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Conserved domains on  [gi|42566436|ref|NP_192862|]
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Riboflavin synthase-like superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 159-258 3.22e-46

Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory burst NADPH oxidase proteins which produce reactive oxygen species as a defence mechanism. It tends to occur to the N-terminus of an EF-hand (pfam00036), which suggests a direct regulatory effect of Ca2+ on the activity of the NADPH oxidase in plants.


:

Pssm-ID: 462469  Cd Length: 100  Bit Score: 160.44  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   159 NRDGSGTERAIHGLKFIS-SKENGIVDWNDVQNNFAHLSKDGYLFKSDFAHCIGLENenSKEFADELFDALCRRRRIMVD 237
Cdd:pfam08414   2 DRTKSGAARALKGLRFISkTDGGEGAGWKAVEKRFDKLAVDGLLPRSKFGECIGMKD--SKEFAGELFDALARRRGITGD 79

                          90       100
                  ....*....|....*....|.
gi 42566436   238 KINLQELYEFWYQITDESFDS 258
Cdd:pfam08414  80 SITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
733-923 2.36e-44

Ferric reductase NAD binding domain;


:

Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 157.12  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   733 YDVVLLVGLGIGATPFVSILRDLLNNIikqqeqaecisgscsnsnissdhsfsclnseaasripqtqrKTLNTKNAYFYW 812
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKS-----------------------------------------KKLKTKKIKFYW 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   813 VTREQGSFDWFKEIMNEIADSDRKgVIEMHNYLTSVYEEGD-----TRSNLLTMIQTLNHAKNGVDIfsgtkVRTHFGRP 887
Cdd:pfam08030  40 VVRDLSSLEWFKDVLNELEELKEL-NIEIHIYLTGEYEAEDasdqsDSSIRSENFDSLMNEVIGVDF-----VEFHFGRP 113

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 42566436   888 KWKKVLSKISTKHRNARIGVFYCGVPSLGKELSTLC 923
Cdd:pfam08030 114 NWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 616-849 1.71e-42

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: 154.00  E-value: 1.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 616 ICKVVIYP-GNVVVLRMSKPTSFDYKSGQYVFVQCPSV-SKFEWHPFSITSSPGD--DYLSIHIR-QRGDWTEGIKKAFS 690
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRaKKGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 691 VvchapeagksgllradvPNQRSFPELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLNNIikqqeqaecis 770
Cdd:cd06186  81 S-----------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS----------- 132

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42566436 771 gscsnsnissdhsfsclnseaasripqtqRKTLNTKNAYFYWVTREQGSFDWFKEIMNEIADSDRKGVIemHNYLTSVY 849
Cdd:cd06186 133 -----------------------------SKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVV 180
COG4097 super family cl34712
Predicted ferric reductase [Inorganic ion transport and metabolism];
450-755 4.40e-19

Predicted ferric reductase [Inorganic ion transport and metabolism];


The actual alignment was detected with superfamily member COG4097:

Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 91.11  E-value: 4.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 450 DDCINFHKTISVAIISAMLLHatshlacdfPRILASTdtdykrYLVKYFGVTRPTYFGLVNTP------VGITGII-MVA 522
Cdd:COG4097  75 DRLYRLHKWLGILALVLALAH---------PLLLLGP------KWLVGWGGLPARLAALLTLLrglaelLGEWAFYlLLA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 523 FMLIAFTlasrrcRRnltKLPkpfdkltgYNAFWYSHHLLLTVYVLLVIHGVSL---YLEHKWYRKTVWMYLAVPVLLYV 599
Cdd:COG4097 140 LVVLSLL------RR---RLP--------YELWRLTHRLLAVAYLLLAFHHLLLggpFYWSPPAGVLWAALAAAGLAAAV 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 600 GERIFRFFRSRLYTVEICKVVIYPGNVVVLRMSKPTS--FDYKSGQYVFVQCP-SVSKFEWHPFSITSSP-GDDYLSIHI 675
Cdd:COG4097 203 YSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDgSPFWEEAHPFSISSAPgGDGRLRFTI 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 676 RQRGDWTEGIKKafsvvchapeagksglLRadvPNQRsfpeLLIDGPYGA-PAQDHWKYDVVLLVGLGIGATPFVSILRD 754
Cdd:COG4097 283 KALGDFTRRLGR----------------LK---PGTR----VYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRA 339


                .
gi 42566436 755 L 755
Cdd:COG4097 340 L 340
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 238-283 8.48e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


The actual alignment was detected with superfamily member cd00051:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 63  Bit Score: 35.60  E-value: 8.48e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 42566436 238 KINLQELYEFWYQITDESFDSRLQIFFNMV-KNGDGRITENEVKEII 283
Cdd:cd00051  16 TISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELM 62
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 159-258 3.22e-46

Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory burst NADPH oxidase proteins which produce reactive oxygen species as a defence mechanism. It tends to occur to the N-terminus of an EF-hand (pfam00036), which suggests a direct regulatory effect of Ca2+ on the activity of the NADPH oxidase in plants.


Pssm-ID: 462469  Cd Length: 100  Bit Score: 160.44  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   159 NRDGSGTERAIHGLKFIS-SKENGIVDWNDVQNNFAHLSKDGYLFKSDFAHCIGLENenSKEFADELFDALCRRRRIMVD 237
Cdd:pfam08414   2 DRTKSGAARALKGLRFISkTDGGEGAGWKAVEKRFDKLAVDGLLPRSKFGECIGMKD--SKEFAGELFDALARRRGITGD 79

                          90       100
                  ....*....|....*....|.
gi 42566436   238 KINLQELYEFWYQITDESFDS 258
Cdd:pfam08414  80 SITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
733-923 2.36e-44

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 157.12  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   733 YDVVLLVGLGIGATPFVSILRDLLNNIikqqeqaecisgscsnsnissdhsfsclnseaasripqtqrKTLNTKNAYFYW 812
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKS-----------------------------------------KKLKTKKIKFYW 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   813 VTREQGSFDWFKEIMNEIADSDRKgVIEMHNYLTSVYEEGD-----TRSNLLTMIQTLNHAKNGVDIfsgtkVRTHFGRP 887
Cdd:pfam08030  40 VVRDLSSLEWFKDVLNELEELKEL-NIEIHIYLTGEYEAEDasdqsDSSIRSENFDSLMNEVIGVDF-----VEFHFGRP 113

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 42566436   888 KWKKVLSKISTKHRNARIGVFYCGVPSLGKELSTLC 923
Cdd:pfam08030 114 NWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 616-849 1.71e-42

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: 154.00  E-value: 1.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 616 ICKVVIYP-GNVVVLRMSKPTSFDYKSGQYVFVQCPSV-SKFEWHPFSITSSPGD--DYLSIHIR-QRGDWTEGIKKAFS 690
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRaKKGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 691 VvchapeagksgllradvPNQRSFPELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLNNIikqqeqaecis 770
Cdd:cd06186  81 S-----------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS----------- 132

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42566436 771 gscsnsnissdhsfsclnseaasripqtqRKTLNTKNAYFYWVTREQGSFDWFKEIMNEIADSDRKGVIemHNYLTSVY 849
Cdd:cd06186 133 -----------------------------SKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVV 180
FAD_binding_8 pfam08022
FAD-binding domain;
612-727 1.23e-37

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 136.31  E-value: 1.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   612 YTVEICKVVIYPGNVVVLRMSKPT-SFDYKSGQYVFVQC-PSVSKFEWHPFSITSSPGDDYLSIHIRQRGDWTEGIKKAF 689
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYL 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 42566436   690 SVVCHAPEAgksgllradvpNQRSFPELLIDGPYGAPA 727
Cdd:pfam08022  82 SSSCPKSPE-----------NGKDKPRVLIEGPYGPPS 108
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 552-831 1.59e-20

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 97.23  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  552 YNAFWYSHHLLltvyvllvIHGVSLYLEHKWYRKTVWMYLAVpvLLYVGERIFRFFRSRLYTVeICKVVIYPGNVVVLRM 631
Cdd:PLN02844 263 FEIFYYTHHLY--------IVFLIFFLFHAGDRHFYMVFPGI--FLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVL 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  632 SKPTSFDYKSGQYVFVQCPSVSKFEWHPFSITSSPG--DDYLSIHIRQRGDWTEgikkafSVVCHAPEAGKSGllradvP 709
Cdd:PLN02844 332 PKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMSVIIKCEGGWTN------SLYNKIQAELDSE------T 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  710 NQRSFPELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLN---NIIKQQEQAECISGSCSNSNIssdhsfsC 786
Cdd:PLN02844 400 NQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASqssSRYRFPKRVQLIYVVKKSQDI-------C 472

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 42566436  787 LNSEAASRIPQTQRKTLNTKNAYFywVTREQGSFDWFKEIMNEIA 831
Cdd:PLN02844 473 LLNPISSLLLNQSSNQLNLKLKVF--VTQEEKPNATLRELLNQFS 515
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
450-755 4.40e-19

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 91.11  E-value: 4.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 450 DDCINFHKTISVAIISAMLLHatshlacdfPRILASTdtdykrYLVKYFGVTRPTYFGLVNTP------VGITGII-MVA 522
Cdd:COG4097  75 DRLYRLHKWLGILALVLALAH---------PLLLLGP------KWLVGWGGLPARLAALLTLLrglaelLGEWAFYlLLA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 523 FMLIAFTlasrrcRRnltKLPkpfdkltgYNAFWYSHHLLLTVYVLLVIHGVSL---YLEHKWYRKTVWMYLAVPVLLYV 599
Cdd:COG4097 140 LVVLSLL------RR---RLP--------YELWRLTHRLLAVAYLLLAFHHLLLggpFYWSPPAGVLWAALAAAGLAAAV 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 600 GERIFRFFRSRLYTVEICKVVIYPGNVVVLRMSKPTS--FDYKSGQYVFVQCP-SVSKFEWHPFSITSSP-GDDYLSIHI 675
Cdd:COG4097 203 YSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDgSPFWEEAHPFSISSAPgGDGRLRFTI 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 676 RQRGDWTEGIKKafsvvchapeagksglLRadvPNQRsfpeLLIDGPYGA-PAQDHWKYDVVLLVGLGIGATPFVSILRD 754
Cdd:COG4097 283 KALGDFTRRLGR----------------LK---PGTR----VYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRA 339


                .
gi 42566436 755 L 755
Cdd:COG4097 340 L 340
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
609-756 5.19e-10

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 60.57  E-value: 5.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 609 SRLYTVEICKVVIYPGNVVVLRMSKPTS---FDYKSGQYVFVQCPSVSKFEWHPFSITSSPGDDYLSIHIRqrgdwtegi 685
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVK--------- 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42566436 686 kkafsvvcHAPEAGKSGLLRADV-PNQRsfpeLLIDGPYG-----APAQDHwkydvVLLVGLGIGATPFVSILRDLL 756
Cdd:COG1018  72 --------RVPGGGGSNWLHDHLkVGDT----LEVSGPRGdfvldPEPARP-----LLLIAGGIGITPFLSMLRTLL 131
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 422-560 4.85e-07

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: 49.57  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   422 NMALILLPVCRNTITylrstALSHSVPFDDCINFHKTISVAIISAMLLHATSHLACDfpriLASTDTDYKRYLVKYFGVt 501
Cdd:pfam01794   8 LLPLLLLLALRNNPL-----EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW----LRFSLEGILDLLLKRPYN- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42566436   502 rptyfglvntpvgITGIIMVAFMLIAFTLASRRCRRNltklpkpfdkltGYNAFWYSHH 560
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHI 111
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 238-283 8.48e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.60  E-value: 8.48e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 42566436 238 KINLQELYEFWYQITDESFDSRLQIFFNMV-KNGDGRITENEVKEII 283
Cdd:cd00051  16 TISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELM 62
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 159-258 3.22e-46

Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory burst NADPH oxidase proteins which produce reactive oxygen species as a defence mechanism. It tends to occur to the N-terminus of an EF-hand (pfam00036), which suggests a direct regulatory effect of Ca2+ on the activity of the NADPH oxidase in plants.


Pssm-ID: 462469  Cd Length: 100  Bit Score: 160.44  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   159 NRDGSGTERAIHGLKFIS-SKENGIVDWNDVQNNFAHLSKDGYLFKSDFAHCIGLENenSKEFADELFDALCRRRRIMVD 237
Cdd:pfam08414   2 DRTKSGAARALKGLRFISkTDGGEGAGWKAVEKRFDKLAVDGLLPRSKFGECIGMKD--SKEFAGELFDALARRRGITGD 79

                          90       100
                  ....*....|....*....|.
gi 42566436   238 KINLQELYEFWYQITDESFDS 258
Cdd:pfam08414  80 SITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
733-923 2.36e-44

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 157.12  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   733 YDVVLLVGLGIGATPFVSILRDLLNNIikqqeqaecisgscsnsnissdhsfsclnseaasripqtqrKTLNTKNAYFYW 812
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKS-----------------------------------------KKLKTKKIKFYW 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   813 VTREQGSFDWFKEIMNEIADSDRKgVIEMHNYLTSVYEEGD-----TRSNLLTMIQTLNHAKNGVDIfsgtkVRTHFGRP 887
Cdd:pfam08030  40 VVRDLSSLEWFKDVLNELEELKEL-NIEIHIYLTGEYEAEDasdqsDSSIRSENFDSLMNEVIGVDF-----VEFHFGRP 113

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 42566436   888 KWKKVLSKISTKHRNARIGVFYCGVPSLGKELSTLC 923
Cdd:pfam08030 114 NWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 616-849 1.71e-42

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: 154.00  E-value: 1.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 616 ICKVVIYP-GNVVVLRMSKPTSFDYKSGQYVFVQCPSV-SKFEWHPFSITSSPGD--DYLSIHIR-QRGDWTEGIKKAFS 690
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRaKKGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 691 VvchapeagksgllradvPNQRSFPELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLNNIikqqeqaecis 770
Cdd:cd06186  81 S-----------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS----------- 132

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42566436 771 gscsnsnissdhsfsclnseaasripqtqRKTLNTKNAYFYWVTREQGSFDWFKEIMNEIADSDRKGVIemHNYLTSVY 849
Cdd:cd06186 133 -----------------------------SKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVV 180
FAD_binding_8 pfam08022
FAD-binding domain;
612-727 1.23e-37

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 136.31  E-value: 1.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   612 YTVEICKVVIYPGNVVVLRMSKPT-SFDYKSGQYVFVQC-PSVSKFEWHPFSITSSPGDDYLSIHIRQRGDWTEGIKKAF 689
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYL 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 42566436   690 SVVCHAPEAgksgllradvpNQRSFPELLIDGPYGAPA 727
Cdd:pfam08022  82 SSSCPKSPE-----------NGKDKPRVLIEGPYGPPS 108
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 552-831 1.59e-20

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 97.23  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  552 YNAFWYSHHLLltvyvllvIHGVSLYLEHKWYRKTVWMYLAVpvLLYVGERIFRFFRSRLYTVeICKVVIYPGNVVVLRM 631
Cdd:PLN02844 263 FEIFYYTHHLY--------IVFLIFFLFHAGDRHFYMVFPGI--FLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVL 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  632 SKPTSFDYKSGQYVFVQCPSVSKFEWHPFSITSSPG--DDYLSIHIRQRGDWTEgikkafSVVCHAPEAGKSGllradvP 709
Cdd:PLN02844 332 PKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMSVIIKCEGGWTN------SLYNKIQAELDSE------T 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  710 NQRSFPELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLN---NIIKQQEQAECISGSCSNSNIssdhsfsC 786
Cdd:PLN02844 400 NQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASqssSRYRFPKRVQLIYVVKKSQDI-------C 472

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 42566436  787 LNSEAASRIPQTQRKTLNTKNAYFywVTREQGSFDWFKEIMNEIA 831
Cdd:PLN02844 473 LLNPISSLLLNQSSNQLNLKLKVF--VTQEEKPNATLRELLNQFS 515
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
450-755 4.40e-19

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 91.11  E-value: 4.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 450 DDCINFHKTISVAIISAMLLHatshlacdfPRILASTdtdykrYLVKYFGVTRPTYFGLVNTP------VGITGII-MVA 522
Cdd:COG4097  75 DRLYRLHKWLGILALVLALAH---------PLLLLGP------KWLVGWGGLPARLAALLTLLrglaelLGEWAFYlLLA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 523 FMLIAFTlasrrcRRnltKLPkpfdkltgYNAFWYSHHLLLTVYVLLVIHGVSL---YLEHKWYRKTVWMYLAVPVLLYV 599
Cdd:COG4097 140 LVVLSLL------RR---RLP--------YELWRLTHRLLAVAYLLLAFHHLLLggpFYWSPPAGVLWAALAAAGLAAAV 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 600 GERIFRFFRSRLYTVEICKVVIYPGNVVVLRMSKPTS--FDYKSGQYVFVQCP-SVSKFEWHPFSITSSP-GDDYLSIHI 675
Cdd:COG4097 203 YSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDgSPFWEEAHPFSISSAPgGDGRLRFTI 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 676 RQRGDWTEGIKKafsvvchapeagksglLRadvPNQRsfpeLLIDGPYGA-PAQDHWKYDVVLLVGLGIGATPFVSILRD 754
Cdd:COG4097 283 KALGDFTRRLGR----------------LK---PGTR----VYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRA 339


                .
gi 42566436 755 L 755
Cdd:COG4097 340 L 340
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 625-757 1.22e-17

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: 82.88  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 625 NVVVLRMSKPTSFDYKSGQYVFVQCPSVSKFEWHPFSITSSPGD-DYLSIHIRqrgdwtegikkafsvvcHAPEAGKSGL 703
Cdd:cd00322   9 DVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVK-----------------IVPGGPFSAW 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42566436 704 LRADVPNQrsfpELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLN 757
Cdd:cd00322  72 LHDLKPGD----EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAA 121
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 619-755 1.40e-16

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: 79.61  E-value: 1.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 619 VVIYPGNVVVLRMSKPT-SFDYKSGQYVFVQCPSVSKFEWHPFSITSSPGDDY-LSIHIRQRGDWTEGIKKAfsvvchap 696
Cdd:cd06198   2 RVTEVRPTTTLTLEPRGpALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAER-------- 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42566436 697 eagksglLRadvPNQRsfpeLLIDGPYGAPAQDHWKYDVVLLVGlGIGATPFVSILRDL 755
Cdd:cd06198  74 -------LK---PGTR----VTVEGPYGRFTFDDRRARQIWIAG-GIGITPFLALLEAL 117
PLN02292 PLN02292
ferric-chelate reductase
 597-756 3.15e-16

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 83.38  E-value: 3.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  597 LYVGERIFRFFRSRlYTVEICKVVIYPGNVVVLRMSKPTSFDYKSGQYVFVQCPSVSKFEWHPFSITSSPG--DDYLSIH 674
Cdd:PLN02292 311 IFLVDRFLRFLQSR-NNVKLVSARVLPCDTVELNFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSKlePEKLSVM 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  675 IRQRGDWTEGIKKAFSVVCHAPEAGKSgllradvpnqrsfpellIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRD 754
Cdd:PLN02292 390 IKSQGKWSTKLYHMLSSSDQIDRLAVS-----------------VEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRD 452


                 ..
gi 42566436  755 LL 756
Cdd:PLN02292 453 LI 454
PLN02631 PLN02631
ferric-chelate reductase
 552-756 6.40e-16

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 82.40  E-value: 6.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  552 YNAFWYSHHLLLTVYVLLVIH-GVSlylehkwyrktvWMYLAVP-VLLYVGERIFRFF----RSRLYTVEIckvviYPGN 625
Cdd:PLN02631 259 FELFFYTHHLYGLYIVFYVIHvGDS------------WFCMILPnIFLFFIDRYLRFLqstkRSRLVSARI-----LPSD 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  626 VVVLRMSKPTSFDYKSGQYVFVQCPSVSKFEWHPFSITSSPG--DDYLSIHIRQRGDWTEGIKKAFSVVCHAPEAGKsgl 703
Cdd:PLN02631 322 NLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNleKDTLSVVIRRQGSWTQKLYTHLSSSIDSLEVST--- 398

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 42566436  704 lradvpnqrsfpelliDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLL 756
Cdd:PLN02631 399 ----------------EGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELI 435
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
609-756 5.19e-10

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 60.57  E-value: 5.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 609 SRLYTVEICKVVIYPGNVVVLRMSKPTS---FDYKSGQYVFVQCPSVSKFEWHPFSITSSPGDDYLSIHIRqrgdwtegi 685
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVK--------- 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42566436 686 kkafsvvcHAPEAGKSGLLRADV-PNQRsfpeLLIDGPYG-----APAQDHwkydvVLLVGLGIGATPFVSILRDLL 756
Cdd:COG1018  72 --------RVPGGGGSNWLHDHLkVGDT----LEVSGPRGdfvldPEPARP-----LLLIAGGIGITPFLSMLRTLL 131
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 616-758 1.35e-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: 56.57  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 616 ICKVVIYPGNVVVLRMSKP-TSFDYKSGQYVFVQCPSVSKFEWHPFSI-TSSPGDDYLSIHIRQRGdwtegikkafsvvc 693
Cdd:cd06192   1 IVKKEQLEPNLVLLTIKAPlAARLFRPGQFVFLRNFESPGLERIPLSLaGVDPEEGTISLLVEIRG-------------- 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566436 694 hapeaGKSGLLRADVPNQrsfpELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLNN 758
Cdd:cd06192  67 -----PKTKLIAELKPGE----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAKKLAAN 122
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 629-758 1.53e-08

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). 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+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 56.46  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 629 LRMSKPTSFDYKSGQYVFVQCPSVSKFewhPFSITSSPG-DDYLSIHIRQRGDWTEGIkkafsvvcHAPEAGKSGLLRad 707
Cdd:cd06221  18 LEDDDEELFTFKPGQFVMLSLPGVGEA---PISISSDPTrRGPLELTIRRVGRVTEAL--------HELKPGDTVGLR-- 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42566436 708 vpnqrsfpellidGPYGAP-----AQDHwkyDVVLLVGlGIGATPFVSILRDLLNN 758
Cdd:cd06221  85 -------------GPFGNGfpveeMKGK---DLLLVAG-GLGLAPLRSLINYILDN 123
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 626-756 9.35e-08

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 53.75  E-value: 9.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 626 VVVLRMSKPtsFDYKSGQYVFVQCPSVSKfEWHPFSITSSPGDD-YLSIHIRqrgdwtegikkafsvvchAPEAGK-SGL 703
Cdd:cd06187  13 VVRLQLDQP--LPFWAGQYVNVTVPGRPR-TWRAYSPANPPNEDgEIEFHVR------------------AVPGGRvSNA 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42566436 704 LRADV-PNQRsfpeLLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLL 756
Cdd:cd06187  72 LHDELkVGDR----VRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDAL 121
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 612-756 3.20e-07

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: 52.24  E-value: 3.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 612 YTVEICKVVIYPGNVVVLRMSKPTSFDYKSGQYVFVqcpSVSKFEW----HPFSITSSPGDDYLSIHIRQRGDwtegikk 687
Cdd:cd06196   1 HTVTLLSIEPVTHDVKRLRFDKPEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVLEFVIKSYPD------- 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 688 afsvvcHAPEAGKSGLLRA-DvpnqrsfpELLIDGPYGApAQDhwKYDVVLLVGlGIGATPFVSILRDLL 756
Cdd:cd06196  71 ------HDGVTEQLGRLQPgD--------TLLIEDPWGA-IEY--KGPGVFIAG-GAGITPFIAILRDLA 122
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 422-560 4.85e-07

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: 49.57  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436   422 NMALILLPVCRNTITylrstALSHSVPFDDCINFHKTISVAIISAMLLHATSHLACDfpriLASTDTDYKRYLVKYFGVt 501
Cdd:pfam01794   8 LLPLLLLLALRNNPL-----EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW----LRFSLEGILDLLLKRPYN- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42566436   502 rptyfglvntpvgITGIIMVAFMLIAFTLASRRCRRNltklpkpfdkltGYNAFWYSHH 560
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHI 111
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 627-756 1.73e-06

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 49.96  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 627 VVLRMSKPtsFDYKSGQYVFVQCPSvskFEWHPFSITSSP-GDDYLSIHIRQRgdwtegikkafsvvchaPEAGKSGLLR 705
Cdd:cd06194  14 VRLEPDRP--LPYLPGQYVNLRRAG---GLARSYSPTSLPdGDNELEFHIRRK-----------------PNGAFSGWLG 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42566436 706 ADV-PNQRsfpeLLIDGPYG-APAQDHWKYDVVLLVGLGIGATPFVSILRDLL 756
Cdd:cd06194  72 EEArPGHA----LRLQGPFGqAFYRPEYGEGPLLLVGAGTGLAPLWGIARAAL 120
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 637-758 2.44e-06

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins 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 portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 49.85  E-value: 2.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 637 FDYKSGQYVFVQCPSVSKFEWHPFSITSSPGDDYLSIhirqrgdwteGIKK----AFSV-VCHAPEAGKSglLRADVPnq 711
Cdd:cd06214  31 FRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELRI----------TVKRvpggRFSNwANDELKAGDT--LEVMPP-- 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42566436 712 rsfpelliDGPYGAPAQDHwKYDVVLLVGlGIGATPFVSILRDLLNN 758
Cdd:cd06214  97 --------AGRFTLPPLPG-ARHYVLFAA-GSGITPVLSILKTALAR 133
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 627-755 7.58e-05

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 45.01  E-value: 7.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 627 VVLRMSKPTSFDYKSGQYVFVQCPSVSkfEWHPFSITSSPGD-DYLSIHIRQrgdwtegikkafsvvchAPEAGKSGLLR 705
Cdd:cd06212  18 LRLRLEEPEPIKFFAGQYVDITVPGTE--ETRSFSMANTPADpGRLEFIIKK-----------------YPGGLFSSFLD 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42566436 706 ADV-PNQrsfpELLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDL 755
Cdd:cd06212  79 DGLaVGD----PVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDM 125
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 637-758 1.79e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 44.09  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  637 FDYKSGQYVFVQCPSVSKFEWHPFSItSSPGDDYLSIHIRQRGdwtEGIKKAFSVvchapeagKSGllraDvpnqrsfpE 716
Cdd:PRK00054  30 FDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVG---EGTKKLSKL--------KEG----D--------E 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 42566436  717 LLIDGPYGAPAQDHWKYDVVLLVGLGIGATPFVSILRDLLNN 758
Cdd:PRK00054  86 LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKK 127
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 614-755 2.55e-04

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: 43.39  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436 614 VEICKVVIYPGNVVVLRMSKptSFDYKSGQYVFVQCPSVSKFewhPFSITSSPGDDylSIHIRQRGDWTEGikkafsvvC 693
Cdd:cd06220   1 VTIKEVIDETPTVKTFVFDW--DFDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN--SITVKKVGEATSA--------L 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42566436 694 HAPEAGKsgllradvpnqrsfpELLIDGPYGAPAQDhwKYDVVLLVGLGIGATPFVSILRDL 755
Cdd:cd06220  66 HDLKEGD---------------KLGIRGPYGNGFEL--VGGKVLLIGGGIGIAPLAPLAERL 110
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 636-761 3.08e-04

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 43.64  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566436  636 SFDYKSGQYVFVQCPSVSKFewhPFSITSSPG-DDYLSIHIRQRGDWTEGIKKafsvvchapeagksgLLRADVpnqrsf 714
Cdd:PRK08345  35 SFTFKPGQFVQVTIPGVGEV---PISICSSPTrKGFFELCIRRAGRVTTVIHR---------------LKEGDI------ 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 42566436  715 peLLIDGPYGA--PAqDHWKYDVVLLVGLGIGATPFVSILRDLLNNIIK 761
Cdd:PRK08345  91 --VGVRGPYGNgfPV-DEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWK 136
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 617-676 1.09e-03

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: 41.38  E-value: 1.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566436 617 CKVV-IYP--GNVVVLRMSKPTSFDYKSGQYVFVQCPSVSKFewhPFSITSSP-GDDYLSIHIR 676
Cdd:cd06189   1 CKVEsIEPlnDDVYRVRLKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPhEDGEIELHIR 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 238-283 8.48e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.60  E-value: 8.48e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 42566436 238 KINLQELYEFWYQITDESFDSRLQIFFNMV-KNGDGRITENEVKEII 283
Cdd:cd00051  16 TISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELM 62
 
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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