NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|654964853|ref|WP_028414603|]
View 

MULTISPECIES: FMN-dependent NADH-azoreductase [Priestia]

Protein Classification

NADPH-dependent FMN reductase family protein( domain architecture ID 325)

NADPH-dependent FMN reductase family protein contains a flavodoxin-like fold, which is characterized by an open twisted/alpha beta structure consisting of five parallel beta-sheets connected by alpha-helices which surround the sheet

CATH:  3.40.50.360
Gene Ontology:  GO:0010181
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
FMN_red super family cl00438
NADPH-dependent FMN reductase;
1-210 1.17e-87

NADPH-dependent FMN reductase;


The actual alignment was detected with superfamily member PRK00170:

Pssm-ID: 469770 [Multi-domain]  Cd Length: 201  Bit Score: 256.74  E-value: 1.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAeDESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNGWKKLRshssiQDLSTDERLKV 80
Cdd:PRK00170   1 MSKVLVIKSSILG-DYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSA-----ETLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  81 GRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPemaRE 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGP---TD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 654964853 161 MGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKT 210
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA 201
 
Name Accession Description Interval E-value
PRK00170 PRK00170
azoreductase; Reviewed
 1-210 1.17e-87

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 256.74  E-value: 1.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAeDESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNGWKKLRshssiQDLSTDERLKV 80
Cdd:PRK00170   1 MSKVLVIKSSILG-DYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSA-----ETLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  81 GRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPemaRE 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGP---TD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 654964853 161 MGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKT 210
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA 201
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 2.59e-79

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 235.79  E-value: 2.59e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAEdESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNGWKKLRshssiQDLSTDERLKV 80
Cdd:COG1182    1 MMKLLHIDSSPRGE-GSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPA-----EGRTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  81 GRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPEMARE 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 654964853 161 MGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKTF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-204 1.28e-42

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: 142.09  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853    3 NVLYITAHPlaEDESLSMAVGKEFIDVYKQTHpeDDVVHLDLYQADIPYLDADVFNGWkklrshsSIQDLSTDERLKVGR 82
Cdd:pfam02525   2 KILIINAHP--RPGSFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLADL-------TYPQGAADVESEQEE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   83 LAElggqfvlADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTY-TKEGAQGLLKGKKAIHIQSRG---DVYSEGPEMA 158
Cdd:pfam02525  71 LLA-------ADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYeEGGPGGGGLLGKKVLVIVTTGgpeYAYGKGGYNG 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 654964853  159 REMGH--RYLEIMMDFFGIEAFESIIIEGQV--KFPDQIPQIKEKALQKA 204
Cdd:pfam02525 144 FSLDEllPYLRGILGFCGITDLPPFAVEGTAgpEDEAALAEALERYEERL 193
RRM1_hnRNPH_hnRNPH2_hnRNPF cd12729
RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP H , ...
 120-168 5.17e-03

RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP H , hnRNP H2, hnRNP F and similar proteins; This subgroup corresponds to the RRM1 of hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H') and hnRNP F. These represent a group of nuclear RNA binding proteins that play important roles in the regulation of alternative splicing decisions. hnRNP H and hnRNP F are two closely related proteins, both of which bind to the RNA sequence DGGGD. They are present in a complex with the tissue-specific splicing factor Fox2, and regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts. The presence of Fox 2 can allows hnRNP H and hnRNP F to better compete with the SR protein ASF/SF2 for binding to FGFR2 exon IIIc. Thus, hnRNP H and hnRNP F can function as potent silencers of FGFR2 exon IIIc inclusion through an interaction with the exonic GGG motifs. Furthermore, hnRNP H and hnRNP H2 are almost identical. Both of them have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize.


Pssm-ID: 410128 [Multi-domain]  Cd Length: 79  Bit Score: 34.75  E-value: 5.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 654964853 120 VSGKTFTYTKEGAQgllKGKKAIHIQSRGDVYSEGPEMAREMGHRYLEI 168
Cdd:cd12729   31 ASGIHFIYTREGRP---SGEAFVELESEEDVKLALKKDRETMGHRYVEV 76
 
Name Accession Description Interval E-value
PRK00170 PRK00170
azoreductase; Reviewed
 1-210 1.17e-87

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 256.74  E-value: 1.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAeDESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNGWKKLRshssiQDLSTDERLKV 80
Cdd:PRK00170   1 MSKVLVIKSSILG-DYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSA-----ETLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  81 GRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPemaRE 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGP---TD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 654964853 161 MGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKT 210
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA 201
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 2.59e-79

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 235.79  E-value: 2.59e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAEdESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNGWKKLRshssiQDLSTDERLKV 80
Cdd:COG1182    1 MMKLLHIDSSPRGE-GSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPA-----EGRTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  81 GRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPEMARE 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 654964853 161 MGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKTF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
1-211 2.01e-64

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 198.06  E-value: 2.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAEDESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNG-WKKLRShssiQDLSTDERLK 79
Cdd:PRK13556   1 MSKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGtFKAGKG----FELTEEEAKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  80 VGRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPEMAR 159
Cdd:PRK13556  77 VAVADKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKVALLNARGGVYSEGPAAEV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654964853 160 EMGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKTF 211
Cdd:PRK13556 157 EMAVKYVASMMGFFGVTNMETVVIEGHNQFPDKAEEIITAGLEEAAKVAAKF 208
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
1-211 2.07e-43

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 144.50  E-value: 2.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAEDESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIPYLDADVFNGWKKlrsHSSIQDLSTDERLKV 80
Cdd:PRK13555   1 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYK---RSQGMELTAEEEKAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  81 GRLAELGGQFVLADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHIQSRGDVYSEGPEMARE 160
Cdd:PRK13555  78 ATVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEQMAPME 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 654964853 161 MGHRYLEIMMDFFGIEAFESIIIEGQVKFPDQIPQIKEKALQKAHSMAKTF 211
Cdd:PRK13555 158 MAVNYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 208
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-204 1.28e-42

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: 142.09  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853    3 NVLYITAHPlaEDESLSMAVGKEFIDVYKQTHpeDDVVHLDLYQADIPYLDADVFNGWkklrshsSIQDLSTDERLKVGR 82
Cdd:pfam02525   2 KILIINAHP--RPGSFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLADL-------TYPQGAADVESEQEE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   83 LAElggqfvlADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTY-TKEGAQGLLKGKKAIHIQSRG---DVYSEGPEMA 158
Cdd:pfam02525  71 LLA-------ADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYeEGGPGGGGLLGKKVLVIVTTGgpeYAYGKGGYNG 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 654964853  159 REMGH--RYLEIMMDFFGIEAFESIIIEGQV--KFPDQIPQIKEKALQKA 204
Cdd:pfam02525 144 FSLDEllPYLRGILGFCGITDLPPFAVEGTAgpEDEAALAEALERYEERL 193
PRK01355 PRK01355
azoreductase; Reviewed
 1-211 1.12e-23

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 93.22  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAEDESLSMAVGKEFIDVYKQTHPEDDVVHLDLYQADIP--YLDADVFNG-WKKLRSHSSIQDLSTder 77
Cdd:PRK01355   1 MSKVLVIKGSMVAKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETKVGsvTLTSENFKTfFKEEVSDKYINQLKS--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  78 lkvgrlaelggqfvlADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTY---TKEGAQGLLKGKKAIHIQSRG---DVY 151
Cdd:PRK01355  78 ---------------VDKVVISCPMTNFNVPATLKNYLDHIAVANKTFSYkysKKGDAIGLLDHLKVQILTTQGaplGWY 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654964853 152 SEGPEMAremghrYLEIMMDFFGIEAFESIIIEGqVKFPD----QIPQIKEKALQKAHSMAKTF 211
Cdd:PRK01355 143 PWGSHTN------YLEGTWEFLGAKVVDSILLAG-TKVEPlsnkTPKEIVEEFDKEIIEKAKNF 199
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-144 2.06e-15

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 71.02  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   3 NVLYITAHPlaEDESLSMAVgkefIDVYKQTHPE--DDVVHLDLYQADI-PYLDADVFNGWKKLRshssiQDLStDERlk 79
Cdd:COG2249    1 KILIIYAHP--DPSSFNAAL----AEAAAEGLEAagHEVTVHDLYAEGFdPVLSAADFYRDGPLP-----IDVA-AEQ-- 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654964853  80 vGRLAElggqfvlADKYIFVTPMWNFSVPAIMKTYIDAITVSGKTFTYTKEGAQGLLKGKKAIHI 144
Cdd:COG2249   67 -ELLLW-------ADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLV 123
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-116 1.19e-06

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 47.00  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   1 MANVLYITAHPLAEdeSLSMAVGKEFIDVYKQTHPEddVVHLDLYQADI-PYLDADVFNGWKKLRSHSSiqdlSTDERLk 79
Cdd:PRK09739   3 SMRIYLVWAHPRHD--SLTAKVAEAIHQRAQERGHQ--VEELDLYRSGFdPVLTPEDEPDWKNPDKRYS----PEVHQL- 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654964853  80 VGRLAElggqfvlADKYIFVTPMWNFSVPAIMKTYID 116
Cdd:PRK09739  74 YSELLE-------HDALVFVFPLWWYSFPAMLKGYID 103
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
17-116 9.61e-06

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 43.99  E-value: 9.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  17 SLSMAVGKEFIDVYKQthPEDDVVHLDLYQADIPYLDADVFNGWkklrSHSSIQDLSTderlkvgRLAElggqfvlADKY 96
Cdd:COG0431   14 SFNRKLARAAAELAPA--AGAEVELIDLRDLDLPLYDEDLEADG----APPAVKALRE-------AIAA-------ADGV 73

                         90       100
                 ....*....|....*....|
gi 654964853  97 IFVTPMWNFSVPAIMKTYID 116
Cdd:COG0431   74 VIVTPEYNGSYPGVLKNALD 93
FMN_red pfam03358
NADPH-dependent FMN reductase;
38-116 1.08e-04

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 41.07  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654964853   38 DVVHLDLYQADIPYLDADVfngWKKLRSHSSIQDLSTderlkvgRLAElggqfvlADKYIFVTPMWNFSVPAIMKTYID 116
Cdd:pfam03358  32 EVELIDLADLILPLCDEDL---EEEQGDPDDVQELRE-------KIAA-------ADAIIIVTPEYNGSVSGLLKNAID 93
Flavodoxin_4 pfam12682
Flavodoxin; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that ...
 43-154 2.14e-04

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


Pssm-ID: 403777  Cd Length: 155  Bit Score: 40.06  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853   43 DLYQ--ADIPYLDADVfnGWKKLRSHSSIQDlstdeRLKVGRLAeLGGQFVLADKY--IFVT-PMWNFSVPAIMKTYIDA 117
Cdd:pfam12682  27 DLYEikPEVPYTEADL--DWNDKKSRSSVE*-----RDALSRPA-ISGTLFHPEKYevLFVGfPVWWYIAPTIINTFLES 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 654964853  118 ITVSGKTFT-YTKEGAQGLLKGKKAIHIQSRGDVYSEG 154
Cdd:pfam12682  99 YDFAGKIVVpFATSGGSGIGNCEKNLHKAYPDIVWKDG 136
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 93-209 1.25e-03

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 38.37  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964853  93 ADKYIFVTPMWNFSVPAIMKTYIDAitvsgktfTYTKEGAQGLLKGKKAIHIQSRGDvysEGPEMAREmghrYLEIMMDF 172
Cdd:COG0655   71 ADGIIFGSPTYFGNMSAQLKAFIDR--------LYALWAKGKLLKGKVGAVFTTGGH---GGAEATLL----SLNTFLLH 135

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654964853 173 FGIEaFESIIIEGQVKFPDQIPQIKEKALQKAHSMAK 209
Cdd:COG0655  136 HGMI-VVGLPPYGAVGGGGPGDVLDEEGLATARELGK 171
RRM1_hnRNPH_hnRNPH2_hnRNPF cd12729
RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP H , ...
 120-168 5.17e-03

RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein hnRNP H , hnRNP H2, hnRNP F and similar proteins; This subgroup corresponds to the RRM1 of hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H') and hnRNP F. These represent a group of nuclear RNA binding proteins that play important roles in the regulation of alternative splicing decisions. hnRNP H and hnRNP F are two closely related proteins, both of which bind to the RNA sequence DGGGD. They are present in a complex with the tissue-specific splicing factor Fox2, and regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts. The presence of Fox 2 can allows hnRNP H and hnRNP F to better compete with the SR protein ASF/SF2 for binding to FGFR2 exon IIIc. Thus, hnRNP H and hnRNP F can function as potent silencers of FGFR2 exon IIIc inclusion through an interaction with the exonic GGG motifs. Furthermore, hnRNP H and hnRNP H2 are almost identical. Both of them have been found to bind nuclear-matrix proteins. hnRNP H activates exon inclusion by binding G-rich intronic elements downstream of the 5' splice site in the transcripts of c-src, human immunodeficiency virus type 1 (HIV-1), Bcl-X, GRIN1, and myelin. It silences exons when bound to exonic elements in the transcripts of beta-tropomyosin, HIV-1, and alpha-tropomyosin. hnRNP H2 has been implicated in pre-mRNA 3' end formation. Members in this family contain three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. In addition, the family members have an extensive glycine-rich region near the C-terminus, which may allow them to homo- or heterodimerize.


Pssm-ID: 410128 [Multi-domain]  Cd Length: 79  Bit Score: 34.75  E-value: 5.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 654964853 120 VSGKTFTYTKEGAQgllKGKKAIHIQSRGDVYSEGPEMAREMGHRYLEI 168
Cdd:cd12729   31 ASGIHFIYTREGRP---SGEAFVELESEEDVKLALKKDRETMGHRYVEV 76
 
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