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Conserved domains on  [gi|74139691|dbj|BAE31697|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

NADPH oxidase family protein( domain architecture ID 10153067)

NADPH oxidase (NOX) family protein may catalyze the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide

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 ...
 25-298 3.50e-53

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: 172.87  E-value: 3.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  25 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 98
Cdd:cd06186   1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  99 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 178
Cdd:cd06186  81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 179 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 258
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 74139691 259 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 298
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
 
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 ...
 25-298 3.50e-53

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: 172.87  E-value: 3.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  25 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 98
Cdd:cd06186   1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  99 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 178
Cdd:cd06186  81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 179 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 258
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 74139691 259 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 298
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
129-278 8.14e-53

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 169.83  E-value: 8.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   129 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 208
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74139691   209 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 278
Cdd:pfam08030  72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 5-151 1.22e-23

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 100.69  E-value: 1.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691    5 MFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEED--FFSI 81
Cdd:PLN02844 296 IFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDdhTMSV 375

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   82 HIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSV 151
Cdd:PLN02844 376 IIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEI 445
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
12-277 9.13e-17

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 79.94  E-value: 9.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  12 RLVRFWRSQQKV-VITKVVTHPFKTIELQMK---KKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEED-FFSIHIRI 85
Cdd:COG4097 205 RLGRPLRSRRHPyRVESVEPEAGDVVELTLRpegGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDgRLRFTIKA 284

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  86 VGDWTEGLFnacgcdkqefqdawKLP---KIAVDGPFGTasedvFSYEV------VMLVGAGIGVTPFASILKSVwykyc 156
Cdd:COG4097 285 LGDFTRRLG--------------RLKpgtRVYVEGPYGR-----FTFDRrdtaprQVWIAGGIGITPFLALLRAL----- 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 157 dNATSLKLKKIYFYWLCRDTHAfewfADLLQLLETQMQERNNANFlsyniyltgwdesqanhfaVHHDEEKDvitglkqk 236
Cdd:COG4097 341 -AARPGDQRPVDLFYCVRDEED----APFLEELRALAARLAGLRL-------------------HLVVSDED-------- 388

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 74139691 237 tlyGRPNwdneFKTIASEHPN-TTIGVFLCGPEALAETLSKQ 277
Cdd:COG4097 389 ---GRLT----AERLRRLVPDlAEADVFFCGPPGMMDALRRD 423
 
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 ...
 25-298 3.50e-53

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: 172.87  E-value: 3.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  25 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 98
Cdd:cd06186   1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  99 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 178
Cdd:cd06186  81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 179 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 258
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 74139691 259 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 298
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
129-278 8.14e-53

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 169.83  E-value: 8.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   129 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 208
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74139691   209 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 278
Cdd:pfam08030  72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 24-276 4.38e-25

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: 4.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  24 VITKVVTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP-EEDFFSIHIRIV--GDWTEGLFNACGCD 100
Cdd:cd00322   1 VATEDVTDDVRLFRLQ-LPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 101 KqefqdawklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKycdnatsLKLKKIYFYWLCRDTHAFe 180
Cdd:cd00322  80 E-----------VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAAD-------KPGGEITLLYGARTPADL- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 181 WFADLLQLLetqmqERNNANFLsynIYLTGWDESQANHFAVHHDeekdvitglkqktlygrpnwDNEFKTIASEHPNTTI 260
Cdd:cd00322 141 LFLDELEEL-----AKEGPNFR---LVLALSRESEAKLGPGGRI--------------------DREAEILALLPDDSGA 192

                       250
                ....*....|....*.
gi 74139691 261 GVFLCGPEALAETLSK 276
Cdd:cd00322 193 LVYICGPPAMAKAVRE 208
FAD_binding_8 pfam08022
FAD-binding domain;
27-123 1.11e-24

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 95.48  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691    27 KVVTHPFKTIELQMKK--KGFKMEVGQYIFVKC-PKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFN-ACGCDKQ 102
Cdd:pfam08022   8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANyLSSSCPK 87

                          90       100
                  ....*....|....*....|.
gi 74139691   103 EFQDAWKLPKIAVDGPFGTAS 123
Cdd:pfam08022  88 SPENGKDKPRVLIEGPYGPPS 108
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 5-151 1.22e-23

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 100.69  E-value: 1.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691    5 MFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEED--FFSI 81
Cdd:PLN02844 296 IFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDdhTMSV 375

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   82 HIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSV 151
Cdd:PLN02844 376 IIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEI 445
PLN02292 PLN02292
ferric-chelate reductase
 6-167 9.83e-19

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 86.07  E-value: 9.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691    6 FLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQM-KKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP--EEDFFSIH 82
Cdd:PLN02292 310 YIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFsKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSklEPEKLSVM 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   83 IRIVGDWTEGLFNACGCDKQEFQDAwklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWykYCDNATSL 162
Cdd:PLN02292 390 IKSQGKWSTKLYHMLSSSDQIDRLA-----VSVEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI--YTSSTETC 462


                 ....*
gi 74139691  163 KLKKI 167
Cdd:PLN02292 463 KIPKI 467
PLN02631 PLN02631
ferric-chelate reductase
 5-162 5.37e-18

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 83.94  E-value: 5.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691    5 MFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKK-KGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP--EEDFFSI 81
Cdd:PLN02631 292 IFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSnlEKDTLSV 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   82 HIRIVGDWTEGLFNACGCDKQEFQdawklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCDNATS 161
Cdd:PLN02631 372 VIRRQGSWTQKLYTHLSSSIDSLE-------VSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQSQNPSTK 444


                 .
gi 74139691  162 L 162
Cdd:PLN02631 445 L 445
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 35-277 1.70e-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: 1.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  35 TIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFfsiHIRIV----GDWTEGLfnacgcdkqefqdAWKL 110
Cdd:cd06198  11 TLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDG---RLRFTikalGDYTRRL-------------AERL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 111 P---KIAVDGPFGtasedVFSYEV----VMLVGAGIGVTPFASILKsvwykycDNATSLKLKKIYFYWlCRDTHAFEWFA 183
Cdd:cd06198  75 KpgtRVTVEGPYG-----RFTFDDrrarQIWIAGGIGITPFLALLE-------ALAARGDARPVTLFY-CVRDPEDAVFL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 184 DLLQlletqmqernnanflsyniyltgwDESQANHFAVHhdeekdVITGlkqktlyGRPNWDNEFKTIASEHPN-TTIGV 262
Cdd:cd06198 142 DELR------------------------ALAAAAGVVLH------VIDS-------PSDGRLTLEQLVRALVPDlADADV 184

                       250
                ....*....|....*
gi 74139691 263 FLCGPEALAETLSKQ 277
Cdd:cd06198 185 WFCGPPGMADALEKG 199
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
12-277 9.13e-17

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 79.94  E-value: 9.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  12 RLVRFWRSQQKV-VITKVVTHPFKTIELQMK---KKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEED-FFSIHIRI 85
Cdd:COG4097 205 RLGRPLRSRRHPyRVESVEPEAGDVVELTLRpegGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDgRLRFTIKA 284

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  86 VGDWTEGLFnacgcdkqefqdawKLP---KIAVDGPFGTasedvFSYEV------VMLVGAGIGVTPFASILKSVwykyc 156
Cdd:COG4097 285 LGDFTRRLG--------------RLKpgtRVYVEGPYGR-----FTFDRrdtaprQVWIAGGIGITPFLALLRAL----- 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 157 dNATSLKLKKIYFYWLCRDTHAfewfADLLQLLETQMQERNNANFlsyniyltgwdesqanhfaVHHDEEKDvitglkqk 236
Cdd:COG4097 341 -AARPGDQRPVDLFYCVRDEED----APFLEELRALAARLAGLRL-------------------HLVVSDED-------- 388

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 74139691 237 tlyGRPNwdneFKTIASEHPN-TTIGVFLCGPEALAETLSKQ 277
Cdd:COG4097 389 ---GRLT----AERLRRLVPDlAEADVFFCGPPGMMDALRRD 423
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 22-175 2.38e-14

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 71.05  E-value: 2.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  22 KVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKvsKLEWHPFTLTSAP-EEDFFSIHIRIVGDWTEGLFNacgcd 100
Cdd:COG0543   1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAE----- 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74139691 101 KQEFQdawklpKIAVDGPFGTAsedvFSYEV----VMLVGAGIGVTPFASILKSVWYKYCdnatslklkKIYFYWLCRD 175
Cdd:COG0543  74 LKPGD------ELDVRGPLGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAEALLARGR---------RVTLYLGART 133
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
50-277 1.00e-10

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 60.57  E-value: 1.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  50 GQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDwteGLFnacgcdKQEFQDAWKlP--KIAVDGPFGTasedvF 127
Cdd:COG1018  37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG---GGG------SNWLHDHLK-VgdTLEVSGPRGD-----F 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 128 SYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCR--DTHAfewFADLLQLLETQMqernnAN 200
Cdd:COG1018 102 VLDPeparpLLLIAGGIGITPFLSMLRTL-------LARGPFRPVTLVYGARspADLA---FRDELEALAARH-----PR 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74139691 201 FlsyniyltgwdesqanHFAVHHDEEKDVITglkqktlyGRPNwDNEFKTIASEHPNTTigVFLCGPEALAETLSKQ 277
Cdd:COG1018 167 L----------------RLHPVLSREPAGLQ--------GRLD-AELLAALLPDPADAH--VYLCGPPPMMEAVRAA 216
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 34-150 1.18e-09

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 57.58  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691   34 KTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLtSAPEEDFFSIHIRIVGDWTEGLFNacgcdKQEFQdawklpKI 113
Cdd:PRK00054  20 YTLVLD-GEKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLSK-----LKEGD------EL 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 74139691  114 AVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKS 150
Cdd:PRK00054  87 DIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKE 123
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 25-186 7.59e-09

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: 55.03  E-value: 7.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  25 ITKVVTHPFKTIELQMK--KKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSA-PEEDFFSIHIRIVGDWTEGLFNacgcdk 101
Cdd:cd06192   1 IVKKEQLEPNLVLLTIKapLAARLFRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAE------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 102 qefqdaWKLP-KIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKsvwYKYCDNAtslklkKIYFYWLCRDTHA-- 178
Cdd:cd06192  75 ------LKPGeKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK---KLAANGN------KVTVLAGAKKAKEef 139

                       170
                ....*....|..
gi 74139691 179 ----FEWFADLL 186
Cdd:cd06192 140 ldeyFELPADVE 151
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 23-162 5.22e-08

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: 52.64  E-value: 5.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  23 VVITKVV--THPFKTIELQMKkkgFKMEVGQYIFVKCPKVSKLewhPFTLTSAPEEDffSIHIRIVGDWTEGLFNACGCD 100
Cdd:cd06220   1 VTIKEVIdeTPTVKTFVFDWD---FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN--SITVKKVGEATSALHDLKEGD 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74139691 101 KqefqdawklpkIAVDGPFGTASEDVfsYEVVMLVGAGIGVTPFASILKSvwYKYCDNATSL 162
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 ...
 50-201 5.27e-07

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: 49.47  E-value: 5.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  50 GQYIFVKCPKVSKLewhPFTLTSAPEED-FFSIHIRIV--GDWTEGLFNACGCDKqefqdawklpKIAVDGPFGTASEDV 126
Cdd:cd06189  29 GQYLDLLLDDGDKR---PFSIASAPHEDgEIELHIRAVpgGSFSDYVFEELKENG----------LVRIEGPLGDFFLRE 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74139691 127 FSYEVVMLVGAGIGVTPFASILksvwykycDNATSLKLK-KIYFYWLCRDThafewfADLLQLLETQMQERNNANF 201
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 ...
 50-269 1.49e-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: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  50 GQYIFVKCPKVSKLEWHP--FTLTSAPEEDFFSI----------------HIRiVGDwteglfnacgcdkqefqdawklp 111
Cdd:cd06184  40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYYRIsvkrepgglvsnylhdNVK-VGD----------------------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 112 KIAVDGPFGTasedvFSYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCRD--THAF-EWFA 183
Cdd:cd06184  96 VLEVSAPAGD-----FVLDEasdrpLVLISAGVGITPMLSMLEAL-------AAEGPGRPVTFIHAARNsaVHAFrDELE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691 184 DLLQlletqmqerNNANFLSYNIY--LTGWDESQANHFAVHHDEEKdvitgLKQKTLygrpnwdnefktiaseHPNTTig 261
Cdd:cd06184 164 ELAA---------RLPNLKLHVFYsePEAGDREEDYDHAGRIDLAL-----LRELLL----------------PADAD-- 211


                ....*...
gi 74139691 262 VFLCGPEA 269
Cdd:cd06184 212 FYLCGPVP 219
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 29-150 9.72e-05

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: 9.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  29 VTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEEDFFSIHIRIVGDwTEGLFNACGcdkqefqDA 107
Cdd:cd06196  11 VTHDVKRLRFD-KPEGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDDVLEFVIKSYPD-HDGVTEQLG-------RL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74139691 108 WKLPKIAVDGPFGTAS---EDVFsyevvmlVGAGIGVTPFASILKS 150
Cdd:cd06196  82 QPGDTLLIEDPWGAIEykgPGVF-------IAGGAGITPFIAILRD 120
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 68-151 9.49e-04

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: 39.68  E-value: 9.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139691  68 FTLTSAPE----EDFFSIHIRIVGDWTEGLFNAcgcDKQEFQDAWKLPKIAVDGPFgTASEDVFSYEVVML-VGAGIGVT 142
Cdd:cd06197  63 FTVSSAPPhdpaTDEFEITVRKKGPVTGFLFQV---ARRLREQGLEVPVLGVGGEF-TLSLPGEGAERKMVwIAGGVGIT 138


                ....*....
gi 74139691 143 PFASILKSV 151
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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