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Conserved domains on  [gi|57283627|emb|CAG28811|]
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NADPH oxidase 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAD_binding_1 super family cl23719
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 103-213 3.52e-19

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


The actual alignment was detected with superfamily member pfam08030:

Pssm-ID: 451503 [Multi-domain]  Cd Length: 149  Bit Score: 80.85  E-value: 3.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57283627   103 KPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYVNIQLYLSQTD-GIQKIIGEKYHALNSR 171
Cdd:pfam08030  28 KKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDASDQSDSSIRSeNFDSLMNEVIGVDFVE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 57283627   172 LFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 213
Cdd:pfam08030 108 FHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
 
Name Accession Description Interval E-value
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
103-213 3.52e-19

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 80.85  E-value: 3.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57283627   103 KPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYVNIQLYLSQTD-GIQKIIGEKYHALNSR 171
Cdd:pfam08030  28 KKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDASDQSDSSIRSeNFDSLMNEVIGVDFVE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 57283627   172 LFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 213
Cdd:pfam08030 108 FHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 88-230 7.14e-11

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 59.63  E-value: 7.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57283627  88 ILPFIQSRNYPKDdwKPYKLRRLYFIWVCRDIQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyha 167
Cdd:cd06186 121 VLPILRDLLRRSS--KTSRTRRVKLVWVVRDREDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------- 178

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57283627 168 lnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 230
Cdd:cd06186 179 -----------------------------VVVCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
 
Name Accession Description Interval E-value
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
103-213 3.52e-19

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 80.85  E-value: 3.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57283627   103 KPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYVNIQLYLSQTD-GIQKIIGEKYHALNSR 171
Cdd:pfam08030  28 KKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDASDQSDSSIRSeNFDSLMNEVIGVDFVE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 57283627   172 LFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 213
Cdd:pfam08030 108 FHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 88-230 7.14e-11

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 59.63  E-value: 7.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57283627  88 ILPFIQSRNYPKDdwKPYKLRRLYFIWVCRDIQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyha 167
Cdd:cd06186 121 VLPILRDLLRRSS--KTSRTRRVKLVWVVRDREDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------- 178

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57283627 168 lnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 230
Cdd:cd06186 179 -----------------------------VVVCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
 
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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