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Conserved domains on  [gi|665821293|ref|NP_001287924|]
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NADPH oxidase 4 isoform g [Homo sapiens]

Protein Classification

NADPH oxidase family protein( domain architecture ID 10484952)

NADPH oxidase family protein such as ferric reductase (FRE) family protein similar to AIM14, a probable cell surface metalloreductase that may be involved in iron or copper homeostasis, and NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
295-513 1.49e-26

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: 107.01  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 295 SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLLPP------- 364
Cdd:cd06186   10 SDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALKSPgggvslk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 365 ---------SSQDSE----------------ILPFIQSRNYPKDdwKPYKLRRLYFIWVCRDIQSFRWFADLLCMlhnkf 419
Cdd:cd06186   90 vlvegpygsSSEDLLsydnvllvaggsgitfVLPILRDLLRRSS--KTSRTRRVKLVWVVRDREDLEWFLDELRA----- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 420 WQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQN 499
Cdd:cd06186  163 AQELEVDG-EIEIYVTR-------------------------------------------VVVCGPPGLVDDVRNAVAKK 198
                        250
                 ....*....|....
gi 665821293 500 NsyGTRFEYNKESF 513
Cdd:cd06186  199 G--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
45-181 5.12e-15

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


:

Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 71.53  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293   45 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 124
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665821293  125 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 181
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
295-513 1.49e-26

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: 107.01  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 295 SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLLPP------- 364
Cdd:cd06186   10 SDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALKSPgggvslk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 365 ---------SSQDSE----------------ILPFIQSRNYPKDdwKPYKLRRLYFIWVCRDIQSFRWFADLLCMlhnkf 419
Cdd:cd06186   90 vlvegpygsSSEDLLsydnvllvaggsgitfVLPILRDLLRRSS--KTSRTRRVKLVWVVRDREDLEWFLDELRA----- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 420 WQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQN 499
Cdd:cd06186  163 AQELEVDG-EIEIYVTR-------------------------------------------VVVCGPPGLVDDVRNAVAKK 198
                        250
                 ....*....|....
gi 665821293 500 NsyGTRFEYNKESF 513
Cdd:cd06186  199 G--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
386-496 3.19e-18

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 81.62  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293  386 KPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYVNIQLYLSQTD-GIQKIIGEKYHALNSR 454
Cdd:pfam08030  28 KKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDASDQSDSSIRSeNFDSLMNEVIGVDFVE 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 665821293  455 LFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 496
Cdd:pfam08030 108 FHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
45-181 5.12e-15

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 71.53  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293   45 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 124
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665821293  125 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 181
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
45-361 5.74e-07

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 52.16  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293  45 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 123
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 124 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 203
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 204 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 283
Cdd:PLN02844 286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665821293 284 PVTIISVMSHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLL 361
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKI 391
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
286-360 3.86e-04

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 42.16  E-value: 3.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665821293 286 TIISVMSHPSDV--MEIRMVKENFKARPGQYITLHCPsvSALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDL 360
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVP--GDGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL 74
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
295-513 1.49e-26

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: 107.01  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 295 SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLLPP------- 364
Cdd:cd06186   10 SDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALKSPgggvslk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 365 ---------SSQDSE----------------ILPFIQSRNYPKDdwKPYKLRRLYFIWVCRDIQSFRWFADLLCMlhnkf 419
Cdd:cd06186   90 vlvegpygsSSEDLLsydnvllvaggsgitfVLPILRDLLRRSS--KTSRTRRVKLVWVVRDREDLEWFLDELRA----- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 420 WQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQN 499
Cdd:cd06186  163 AQELEVDG-EIEIYVTR-------------------------------------------VVVCGPPGLVDDVRNAVAKK 198
                        250
                 ....*....|....
gi 665821293 500 NsyGTRFEYNKESF 513
Cdd:cd06186  199 G--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
386-496 3.19e-18

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 81.62  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293  386 KPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYVNIQLYLSQTD-GIQKIIGEKYHALNSR 454
Cdd:pfam08030  28 KKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDASDQSDSSIRSeNFDSLMNEVIGVDFVE 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 665821293  455 LFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 496
Cdd:pfam08030 108 FHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
45-181 5.12e-15

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 71.53  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293   45 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 124
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665821293  125 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 181
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
FAD_binding_8 pfam08022
FAD-binding domain;
283-363 3.68e-11

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 60.04  E-value: 3.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293  283 KPVTIISVMSHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWTERFRD 359
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                  ....
gi 665821293  360 LLLP 363
Cdd:pfam08022  80 YLSS 83
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
45-361 5.74e-07

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 52.16  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293  45 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 123
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 124 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 203
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 204 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 283
Cdd:PLN02844 286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665821293 284 PVTIISVMSHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLL 361
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKI 391
PLN02631 PLN02631
ferric-chelate reductase
269-357 1.52e-06

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 50.81  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 269 LYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 347
Cdd:PLN02631 294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373
                         90
                 ....*....|
gi 665821293 348 KIVGDWTERF 357
Cdd:PLN02631 374 RRQGSWTQKL 383
PLN02292 PLN02292
ferric-chelate reductase
149-368 9.68e-05

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 45.24  E-value: 9.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 149 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 227
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821293 228 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKEN- 306
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665821293 307 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQD 368
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSD 408
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
286-360 3.86e-04

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 42.16  E-value: 3.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665821293 286 TIISVMSHPSDV--MEIRMVKENFKARPGQYITLHCPsvSALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDL 360
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVP--GDGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL 74
 
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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