NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|320151123|gb|ADW22501|]
View 

conserved hypothetical protein [Thermus scotoductus SA-01]

Protein Classification

flavodoxin family protein( domain architecture ID 10002025)

flavodoxin family protein is an electron-transfer flavoprotein, such as Methanosarcina thermophila iron-sulfur flavoprotein (Isf) and Clostridium saccharobutylicum flavodoxin, which are [4Fe-4S] cluster-binding electron-transfer flavoproteins

CATH:  3.40.50.360
Gene Ontology:  GO:0009055|GO:0010181
SCOP:  4003377

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
13-202 4.89e-46

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


:

Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 150.85  E-value: 4.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  13 RVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPFPFCVGNYsqdptscGPDTCVQGpwDGFGKIADKLIRA 92
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCG-------GTGKCVIK--DDMNAIYEKLLEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  93 DAVVFATPVYWFSVSARMKALLERMTSMENQGLLNLGKPMVLLAVAEEEGASQALSQMLLPLSYMGFVLAPLGLVYAHYR 172
Cdd:COG0655   72 DGIIFGSPTYFGNMSAQLKAFIDRLYALWAKGKLLKGKVGAVFTTGGHGGAEATLLSLNTFLLHHGMIVVGLPPYGAVGG 151
                        170       180       190
                 ....*....|....*....|....*....|
gi 320151123 173 GAVSLKENTELMEDARIAGENLVLMAEKLR 202
Cdd:COG0655  152 GGPGDVLDEEGLATARELGKRLAELAKKLK 181
 
Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
13-202 4.89e-46

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 150.85  E-value: 4.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  13 RVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPFPFCVGNYsqdptscGPDTCVQGpwDGFGKIADKLIRA 92
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCG-------GTGKCVIK--DDMNAIYEKLLEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  93 DAVVFATPVYWFSVSARMKALLERMTSMENQGLLNLGKPMVLLAVAEEEGASQALSQMLLPLSYMGFVLAPLGLVYAHYR 172
Cdd:COG0655   72 DGIIFGSPTYFGNMSAQLKAFIDRLYALWAKGKLLKGKVGAVFTTGGHGGAEATLLSLNTFLLHHGMIVVGLPPYGAVGG 151
                        170       180       190
                 ....*....|....*....|....*....|
gi 320151123 173 GAVSLKENTELMEDARIAGENLVLMAEKLR 202
Cdd:COG0655  152 GGPGDVLDEEGLATARELGKRLAELAKKLK 181
FMN_red pfam03358
NADPH-dependent FMN reductase;
12-171 7.35e-25

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 95.38  E-value: 7.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123   12 LRVLGVNASARTDGFTAELLDEVLEAARRrGAATERLDLVRYPFPFCVgnysQDPTSCGPDTcvqgpwDGFGKIADKLIR 91
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCD----EDLEEEQGDP------DDVQELREKIAA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123   92 ADAVVFATPVYWFSVSARMKALLERMTSMENQGLLNlGKPMVLLAVAE-EEGASQALSQMLLPLSYMGFVLAPLGLVYAH 170
Cdd:pfam03358  70 ADAIIIVTPEYNGSVSGLLKNAIDWLSRLRGGKELR-GKPVAIVSTGGgRSGGLRAVEQLRQVLAELGAIVVPSGQVAVG 148

                  .
gi 320151123  171 Y 171
Cdd:pfam03358 149 N 149
PRK09739 PRK09739
NAD(P)H oxidoreductase;
11-116 1.57e-08

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 52.78  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  11 SLRVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPFpfcvgnysqDPTSCGPDtcvQGPWDGFGK------ 84
Cdd:PRK09739   3 SMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGF---------DPVLTPED---EPDWKNPDKryspev 70
                         90       100       110
                 ....*....|....*....|....*....|....
gi 320151123  85 --IADKLIRADAVVFATPVYWFSVSARMKALLER 116
Cdd:PRK09739  71 hqLYSELLEHDALVFVFPLWWYSFPAMLKGYIDR 104
 
Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
13-202 4.89e-46

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 150.85  E-value: 4.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  13 RVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPFPFCVGNYsqdptscGPDTCVQGpwDGFGKIADKLIRA 92
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCG-------GTGKCVIK--DDMNAIYEKLLEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  93 DAVVFATPVYWFSVSARMKALLERMTSMENQGLLNLGKPMVLLAVAEEEGASQALSQMLLPLSYMGFVLAPLGLVYAHYR 172
Cdd:COG0655   72 DGIIFGSPTYFGNMSAQLKAFIDRLYALWAKGKLLKGKVGAVFTTGGHGGAEATLLSLNTFLLHHGMIVVGLPPYGAVGG 151
                        170       180       190
                 ....*....|....*....|....*....|
gi 320151123 173 GAVSLKENTELMEDARIAGENLVLMAEKLR 202
Cdd:COG0655  152 GGPGDVLDEEGLATARELGKRLAELAKKLK 181
FMN_red pfam03358
NADPH-dependent FMN reductase;
12-171 7.35e-25

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 95.38  E-value: 7.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123   12 LRVLGVNASARTDGFTAELLDEVLEAARRrGAATERLDLVRYPFPFCVgnysQDPTSCGPDTcvqgpwDGFGKIADKLIR 91
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCD----EDLEEEQGDP------DDVQELREKIAA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123   92 ADAVVFATPVYWFSVSARMKALLERMTSMENQGLLNlGKPMVLLAVAE-EEGASQALSQMLLPLSYMGFVLAPLGLVYAH 170
Cdd:pfam03358  70 ADAIIIVTPEYNGSVSGLLKNAIDWLSRLRGGKELR-GKPVAIVSTGGgRSGGLRAVEQLRQVLAELGAIVVPSGQVAVG 148

                  .
gi 320151123  171 Y 171
Cdd:pfam03358 149 N 149
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
13-194 5.90e-18

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: 78.53  E-value: 5.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123   13 RVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPfpfcvgnysqDPTSCGPDTCVQGPWDGFGKIA---DKL 89
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYALF----------LPVLDAEDLADLTYPQGAADVEseqEEL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123   90 IRADAVVFATPVYWFSVSARMKALLER----------MTSMENQGLLnLGKPMVLL----AVAEEEGAS----QALSQML 151
Cdd:pfam02525  72 LAADVIVFQFPLYWFSVPALLKGWIDRvlragfafkyEEGGPGGGGL-LGKKVLVIvttgGPEYAYGKGgyngFSLDELL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 320151123  152 LPL----SYMGFvlAPLGLVYAHyrGAVSLKENTELMEDARIAGENL 194
Cdd:pfam02525 151 PYLrgilGFCGI--TDLPPFAVE--GTAGPEDEAALAEALERYEERL 193
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
12-166 8.12e-17

NAD(P)H-dependent FMN reductase [Energy production and conversion];


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 74.42  E-value: 8.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  12 LRVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPFPFcvgnYSQDPTSCGPDTCVQgpwdgfgKIADKLIR 91
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPL----YDEDLEADGAPPAVK-------ALREAIAA 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320151123  92 ADAVVFATPVYWFSVSARMKALLERMTsmenQGLLNlGKPMVLLAVA-EEEGASQALSQMLLPLSYMGFVLAPLGL 166
Cdd:COG0431   70 ADGVVIVTPEYNGSYPGVLKNALDWLS----RSELA-GKPVALVSTSgGARGGLRALEHLRPVLSELGAVVLPPQV 140
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
13-164 6.43e-10

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 56.39  E-value: 6.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  13 RVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDL--VRYPFPFCVGNYSQDPTscgPDTCVQgpwdgfgKIADKLI 90
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLyaEGFDPVLSAADFYRDGP---LPIDVA-------AEQELLL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  91 RADAVVFATPVYWFSVSARMKALLER---------MTSMENQGLLNlGKPMVLLAVA-------EEEGASQALSQMLLP- 153
Cdd:COG2249   71 WADHLVFQFPLWWYSMPALLKGWIDRvltpgfaygYGGGYPGGLLK-GKKALLVVTTggpeeaySRLGYGGPIEELLFRg 149
                        170
                 ....*....|...
gi 320151123 154 -LSYMGF-VLAPL 164
Cdd:COG2249  150 tLGYCGMkVLPPF 162
PRK09739 PRK09739
NAD(P)H oxidoreductase;
11-116 1.57e-08

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 52.78  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320151123  11 SLRVLGVNASARTDGFTAELLDEVLEAARRRGAATERLDLVRYPFpfcvgnysqDPTSCGPDtcvQGPWDGFGK------ 84
Cdd:PRK09739   3 SMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGF---------DPVLTPED---EPDWKNPDKryspev 70
                         90       100       110
                 ....*....|....*....|....*....|....
gi 320151123  85 --IADKLIRADAVVFATPVYWFSVSARMKALLER 116
Cdd:PRK09739  71 hqLYSELLEHDALVFVFPLWWYSFPAMLKGYIDR 104
 
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