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Conserved domains on  [gi|1209752|gb|AAB05997|]
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gp91phox [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
401-550 1.04e-49

Ferric reductase NAD binding domain;


:

Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 168.67  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752    401 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 480
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209752    481 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 550
Cdd:pfam08030  72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 297-570 2.24e-49

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: 169.79  E-value: 2.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  297 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 370
Cdd:cd06186   1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  371 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 450
Cdd:cd06186  81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  451 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 530
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 1209752  531 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 570
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
PLN02844 super family cl33578
oxidoreductase/ferric-chelate reductase
 165-423 3.69e-31

oxidoreductase/ferric-chelate reductase


The actual alignment was detected with superfamily member PLN02844:

Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 128.81  E-value: 3.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   165 GGLYVAvTRLAGITGIVITLcliliitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERivrgqtaesleeHnldic 244
Cdd:PLN02844 234 GRIYLA-GEIALVTGLVIWI-------TSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGDR------------H----- 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   245 adkieewgkikecpvpkfagnppmtWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQ 323
Cdd:PLN02844 289 -------------------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTS 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   324 YIFVKCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSY 401
Cdd:PLN02844 344 VIFMKIPSISRFQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRY 423

                        250       260
                 ....*....|....*....|..
gi 1209752   402 EVVMLVGAGIGVTPFASILKSV 423
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEI 445
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 65-220 2.32e-16

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: 75.38  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752     65 MLILLPVCRNLLSFLRGSSaccstrirrqLDRNLTFHKMVAWMIALHTAIHTIAHLFNvewcvnarvgisdrysialsdi 144
Cdd:pfam01794  11 LLLLLALRNNPLEWLTGLS----------YDRLLLFHRWLGRLAFLLALLHVILYLIY---------------------- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209752    145 gdneneeylnfarEKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLA 220
Cdd:pfam01794  59 -------------WLRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
401-550 1.04e-49

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 168.67  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752    401 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 480
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209752    481 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 550
Cdd:pfam08030  72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 297-570 2.24e-49

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: 169.79  E-value: 2.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  297 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 370
Cdd:cd06186   1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  371 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 450
Cdd:cd06186  81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  451 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 530
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 1209752  531 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 570
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 165-423 3.69e-31

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 128.81  E-value: 3.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   165 GGLYVAvTRLAGITGIVITLcliliitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERivrgqtaesleeHnldic 244
Cdd:PLN02844 234 GRIYLA-GEIALVTGLVIWI-------TSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGDR------------H----- 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   245 adkieewgkikecpvpkfagnppmtWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQ 323
Cdd:PLN02844 289 -------------------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTS 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   324 YIFVKCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSY 401
Cdd:PLN02844 344 VIFMKIPSISRFQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRY 423

                        250       260
                 ....*....|....*....|..
gi 1209752   402 EVVMLVGAGIGVTPFASILKSV 423
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEI 445
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 296-548 7.79e-24

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 99.83  E-value: 7.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  296 VITKVVTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP-EEDFFSIHIRIV--GDWTEGLFNACGCD 372
Cdd:cd00322   1 VATEDVTDDVRLFRLQ-LPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  373 KqefqdawklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKycdnatsLKLKKIYFYWLCRDTHAFe 452
Cdd:cd00322  80 E-----------VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAAD-------KPGGEITLLYGARTPADL- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  453 WFADLLQLLetqmqERNNANFLsynIYLTGWDESQANHFAVHHDeekdvitglkqktlygrpnwDNEFKTIASEHPNTTI 532
Cdd:cd00322 141 LFLDELEEL-----AKEGPNFR---LVLALSRESEAKLGPGGRI--------------------DREAEILALLPDDSGA 192

                       250
                ....*....|....*.
gi 1209752  533 GVFLCGPEALAETLSK 548
Cdd:cd00322 193 LVYICGPPAMAKAVRE 208
FAD_binding_8 pfam08022
FAD-binding domain;
299-395 8.31e-24

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 96.25  E-value: 8.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752    299 KVVTHPFKTIELQMKK--KGFKMEVGQYIFVKC-PKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFN-ACGCDKQ 374
Cdd:pfam08022   8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANyLSSSCPK 87

                          90       100
                  ....*....|....*....|.
gi 1209752    375 EFQDAWKLPKIAVDGPFGTAS 395
Cdd:pfam08022  88 SPENGKDKPRVLIEGPYGPPS 108
PLN02292 PLN02292
ferric-chelate reductase
 170-439 1.87e-21

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 98.40  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   170 AVTRLAGitgiVITLCLILIITSST-KTIRRSYFEVFWYTHHLFVIFFIGLAIHgaerivrgqtaesleehnLDICADKI 248
Cdd:PLN02292 247 GVSNLAG----EIALVAGLVMWATTyPKIRRRFFEVFFYTHYLYIVFMLFFVFH------------------VGISFALI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   249 eewgkikecPVPKFagnppmtwkwivgpmFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQM-KKKGFKMEVGQYIFV 327
Cdd:PLN02292 305 ---------SFPGF---------------YIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFsKNPMLMYSPTSIMFV 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   328 KCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAwklpkIAVDGPFGTASEDVFSYEVVM 405
Cdd:PLN02292 361 NIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQIDRLA-----VSVEGPYGPASTDFLRHESLV 435

                        250       260       270
                 ....*....|....*....|....*....|....
gi 1209752   406 LVGAGIGVTPFASILKSVWykYCDNATSLKLKKI 439
Cdd:PLN02292 436 MVSGGSGITPFISIIRDLI--YTSSTETCKIPKI 467
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
152-549 9.65e-18

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 85.72  E-value: 9.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  152 YLNFAREKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTktIRR--SYfEVFWYTHHLFVIFFIGLAIHGAerivr 229
Cdd:COG4097 103 KWLVGWGGLPARLAALLTLLRGLAELLGEWAFYLLLALVVLSL--LRRrlPY-ELWRLTHRLLAVAYLLLAFHHL----- 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  230 gqtaeSLeehnldicadkieewgkikecpVPKFAGNPPMTWKWI---VGPMFLYLCERLVRFWRSQQKV-VITKVVTHPF 305
Cdd:COG4097 175 -----LL----------------------GGPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAG 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  306 KTIELQMK---KKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEED-FFSIHIRIVGDWTEGLFnacgcdkqefqdaw 380
Cdd:COG4097 228 DVVELTLRpegGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRLG-------------- 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  381 KLP---KIAVDGPFGTasedvFSYEV------VMLVGAGIGVTPFASILKSVwykycdNATSLKLKKIYFYWLCRDTHAf 451
Cdd:COG4097 294 RLKpgtRVYVEGPYGR-----FTFDRrdtaprQVWIAGGIGITPFLALLRAL------AARPGDQRPVDLFYCVRDEED- 361

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  452 ewfADLLQLLETQMQERNNANFlsyniyltgwdesqanhfaVHHDEEKDvitglkqktlyGRPNwdneFKTIASEHPN-T 530
Cdd:COG4097 362 ---APFLEELRALAARLAGLRL-------------------HLVVSDED-----------GRLT----AERLRRLVPDlA 404

                       410
                ....*....|....*....
gi 1209752  531 TIGVFLCGPEALAETLSKQ 549
Cdd:COG4097 405 EADVFFCGPPGMMDALRRD 423
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 65-220 2.32e-16

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: 75.38  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752     65 MLILLPVCRNLLSFLRGSSaccstrirrqLDRNLTFHKMVAWMIALHTAIHTIAHLFNvewcvnarvgisdrysialsdi 144
Cdd:pfam01794  11 LLLLLALRNNPLEWLTGLS----------YDRLLLFHRWLGRLAFLLALLHVILYLIY---------------------- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209752    145 gdneneeylnfarEKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLA 220
Cdd:pfam01794  59 -------------WLRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
322-549 3.15e-10

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 60.57  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  322 GQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDwteGLFnacgcdKQEFQDAWKlP--KIAVDGPFGTasedvF 399
Cdd:COG1018  37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG---GGG------SNWLHDHLK-VgdTLEVSGPRGD-----F 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  400 SYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCR--DTHAfewFADLLQLLETQMqernnAN 472
Cdd:COG1018 102 VLDPeparpLLLIAGGIGITPFLSMLRTL-------LARGPFRPVTLVYGARspADLA---FRDELEALAARH-----PR 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209752  473 FlsyniyltgwdesqanHFAVHHDEEKDVITglkqktlyGRPNwDNEFKTIASEHPNTTigVFLCGPEALAETLSKQ 549
Cdd:COG1018 167 L----------------RLHPVLSREPAGLQ--------GRLD-AELLAALLPDPADAH--VYLCGPPPMMEAVRAA 216
 
Name Accession Description Interval E-value
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
401-550 1.04e-49

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 168.67  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752    401 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 480
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209752    481 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 550
Cdd:pfam08030  72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 297-570 2.24e-49

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: 169.79  E-value: 2.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  297 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 370
Cdd:cd06186   1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  371 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 450
Cdd:cd06186  81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  451 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 530
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 1209752  531 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 570
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 165-423 3.69e-31

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 128.81  E-value: 3.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   165 GGLYVAvTRLAGITGIVITLcliliitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERivrgqtaesleeHnldic 244
Cdd:PLN02844 234 GRIYLA-GEIALVTGLVIWI-------TSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGDR------------H----- 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   245 adkieewgkikecpvpkfagnppmtWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQ 323
Cdd:PLN02844 289 -------------------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTS 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   324 YIFVKCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSY 401
Cdd:PLN02844 344 VIFMKIPSISRFQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRY 423

                        250       260
                 ....*....|....*....|..
gi 1209752   402 EVVMLVGAGIGVTPFASILKSV 423
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEI 445
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 296-548 7.79e-24

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 99.83  E-value: 7.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  296 VITKVVTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP-EEDFFSIHIRIV--GDWTEGLFNACGCD 372
Cdd:cd00322   1 VATEDVTDDVRLFRLQ-LPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  373 KqefqdawklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKycdnatsLKLKKIYFYWLCRDTHAFe 452
Cdd:cd00322  80 E-----------VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAAD-------KPGGEITLLYGARTPADL- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  453 WFADLLQLLetqmqERNNANFLsynIYLTGWDESQANHFAVHHDeekdvitglkqktlygrpnwDNEFKTIASEHPNTTI 532
Cdd:cd00322 141 LFLDELEEL-----AKEGPNFR---LVLALSRESEAKLGPGGRI--------------------DREAEILALLPDDSGA 192

                       250
                ....*....|....*.
gi 1209752  533 GVFLCGPEALAETLSK 548
Cdd:cd00322 193 LVYICGPPAMAKAVRE 208
FAD_binding_8 pfam08022
FAD-binding domain;
299-395 8.31e-24

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 96.25  E-value: 8.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752    299 KVVTHPFKTIELQMKK--KGFKMEVGQYIFVKC-PKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFN-ACGCDKQ 374
Cdd:pfam08022   8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANyLSSSCPK 87

                          90       100
                  ....*....|....*....|.
gi 1209752    375 EFQDAWKLPKIAVDGPFGTAS 395
Cdd:pfam08022  88 SPENGKDKPRVLIEGPYGPPS 108
PLN02292 PLN02292
ferric-chelate reductase
 170-439 1.87e-21

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 98.40  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   170 AVTRLAGitgiVITLCLILIITSST-KTIRRSYFEVFWYTHHLFVIFFIGLAIHgaerivrgqtaesleehnLDICADKI 248
Cdd:PLN02292 247 GVSNLAG----EIALVAGLVMWATTyPKIRRRFFEVFFYTHYLYIVFMLFFVFH------------------VGISFALI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   249 eewgkikecPVPKFagnppmtwkwivgpmFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQM-KKKGFKMEVGQYIFV 327
Cdd:PLN02292 305 ---------SFPGF---------------YIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFsKNPMLMYSPTSIMFV 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   328 KCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAwklpkIAVDGPFGTASEDVFSYEVVM 405
Cdd:PLN02292 361 NIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQIDRLA-----VSVEGPYGPASTDFLRHESLV 435

                        250       260       270
                 ....*....|....*....|....*....|....
gi 1209752   406 LVGAGIGVTPFASILKSVWykYCDNATSLKLKKI 439
Cdd:PLN02292 436 MVSGGSGITPFISIIRDLI--YTSSTETCKIPKI 467
PLN02631 PLN02631
ferric-chelate reductase
 171-434 5.43e-21

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 97.04  E-value: 5.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   171 VTRLAGITGIVITLCLILiitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAErivrgqtaesleehnldicadkiee 250
Cdd:PLN02631 231 VPNLAGTIAMVIGIAMWV---TSLPSFRRKKFELFFYTHHLYGLYIVFYVIHVGD------------------------- 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   251 wgkikecpvpkfagnppmTWKWIVGP-MFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKK-KGFKMEVGQYIFVK 328
Cdd:PLN02631 283 ------------------SWFCMILPnIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLH 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   329 CPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQdawklpkIAVDGPFGTASEDVFSYEVVML 406
Cdd:PLN02631 345 VPSISKLQWHPFTITSSSnlEKDTLSVVIRRQGSWTQKLYTHLSSSIDSLE-------VSTEGPYGPNSFDVSRHNSLIL 417

                        250       260
                 ....*....|....*....|....*...
gi 1209752   407 VGAGIGVTPFASILKSVWYKYCDNATSL 434
Cdd:PLN02631 418 VSGGSGITPFISVIRELIFQSQNPSTKL 445
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
152-549 9.65e-18

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 85.72  E-value: 9.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  152 YLNFAREKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTktIRR--SYfEVFWYTHHLFVIFFIGLAIHGAerivr 229
Cdd:COG4097 103 KWLVGWGGLPARLAALLTLLRGLAELLGEWAFYLLLALVVLSL--LRRrlPY-ELWRLTHRLLAVAYLLLAFHHL----- 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  230 gqtaeSLeehnldicadkieewgkikecpVPKFAGNPPMTWKWI---VGPMFLYLCERLVRFWRSQQKV-VITKVVTHPF 305
Cdd:COG4097 175 -----LL----------------------GGPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAG 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  306 KTIELQMK---KKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEED-FFSIHIRIVGDWTEGLFnacgcdkqefqdaw 380
Cdd:COG4097 228 DVVELTLRpegGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRLG-------------- 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  381 KLP---KIAVDGPFGTasedvFSYEV------VMLVGAGIGVTPFASILKSVwykycdNATSLKLKKIYFYWLCRDTHAf 451
Cdd:COG4097 294 RLKpgtRVYVEGPYGR-----FTFDRrdtaprQVWIAGGIGITPFLALLRAL------AARPGDQRPVDLFYCVRDEED- 361

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  452 ewfADLLQLLETQMQERNNANFlsyniyltgwdesqanhfaVHHDEEKDvitglkqktlyGRPNwdneFKTIASEHPN-T 530
Cdd:COG4097 362 ---APFLEELRALAARLAGLRL-------------------HLVVSDED-----------GRLT----AERLRRLVPDlA 404

                       410
                ....*....|....*....
gi 1209752  531 TIGVFLCGPEALAETLSKQ 549
Cdd:COG4097 405 EADVFFCGPPGMMDALRRD 423
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 307-549 9.76e-17

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 79.22  E-value: 9.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  307 TIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFfsiHIRIV----GDWTEGLfnacgcdkqefqdAWKL 382
Cdd:cd06198  11 TLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDG---RLRFTikalGDYTRRL-------------AERL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  383 P---KIAVDGPFGtasedVFSYEV----VMLVGAGIGVTPFASILKsvwykycDNATSLKLKKIYFYWlCRDTHAFEWFA 455
Cdd:cd06198  75 KpgtRVTVEGPYG-----RFTFDDrrarQIWIAGGIGITPFLALLE-------ALAARGDARPVTLFY-CVRDPEDAVFL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  456 DLLQlletqmqernnanflsyniyltgwDESQANHFAVHhdeekdVITGlkqktlyGRPNWDNEFKTIASEHPN-TTIGV 534
Cdd:cd06198 142 DELR------------------------ALAAAAGVVLH------VIDS-------PSDGRLTLEQLVRALVPDlADADV 184

                       250
                ....*....|....*
gi 1209752  535 FLCGPEALAETLSKQ 549
Cdd:cd06198 185 WFCGPPGMADALEKG 199
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 65-220 2.32e-16

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: 75.38  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752     65 MLILLPVCRNLLSFLRGSSaccstrirrqLDRNLTFHKMVAWMIALHTAIHTIAHLFNvewcvnarvgisdrysialsdi 144
Cdd:pfam01794  11 LLLLLALRNNPLEWLTGLS----------YDRLLLFHRWLGRLAFLLALLHVILYLIY---------------------- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209752    145 gdneneeylnfarEKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLA 220
Cdd:pfam01794  59 -------------WLRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 294-447 1.34e-13

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 70.66  E-value: 1.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  294 KVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKvsKLEWHPFTLTSAP-EEDFFSIHIRIVGDWTEGLFNacgcd 372
Cdd:COG0543   1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAE----- 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209752  373 KQEFQdawklpKIAVDGPFGTAsedvFSYEV----VMLVGAGIGVTPFASILKSVWYKYCdnatslklkKIYFYWLCRD 447
Cdd:COG0543  74 LKPGD------ELDVRGPLGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAEALLARGR---------RVTLYLGART 133
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
322-549 3.15e-10

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 60.57  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  322 GQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDwteGLFnacgcdKQEFQDAWKlP--KIAVDGPFGTasedvF 399
Cdd:COG1018  37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG---GGG------SNWLHDHLK-VgdTLEVSGPRGD-----F 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  400 SYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCR--DTHAfewFADLLQLLETQMqernnAN 472
Cdd:COG1018 102 VLDPeparpLLLIAGGIGITPFLSMLRTL-------LARGPFRPVTLVYGARspADLA---FRDELEALAARH-----PR 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209752  473 FlsyniyltgwdesqanHFAVHHDEEKDVITglkqktlyGRPNwDNEFKTIASEHPNTTigVFLCGPEALAETLSKQ 549
Cdd:COG1018 167 L----------------RLHPVLSREPAGLQ--------GRLD-AELLAALLPDPADAH--VYLCGPPPMMEAVRAA 216
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 306-422 3.85e-09

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 57.58  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752   306 KTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLtSAPEEDFFSIHIRIVGDWTEGLFNacgcdKQEFQdawklpKI 385
Cdd:PRK00054  20 YTLVLD-GEKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLSK-----LKEGD------EL 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 1209752   386 AVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKS 422
Cdd:PRK00054  87 DIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKE 123
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 297-458 5.06e-08

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 54.25  E-value: 5.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  297 ITKVVTHPFKTIELQMK--KKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSA-PEEDFFSIHIRIVGDWTEGLFNacgcdk 373
Cdd:cd06192   1 IVKKEQLEPNLVLLTIKapLAARLFRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAE------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  374 qefqdaWKLP-KIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKsvwYKYCDNAtslklkKIYFYWLCRDTHA-- 450
Cdd:cd06192  75 ------LKPGeKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK---KLAANGN------KVTVLAGAKKAKEef 139

                       170
                ....*....|..
gi 1209752  451 ----FEWFADLL 458
Cdd:cd06192 140 ldeyFELPADVE 151
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 295-434 1.87e-07

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 52.25  E-value: 1.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  295 VVITKVV--THPFKTIELQMKkkgFKMEVGQYIFVKCPKVSKLewhPFTLTSAPEEDffSIHIRIVGDWTEGLFNACGCD 372
Cdd:cd06220   1 VTIKEVIdeTPTVKTFVFDWD---FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN--SITVKKVGEATSALHDLKEGD 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209752  373 KqefqdawklpkIAVDGPFGTASEDVfsYEVVMLVGAGIGVTPFASILKSvwYKYCDNATSL 434
Cdd:cd06220  73 K-----------LGIRGPYGNGFELV--GGKVLLIGGGIGIAPLAPLAER--LKKAADVTVL 119
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 322-473 1.73e-06

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 49.08  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  322 GQYIFVKCPKVSKLewhPFTLTSAPEED-FFSIHIRIV--GDWTEGLFNACGCDKqefqdawklpKIAVDGPFGTASEDV 398
Cdd:cd06189  29 GQYLDLLLDDGDKR---PFSIASAPHEDgEIELHIRAVpgGSFSDYVFEELKENG----------LVRIEGPLGDFFLRE 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209752  399 FSYEVVMLVGAGIGVTPFASILksvwykycDNATSLKLK-KIYFYWLCRDThafewfADLLQLLETQMQERNNANF 473
Cdd:cd06189  96 DSDRPLILIAGGTGFAPIKSIL--------EHLLAQGSKrPIHLYWGARTE------EDLYLDELLEAWAEAHPNF 157
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 322-541 3.96e-05

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 45.24  E-value: 3.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  322 GQYIFVKCPKVSKLEWHP--FTLTSAPEEDFFSI----------------HIRiVGDwteglfnacgcdkqefqdawklp 383
Cdd:cd06184  40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYYRIsvkrepgglvsnylhdNVK-VGD----------------------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  384 KIAVDGPFGTasedvFSYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCRD--THAF-EWFA 455
Cdd:cd06184  96 VLEVSAPAGD-----FVLDEasdrpLVLISAGVGITPMLSMLEAL-------AAEGPGRPVTFIHAARNsaVHAFrDELE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  456 DLLQlletqmqerNNANFLSYNIY--LTGWDESQANHFAVHHDEEKdvitgLKQKTLygrpnwdnefktiaseHPNTTig 533
Cdd:cd06184 164 ELAA---------RLPNLKLHVFYsePEAGDREEDYDHAGRIDLAL-----LRELLL----------------PADAD-- 211


                ....*...
gi 1209752  534 VFLCGPEA 541
Cdd:cd06184 212 FYLCGPVP 219
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 301-422 2.44e-04

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 42.61  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  301 VTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEEDFFSIHIRIVGDwTEGLFNACGcdkqefqDA 379
Cdd:cd06196  11 VTHDVKRLRFD-KPEGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDDVLEFVIKSYPD-HDGVTEQLG-------RL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 1209752  380 WKLPKIAVDGPFGTAS---EDVFsyevvmlVGAGIGVTPFASILKS 422
Cdd:cd06196  82 QPGDTLLIEDPWGAIEykgPGVF-------IAGGAGITPFIAILRD 120
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 340-423 1.95e-03

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 40.07  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209752  340 FTLTSAPE----EDFFSIHIRIVGDWTEGLFNAcgcDKQEFQDAWKLPKIAVDGPFgTASEDVFSYEVVML-VGAGIGVT 414
Cdd:cd06197  63 FTVSSAPPhdpaTDEFEITVRKKGPVTGFLFQV---ARRLREQGLEVPVLGVGGEF-TLSLPGEGAERKMVwIAGGVGIT 138


                ....*....
gi 1209752  415 PFASILKSV 423
Cdd:cd06197 139 PFLAMLRAI 147
 
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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