPCNSWV 102
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 317-417 6.98e-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: 71.60  E-value: 6.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 317 EWKVLVLTGN---TGTQANVTLWVYGDKGVTGPISLRKDSSEqlFLPGHEDEFQVEIR-NTGNIYKIRIGHDGTSEQPEW 392
Cdd:cd00113     2 RYTVTIKTGDkkgAGTDSNISLALYGENGNSSDIPILDGPGS--FERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                          90       100
                  ....*....|....*....|....*
gi 1034662933 393 NLQRVTMQHMKSKKILDFAANVWLS 417
Cdd:cd00113    80 YCESITVQALGTKKVYTFPVNRWVL 104
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 320-431 1.93e-14

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 70.38  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 320 VLVLTG---NTGTQANVTLWVYGDKGVTGPISLRkDSSEQLFLPGHEDEFQVEI-RNTGNIYKIRIGHDGTSEQPEWNLQ 395
Cdd:cd01752     5 VTVFTGwrrGAGTTAKVTITLYGAEGESEPHHLR-DPEKPIFERGSVDSFLLTTpFPLGELQSIRLWHDNSGLSPSWYLS 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034662933 396 RVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPV 431
Cdd:cd01752    84 RVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 443-546 3.40e-14

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: 69.68  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 443 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNmqVKFQRGQIDKFQVAA-VSLGKLQKVLLRCEASDKSQYW 521
Cdd:cd00113     2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGP--GSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                          90       100
                  ....*....|....*....|....*
gi 1034662933 522 YCEQVIVREPGTTSESIFTCQRWLP 546
Cdd:cd00113    80 YCESITVQALGTKKVYTFPVNRWVL 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
581-684 3.76e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 69.21  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  581 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILGSGKHQLFNPNTADIFKINLK-DIGEIYKIRIGHDNtgKNPRWYL 659
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDeDFGELGAVKIKNEH--RHPEWFL 80

                           90       100
                   ....*....|....*....|....*
gi 1034662933  660 EEVRLENIATYELFCLPVDSWIAEN 684
Cdd:smart00308  81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 709-824 1.49e-13

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: 67.75  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 709 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQsknNEIKFQRGQVDIFSIKA-VSLGKLKKVLISHDGTGPGNGW 787
Cdd:cd00113     3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILD---GPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034662933 788 FLGSIVVKSedEDSSEEVLFLCNRWLDEYQDDGKTQR 824
Cdd:cd00113    80 YCESITVQA--LGTKKVYTFPVNRWVLGGKWYTSVRS 114
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 581-689 4.80e-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: 66.30  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 581 WKVTIVTGDLENAGTTATVFLYVYGE--TKCSGPIILGSGKhqlFNPNTADIFKINLK-DIGEIYKIRIGHDNTGKNPRW 657
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKvgESAQLEITLDNPD---FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEW 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034662933 658 YLEEVRLENIATYE---LFClpVDSWIAENENDGD 689
Cdd:pfam01477  78 FLKSITVEVPGETGgkyTFP--CNSWVYGSKKYKE 110
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 442-545 4.50e-10

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: 57.70  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 442 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLykSNMQVKFQRGQIDKFQV-AAVSLGKLQKVLLRceasdKSQY 520
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLL--DRPGYDFERGAVDEYKVkVPEDLGELLLVRLR-----KRKY 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034662933 521 -----WYCEQVIVREPGTTsESIFTCQRWL 545
Cdd:cd01753    74 llfdaWFCNYITVTGPGGD-EYHFPCYRWI 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
709-816 5.45e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 57.27  E-value: 5.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  709 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRrlHQSKNNEIKFQRGQVDIFSIK-AVSLGKLKKVLISHDGTGPgnGW 787
Cdd:smart00308   3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKES--KLDYLFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHP--EW 78

                           90       100
                   ....*....|....*....|....*....
gi 1034662933  788 FLGSIVVKSEDEDSseEVLFLCNRWLDEY 816
Cdd:smart00308  79 FLKSITVKDLPTGG--KYHFPCNSWVYPD 105
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 707-816 5.73e-10

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: 57.32  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 707 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNNeikFQRGQVDIFSIKA-VSLGKL------KKVLISHD 779
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD---FERGAVDEYKVKVpEDLGELllvrlrKRKYLLFD 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034662933 780 gtgpgnGWFLGSIVVKSEDEDsseEVLFLCNRWLDEY 816
Cdd:cd01753    78 ------AWFCNYITVTGPGGD---EYHFPCYRWIEGY 105
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 580-688 8.22e-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: 57.16  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 580 DWKVTIVTGD-LENAGTTATVFLYVYGETKCSGPIILgsgkhqlfNPNTADiFKINLKDIGEIYKIRIGHDNTGKNPRWY 658
Cdd:cd01757     2 PYHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQI--------PKNSLE-MTFDCQNLGKLTTVQIGHDNSGLLAKWL 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034662933 659 LEEVRLENIATYELFCLPVDSWIAENENDG 688
Cdd:cd01757    73 VEYVMVRNEITGHTYKFPCGRWLGEGVDDG 102
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 318-418 1.33e-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: 56.29  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 318 WKVLVLTGNT---GTQANVTLWVYGDKGVTGPISLRKDSSEqlFLPGHEDEFQVEIR-NTGNIYKIRIGHDGTSEQPEWN 393
Cdd:pfam01477   1 YQVKVVTGDElgaGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                          90       100
                  ....*....|....*....|....*.
gi 1034662933 394 LQRVT-MQHMKSKKILDFAANVWLSR 418
Cdd:pfam01477  79 LKSITvEVPGETGGKYTFPCNSWVYG 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
443-545 2.52e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 52.64  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  443 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKsNMQVKFQRGQIDKFQVA-AVSLGKLQKVLLRCEASDKSqyW 521
Cdd:smart00308   2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDY-LFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHPE--W 78

                           90       100
                   ....*....|....*....|....
gi 1034662933  522 YCEQVIVREPGTTSESIFTCQRWL 545
Cdd:smart00308  79 FLKSITVKDLPTGGKYHFPCNSWV 102
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 583-681 3.02e-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: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 583 VTIVTGDLENAGTTATVFLYVYGETKCSGPIILgsgkHQLFNPNTADIFKINLKDIGEIYKIRIGhdNTGKNPRWYLEEV 662
Cdd:cd02899     5 ASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTL----SQGFYPGSLKRIRFRAADVGDINAIILS--NTALNDPWYCDYV 78

                          90       100
                  ....*....|....*....|.
gi 1034662933 663 RlenIATYE--LFCLPVDSWI 681
Cdd:cd02899    79 R---IKSEDgkVFAFNVKRWI 96
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 444-547 1.37e-06

Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1.


Pssm-ID: 239228  Cd Length: 109  Bit Score: 47.84  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 444 YQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSnmqvkFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSqyWYC 523
Cdd:cd02899     3 YTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG-----FYPGSLKRIRFRAADVGDINAIILSNTALNDP--WYC 75

                          90       100
                  ....*....|....*....|....*.
gi 1034662933 524 EQVIVREPGTTSeSIFTCQRWL--PF 547
Cdd:cd02899    76 DYVRIKSEDGKV-FAFNVKRWIgyPY 100
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 708-813 1.22e-05

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: 45.61  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 708 LYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNNEIK-----FQRGQVDIFSIKAVSL-GKLKKVLISHDGT 781
Cdd:cd01754     2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGaghdyFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034662933 782 GPGNGWFLGSIVVKSEDEDS-SEEVLFLCNRWL 813
Cdd:cd01754    82 GNHPGWYVNYVEVTQAGQHApCMQHLFAVEQWL 114
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 444-545 2.03e-05

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: 44.45  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 444 YQVDVYTGQ-LKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQrgqidkfqvaAVSLGKLQKVLLRCEASDKSQYWY 522
Cdd:cd01757     3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFD----------CQNLGKLTTVQIGHDNSGLLAKWL 72

                          90       100
                  ....*....|....*....|...
gi 1034662933 523 CEQVIVREPGTTSESIFTCQRWL 545
Cdd:cd01757    73 VEYVMVRNEITGHTYKFPCGRWL 95
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 318-425 1.60e-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: 41.76  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 318 WKVLVLT----GNTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFlpghedefqvEIRNTGNIYKIRIGHDGTSEQPEWN 393
Cdd:cd01757     3 YHVVIVPskklGGSMFTANPWICVSGELGETPPLQIPKNSLEMTF----------DCQNLGKLTTVQIGHDNSGLLAKWL 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034662933 394 LQRVTMQHMKSKKILDFAANVWLSRIQADGDV 425
Cdd:cd01757    73 VEYVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
318-417 2.06e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 41.47  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  318 WKVLVLTGN---TGTQANVTLWVYG---DKGVTGPISLRKdsseQLFLPG--HEDEFQVEIrNTGNIYKIRIGHDGTseQ 389
Cdd:smart00308   3 YKVTVTTGGldfAGTTASVSLSLVGaegDGKESKLDYLFK----GIFARGstYEFTFDVDE-DFGELGAVKIKNEHR--H 75

                           90       100
                   ....*....|....*....|....*...
gi 1034662933  390 PEWNLQRVTMQHMKSKKILDFAANVWLS 417
Cdd:smart00308  76 PEWFLKSITVKDLPTGGKYHFPCNSWVY 103
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 707-822 3.89e-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: 40.98  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 707 VLYEIRIYTGT-MTGAETESNVFINLIGTRGDSGKRrlhQSKNNEIKFqrgqvdIFSIKavSLGKLKKVLISHDGTGPGN 785
Cdd:cd01757     1 MPYHVVIVPSKkLGGSMFTANPWICVSGELGETPPL---QIPKNSLEM------TFDCQ--NLGKLTTVQIGHDNSGLLA 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034662933 786 GWFLGSIVVKSEDEDSSEEvlFLCNRWLDEYQDDGKT 822
Cdd:cd01757    70 KWLVEYVMVRNEITGHTYK--FPCGRWLGEGVDDGNG 104
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 31-124 9.11e-04

FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily; The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466989  Cd Length: 127  Bit Score: 39.87  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933  31 KEGVFDVIFNKRNICIFQSHEmRHLSLALD-NGIVTGMVSGEATTELRVLYQPNRCALLESALVP----GHTVVFDRHGK 105
Cdd:cd00058    30 PYAILELQSVGTGLVRIKGVK-TGRYLAMDkNGKLYGTKKPTEDCVFKETLEENGYNTYSSYKYYhtrkGWYLAIKKNGK 108

                          90
                  ....*....|....*....
gi 1034662933 106 IADASSAGYANLSKEFVIF 124
Cdd:cd00058   109 PKRGKKTKPGQKSTQFLPL 127
beta-trefoil_FGF4 cd23316
FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; ...
 149-238 3.40e-03

FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF4 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467002  Cd Length: 125  Bit Score: 38.32  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 149 PDGSCTGVGSQSEKSYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKiKKNLKNASISLESTKSPGLF 228
Cdd:cd23316    19 PDGRINGVHNENRYSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDECKFK-EILLPNNYNAYESRKYPGMY 97

                          90
                  ....*....|
gi 1034662933 229 VGLQSDGQAK 238
Cdd:cd23316    98 IALSKNGKTK 107
beta-trefoil_FGF3-like cd23305
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The ...
 145-238 9.18e-03

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The FGF3-like family includes FGF3-6. FGF3, also called heparin-binding growth factor 3 (HBGF3), or proto-oncogene Int-2, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal ear development. FGF3 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. FGF5, also called heparin-binding growth factor 5 (HBGF5), or Smag-82, plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle. It functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase. FGF5 interacts with FGFR1 and FGFR2. FGF6, also called heparin secretory-transforming protein 2 (HST-2), or HSTF-2, or heparin-binding growth factor 6 (HBGF6), plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. FGF6 interacts with FGFR1, FGFR2, and FGFR4. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466991  Cd Length: 127  Bit Score: 37.28  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662933 145 LCLQPDGSCTGVGSQSEKSYWKVHKISSGICMFESVKnAQMYLRI-KDGRCDGTGTGDVDCHFK--IKKNLKNASIS-LE 220
Cdd:cd23305    14 LQILPDGSVNGTHEDTEYSWLEIFAVEVGVVGIKGVK-SGLYLCMnKKGKLYGSKEFTDECKFKerLEENHYNTYSSaLY 92

                          90
                  ....*....|....*...
gi 1034662933 221 STKSPGLFVGLQSDGQAK 238
Cdd:cd23305    93 PRRKRGWYVALSKKGRPR 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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