NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1188412680|ref|WP_085533433|]
View 

MULTISPECIES: NAD(P)H:quinone oxidoreductase [Pseudomonas]

Protein Classification

NAD(P)H:quinone oxidoreductase( domain architecture ID 10012077)

NAD(P)H:quinone oxidoreductase catalyzes the transfer of electrons from NADH to ubiquinone

CATH:  3.40.50.360
EC:  1.6.5.2
Gene Ontology:  GO:0010181|GO:0050660|GO:0030554|GO:0003955
SCOP:  3001217

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-197 8.62e-126

NAD(P)H:quinone oxidoreductase; Provisional


:

Pssm-ID: 179647  Cd Length: 200  Bit Score: 352.69  E-value: 8.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   1 MAKVLVLYHSMYGHIETMAQSVSEGARSVPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTPTR 80
Cdd:PRK03767    1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADYDAIIFGTPTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  81 FGNMSGQMRNFLDQTGGLWAKGGLVGKLASVFTSTGTG-GGQEMTITSTWTTLAHHGMIIVPIGYSSPALFDTSSVGGGT 159
Cdd:PRK03767   81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1188412680 160 PYGASTIAGGDGSRQPDARELEIARHQGQYVAQLAVKL 197
Cdd:PRK03767  161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKL 198
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-197 8.62e-126

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 352.69  E-value: 8.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   1 MAKVLVLYHSMYGHIETMAQSVSEGARSVPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTPTR 80
Cdd:PRK03767    1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADYDAIIFGTPTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  81 FGNMSGQMRNFLDQTGGLWAKGGLVGKLASVFTSTGTG-GGQEMTITSTWTTLAHHGMIIVPIGYSSPALFDTSSVGGGT 159
Cdd:PRK03767   81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1188412680 160 PYGASTIAGGDGSRQPDARELEIARHQGQYVAQLAVKL 197
Cdd:PRK03767  161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKL 198
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 2-197 3.02e-107

NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and slightly larger than flavodoxin. It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. In E. coli, this protein was earlier reported to be produced during stationary phase, bind to the trp repressor, and make trp operon repression more efficient. WrbA does not interact with the trp operator by itself. Members are found in species in which homologs of the E. coli trp operon repressor TrpR (SP:P03032) are not detected. [Energy metabolism, Electron transport]


Pssm-ID: 130816 [Multi-domain]  Cd Length: 197  Bit Score: 305.67  E-value: 3.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   2 AKVLVLYHSMYGHIETMAQSVSEGARSVPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTPTRF 81
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTDQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  82 GNMSGQMRNFLDQTGGLWAKGGLVGKLASVFTSTGTG-GGQEMTITSTWTTLAHHGMIIVPIGYSSPALFDTSSVGGGTP 160
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQhGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1188412680 161 YGASTIAGGDGSRQPDARELEIARHQGQYVAQLAVKL 197
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-198 9.65e-52

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 164.33  E-value: 9.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   3 KVLVLYHS--MYGHIETMAQSVSEGARSvPGVEVTLKRVPETM--DPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTP 78
Cdd:COG0655     1 KILVINGSprKNGNTAALAEAVAEGAEE-AGAEVELIRLADLDikPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFGSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  79 TRFGNMSGQMRNFLDQTGGLWAKGG-LVGKLASVFTSTGtGGGQEMTITSTWTTLAHHGMIIVPIGysspalfdtssvgg 157
Cdd:COG0655    80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG-HGGAEATLLSLNTFLLHHGMIVVGLP-------------- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1188412680 158 gtPYGASTIAGGDGSRQPDAreLEIARHQGQYVAQLAVKLS 198
Cdd:COG0655   145 --PYGAVGGGGPGDVLDEEG--LATARELGKRLAELAKKLK 181
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-146 1.15e-12

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 62.64  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   3 KVLVLYHSMY--GHIETMAQSVSEGARsvPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGE-LGDYDAIILGTPT 79
Cdd:pfam03358   2 KILAISGSPRkgSNTRKLARWAAELLE--EGAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREkIAAADAIIIVTPE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1188412680  80 RFGNMSGQMRNFLDQTGGLWAKGGLVGK-LASVFTSTGTGGGQEMTItSTWTTLAHHGMIIVPIGYSS 146
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKpVAIVSTGGGRSGGLRAVE-QLRQVLAELGAIVVPSGQVA 146
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-197 8.62e-126

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 352.69  E-value: 8.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   1 MAKVLVLYHSMYGHIETMAQSVSEGARSVPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTPTR 80
Cdd:PRK03767    1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADYDAIIFGTPTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  81 FGNMSGQMRNFLDQTGGLWAKGGLVGKLASVFTSTGTG-GGQEMTITSTWTTLAHHGMIIVPIGYSSPALFDTSSVGGGT 159
Cdd:PRK03767   81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1188412680 160 PYGASTIAGGDGSRQPDARELEIARHQGQYVAQLAVKL 197
Cdd:PRK03767  161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKL 198
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 2-197 3.02e-107

NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and slightly larger than flavodoxin. It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. In E. coli, this protein was earlier reported to be produced during stationary phase, bind to the trp repressor, and make trp operon repression more efficient. WrbA does not interact with the trp operator by itself. Members are found in species in which homologs of the E. coli trp operon repressor TrpR (SP:P03032) are not detected. [Energy metabolism, Electron transport]


Pssm-ID: 130816 [Multi-domain]  Cd Length: 197  Bit Score: 305.67  E-value: 3.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   2 AKVLVLYHSMYGHIETMAQSVSEGARSVPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTPTRF 81
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTDQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  82 GNMSGQMRNFLDQTGGLWAKGGLVGKLASVFTSTGTG-GGQEMTITSTWTTLAHHGMIIVPIGYSSPALFDTSSVGGGTP 160
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQhGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1188412680 161 YGASTIAGGDGSRQPDARELEIARHQGQYVAQLAVKL 197
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-198 9.65e-52

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 164.33  E-value: 9.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   3 KVLVLYHS--MYGHIETMAQSVSEGARSvPGVEVTLKRVPETM--DPEAFKAAHGKVDQSAAVATPGELGDYDAIILGTP 78
Cdd:COG0655     1 KILVINGSprKNGNTAALAEAVAEGAEE-AGAEVELIRLADLDikPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFGSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680  79 TRFGNMSGQMRNFLDQTGGLWAKGG-LVGKLASVFTSTGtGGGQEMTITSTWTTLAHHGMIIVPIGysspalfdtssvgg 157
Cdd:COG0655    80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG-HGGAEATLLSLNTFLLHHGMIVVGLP-------------- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1188412680 158 gtPYGASTIAGGDGSRQPDAreLEIARHQGQYVAQLAVKLS 198
Cdd:COG0655   145 --PYGAVGGGGPGDVLDEEG--LATARELGKRLAELAKKLK 181
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-120 6.10e-14

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 69.09  E-value: 6.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   3 KVLVLYHSMYGHIETMAQSVSEGARSvPGVEVTLKRVPETmdpeafkaahgkvDQSAAVAtpgELGDYDAIILGTPTRFG 82
Cdd:COG0426   248 KVVIVYASMYGNTEKMAEAIAEGLTE-EGVKVKLYDLEKT-------------DPSEIIT---EIFDAKGIVIGSPTYNG 310

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1188412680  83 NMSGQMRNFLDQTGGLWAKgglvGKLASVFTSTGTGGG 120
Cdd:COG0426   311 GAFPPIADLLGYLKGLAPK----NKLAGAFGSYGWSGE 344
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-146 1.15e-12

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 62.64  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   3 KVLVLYHSMY--GHIETMAQSVSEGARsvPGVEVTLKRVPETMDPEAFKAAHGKVDQSAAVATPGE-LGDYDAIILGTPT 79
Cdd:pfam03358   2 KILAISGSPRkgSNTRKLARWAAELLE--EGAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREkIAAADAIIIVTPE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1188412680  80 RFGNMSGQMRNFLDQTGGLWAKGGLVGK-LASVFTSTGTGGGQEMTItSTWTTLAHHGMIIVPIGYSS 146
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKpVAIVSTGGGRSGGLRAVE-QLRQVLAELGAIVVPSGQVA 146
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 4-121 6.92e-10

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 54.91  E-value: 6.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   4 VLVLYHSMYGHIETMAQSVSEGARsvpGVEVTLKRVPEtmdpeafkaahgkvdqsaavATPGELGDYDAIILGTPTRFGN 83
Cdd:COG0716     1 ILIVYGSTTGNTEKVAEAIAEALG---AAGVDLFEIED--------------------ADLDDLEDYDLLILGTPTWAGE 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1188412680  84 MSGQMRNFLDQtgglwAKGGLVGKLASVFtstGTGGGQ 121
Cdd:COG0716    58 LPDDWEDFLEE-----LKEDLSGKKVALF---GTGDSS 87
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 4-119 3.34e-07

flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]


Pssm-ID: 273789 [Multi-domain]  Cd Length: 140  Bit Score: 47.72  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   4 VLVLYHSMYGHIETMAQSVSEGARSVpGVEVTLKRVPEtMDPEAFKaahgkvdqsaavatpgelgDYDAIILGTPTrFGN 83
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEA-GAEVDLLEVAD-ADAEDLL-------------------SYDAVLLGCST-WGD 58

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1188412680  84 ---MSGQMRNFLDQTGGLwakgGLVGKLASVFTSTGTGG 119
Cdd:TIGR01753  59 edlEQDDFEPFFEELEDI----DLGGKKVALFGSGDWGY 93
Flavodoxin_1 pfam00258
Flavodoxin;
6-136 9.66e-07

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 46.21  E-value: 9.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   6 VLYHSMYGHIETMAQSVSEGARS--VPGVEVTLKRVPETM-DPEAFKAAhgkvdqSAAVATPGElGD--------YDAII 74
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEagFEVDVVDLDDVDETLsEIEEEDLL------LVVVSTWGE-GEppdnakpfVDWLL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1188412680  75 LGTPTRFGNMSG---QMRNFLDQTGGL--WAKGGLVGKLASVFTST--GTGGGQEMTITSTWTTLAHHG 136
Cdd:pfam00258  74 LFGTLEDGDLSGlkyAVFGLGDSGYEGfcGAAKKLDEKLSELGASRvgPLGEGDEDPQEDGLEEAFEAW 142
PRK05568 PRK05568
flavodoxin; Provisional
 1-124 2.98e-06

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 45.18  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   1 MAKVLVLYHSMYGHIETMAQSVSEGARSvPGVEVTLKRVPEtmdpeafkaahgkvdqsaavATPGELGDYDAIILGTPTR 80
Cdd:PRK05568    1 MKKINIIYWSGTGNTEAMANLIAEGAKE-NGAEVKLLNVSE--------------------ASVDDVKGADVVALGSPAM 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1188412680  81 FGNM--SGQMRNFLDQTGGLWAkgglvGKLASVFTSTGTGGGQEMT 124
Cdd:PRK05568   60 GDEVleEGEMEPFVESISSLVK-----GKKLVLFGSYGWGDGEWMR 100
PRK05569 PRK05569
flavodoxin; Provisional
 1-94 3.51e-06

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 44.82  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   1 MAKVLVLYHSMYGHIETMAQSVSEGARSVpGVEVTLKRVPEtmdpeafkaahgkvdqsaavATPGELGDYDAIILGTPTR 80
Cdd:PRK05569    1 MKKVSIIYWSCGGNVEVLANTIADGAKEA-GAEVTIKHVAD--------------------AKVEDVLEADAVAFGSPSM 59

                          90
                  ....*....|....*.
gi 1188412680  81 FGNMSGQ--MRNFLDQ 94
Cdd:PRK05569   60 DNNNIEQeeMAPFLDQ 75
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 2-94 4.97e-06

Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport and metabolism];


Pssm-ID: 443673  Cd Length: 179  Bit Score: 44.89  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   2 AKVLVLYHSMYGHIETMAQSVSEGARSvPGVEVTLKrvpetmdpeafkaahgkvdqSAAVATPGELGDYDAIILGTPTRF 81
Cdd:COG4635     1 MKVLILYASRDGQTRKIAERIAEVLRE-AGHDVDLV--------------------DLEDAPDLDLAGYDAVVIGASIRY 59

                          90
                  ....*....|...
gi 1188412680  82 GNMSGQMRNFLDQ 94
Cdd:COG4635    60 GKWLPEAVRFVRR 72
PRK06756 PRK06756
flavodoxin; Provisional
 1-114 1.54e-04

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 40.25  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   1 MAKVLVLYHSMYGHIETMAQSVSEGARSVpGVEVTLKrvpETMD-PEAfkaahgkvdqsaavatpGELGDYDAIILGTPT 79
Cdd:PRK06756    1 MSKLVMIFASMSGNTEEMADHIAGVIRET-ENEIEVI---DIMDsPEA-----------------SILEQYDGIILGAYT 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1188412680  80 -RFGNMSGQMRNFLDQTGGLwakgGLVGKLASVFTS 114
Cdd:PRK06756   60 wGDGDLPDDFLDFYDAMDSI----DLTGKKAAVFGS 91
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-116 1.00e-03

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 38.47  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   3 KVLVLYhsmyGHIET------MAQSVSEGARSVpGVEVTLKRVPETMDP----EAFKAAHGKVDQSAAVATPGELGDYDA 72
Cdd:pfam02525   2 KILIIN----AHPRPgsfssrLADALVEALKAA-GHEVTVRDLYALFLPvldaEDLADLTYPQGAADVESEQEELLAADV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1188412680  73 IILGTPTRFGNMSGQMRNFLDQ----------TGGLWAKGGLVGKLASVFTSTG 116
Cdd:pfam02525  77 IVFQFPLYWFSVPALLKGWIDRvlragfafkyEEGGPGGGGLLGKKVLVIVTTG 130
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 5-94 2.36e-03

Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that carry a molecule of non-covalently bound FMN.


Pssm-ID: 463681 [Multi-domain]  Cd Length: 144  Bit Score: 36.86  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188412680   5 LVLYHSMYGHIETMAQSVSEGARSVpGVEVTLKRVPETMDPEafkaahgkvdqsaavatpgelgDYDAIILGTPTRFGNM 84
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAEELREE-GELVDVEDVEAGEDLS----------------------SYDAVVIGASIYYGKH 57

                          90
                  ....*....|
gi 1188412680  85 SGQMRNFLDQ 94
Cdd:pfam12724  58 LPELRQFVTK 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH