NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958657105|ref|XP_038941370|]
View 

hydroperoxide isomerase ALOXE3 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 2-116 2.07e-58

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: 185.20  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   2 AVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFckDP 81
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLF--DA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958657105  82 WYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPG 116
Cdd:cd01753    79 WFCNYITVTGPGGDEYHFPCYRWIEGYGTLELREG 113
 
Name Accession Description Interval E-value
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 2-116 2.07e-58

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: 185.20  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   2 AVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFckDP 81
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLF--DA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958657105  82 WYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPG 116
Cdd:cd01753    79 WFCNYITVTGPGGDEYHFPCYRWIEGYGTLELREG 113
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 4-108 3.66e-29

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: 109.06  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   4 YRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERfaFFCKDPWY 83
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTDWDVGAILKINLHWDN--NGLSDEWF 78

                          90       100
                  ....*....|....*....|....*..
gi 1958657105  84 CSRICVTTP--DGSVVHFPCYQWIDGY 108
Cdd:pfam01477  79 LKSITVEVPgeTGGKYTFPCNSWVYGS 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
2-108 1.80e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 82.69  E-value: 1.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105    2 AVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGR-DFATGSVQKYKVRCASELGEILLLRLHKERFaffcKD 80
Cdd:smart00308   1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgIFARGSTYEFTFDVDEDFGELGAVKIKNEHR----HP 76

                           90       100
                   ....*....|....*....|....*....
gi 1958657105   81 PWYCSRICV-TTPDGSVVHFPCYQWIDGY 108
Cdd:smart00308  77 EWFLKSITVkDLPTGGKYHFPCNSWVYPD 105
 
Name Accession Description Interval E-value
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 2-116 2.07e-58

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: 185.20  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   2 AVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFckDP 81
Cdd:cd01753     1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLF--DA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958657105  82 WYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPG 116
Cdd:cd01753    79 WFCNYITVTGPGGDEYHFPCYRWIEGYGTLELREG 113
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 4-108 3.66e-29

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: 109.06  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   4 YRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERfaFFCKDPWY 83
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFERGAEDSFEIDTDWDVGAILKINLHWDN--NGLSDEWF 78

                          90       100
                  ....*....|....*....|....*..
gi 1958657105  84 CSRICVTTP--DGSVVHFPCYQWIDGY 108
Cdd:pfam01477  79 LKSITVEVPgeTGGKYTFPCNSWVYGS 105
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
2-108 1.80e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 82.69  E-value: 1.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105    2 AVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGR-DFATGSVQKYKVRCASELGEILLLRLHKERFaffcKD 80
Cdd:smart00308   1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgIFARGSTYEFTFDVDEDFGELGAVKIKNEHR----HP 76

                           90       100
                   ....*....|....*....|....*....
gi 1958657105   81 PWYCSRICV-TTPDGSVVHFPCYQWIDGY 108
Cdd:smart00308  77 EWFLKSITVkDLPTGGKYHFPCNSWVYPD 105
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 3-108 1.81e-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: 69.29  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   3 VYRLCVTTGSYLKAGTLDNIYATLVGTCG-ESPKQKLDRVGRdFATGSVQKYKVRCASELGEILLLRLHKERFAFFckDP 81
Cdd:cd00113     2 RYTVTIKTGDKKGAGTDSNISLALYGENGnSSDIPILDGPGS-FERGSTDTFQIDLKLDIGDITKVYLRRDGSGLS--DG 78

                          90       100
                  ....*....|....*....|....*...
gi 1958657105  82 WYCSRICVTTPDGSVVH-FPCYQWIDGY 108
Cdd:cd00113    79 WYCESITVQALGTKKVYtFPVNRWVLGG 106
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 3-106 3.18e-11

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: 59.88  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   3 VYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRD--FATGSVQKYKVRcASELGEILLLRLHKERFAFFCKd 80
Cdd:cd01756     2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKnkFERGQTDKFTVE-AVDLGKLKKIRIGHDNSGLGAG- 79

                          90       100
                  ....*....|....*....|....*..
gi 1958657105  81 pWYCSRICVTTP-DGSVVHFPCYQWID 106
Cdd:cd01756    80 -WFLDKVEIREPgTGDEYTFPCNRWLD 105
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 4-105 1.63e-10

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: 57.86  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   4 YRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRvgrDFATGSVQKYKVRcASELGEI--LLLRLHKErfaffcKDP 81
Cdd:cd02899     3 YTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQ---GFYPGSLKRIRFR-AADVGDInaIILSNTAL------NDP 72

                          90       100
                  ....*....|....*....|....
gi 1958657105  82 WYCSRICVTTPDGSVVHFPCYQWI 105
Cdd:cd02899    73 WYCDYVRIKSEDGKVFAFNVKRWI 96
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 4-122 1.81e-05

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


Pssm-ID: 238850  Cd Length: 120  Bit Score: 43.80  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657105   4 YRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRD-FATGSVQKYKVRCASELGEILLLRL-HKERfaffCKDP 81
Cdd:cd01752     3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPiFERGSVDSFLLTTPFPLGELQSIRLwHDNS----GLSP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958657105  82 -WYCSRICV---TTPDGSvvHFPCYQWI---DGYCTVElrpgtaRTIC 122
Cdd:cd01752    79 sWYLSRVIVrdlQTGKKW--FFLCNDWLsveEGDGTVE------RTFP 118
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH