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Conserved domains on  [gi|1036094196|ref|WP_064663871|]
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flavodoxin family protein [Pseudoalteromonas sp. MQS005]

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

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List of domain hits

 Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-183 1.32e-34

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


:

Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 120.03  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFS--GYGHTKKVAEFVADGA-----NAQLIAIDE-----------NGDIKDTD-----WDALNNADAIIFGAPT 59
Cdd:COG0655     1 KILVINGSprKNGNTAALAEAVAEGAeeagaEVELIRLADldikpcigcggTGKCVIKDdmnaiYEKLLEADGIIFGSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  60 YMGSYPWQFKKFVDATSKVWFTMG-WKDKVFGGFTNSGslNGDKQVTLISMQTLASQHGGIWVSLGLppanklestrqdi 138
Cdd:COG0655    81 YFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG--HGGAEATLLSLNTFLLHHGMIVVGLPP------------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1036094196 139 nnLGGSVGVLVQSPTDADEtaipsgdLETARLYGERVAKIAKRLK 183
Cdd:COG0655   146 --YGAVGGGGPGDVLDEEG-------LATARELGKRLAELAKKLK 181
 
Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-183 1.32e-34

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 120.03  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFS--GYGHTKKVAEFVADGA-----NAQLIAIDE-----------NGDIKDTD-----WDALNNADAIIFGAPT 59
Cdd:COG0655     1 KILVINGSprKNGNTAALAEAVAEGAeeagaEVELIRLADldikpcigcggTGKCVIKDdmnaiYEKLLEADGIIFGSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  60 YMGSYPWQFKKFVDATSKVWFTMG-WKDKVFGGFTNSGslNGDKQVTLISMQTLASQHGGIWVSLGLppanklestrqdi 138
Cdd:COG0655    81 YFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG--HGGAEATLLSLNTFLLHHGMIVVGLPP------------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1036094196 139 nnLGGSVGVLVQSPTDADEtaipsgdLETARLYGERVAKIAKRLK 183
Cdd:COG0655   146 --YGAVGGGGPGDVLDEEG-------LATARELGKRLAELAKKLK 181
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-183 3.50e-24

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 93.83  E-value: 3.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAQLIA----------------------IDENGDIKDTDwdALNNADAIIFGAP 58
Cdd:PRK03767    1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAevtikrvpetvpeevakkaggkTDQAAPVATPD--ELADYDAIIFGTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  59 TYMGSYPWQFKKFVDATSKVWFTMGWKDKVFGGFTNSGSLNGDKQVTLISMQTLASQHGGIWVslGLPPANKLESTRQDI 138
Cdd:PRK03767   79 TRFGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQHGGQETTITSTHTTLLHHGMVIV--GLPYAFQGQMDVDEV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036094196 139 NnlGGsvgvlvqSP------TDADETAIPSG-DLETARLYGERVAKIAKRLK 183
Cdd:PRK03767  157 T--GG-------SPygattiAGGDGSRQPSEnELAGARYQGRHVAEIAAKLA 199
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 3-182 1.45e-23

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: 92.27  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFSGYGHTKKVAEFVA------DGANAQLIAIDE-------NGDIKDTDWDA-------LNNADAIIFGAPTYMG 62
Cdd:TIGR01755   2 KVLVLYYSMYGHIETMARAVAegarevDGAEVVVKRVPEtvpeevaEKSHGKTDQTApvatpqeLADYDAIIFGTPTRFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  63 SYPWQFKKFVDATSKVWFTMGWKDKVFGGFTNSGSLNGDKQVTLISMQTLASQHGGIWVslGLPPANKlESTRQDINNLG 142
Cdd:TIGR01755  82 NMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQHGGQESTILSTWTTLLHHGMIIV--PLPYAAQ-EQMGVDEVRGG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1036094196 143 GSVGvlVQSPTDADETAIPSG-DLETARLYGERVAKIAKRL 182
Cdd:TIGR01755 159 SPYG--ATTIAGGDGSRQPSAeELDIARYQGRHVAGLAAKL 197
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-124 8.84e-12

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 59.94  E-value: 8.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFS--GYGHTKKVAEFVAD----GANAQLIAI-DENGDIKDTDW--------------DALNNADAIIFGAPTYM 61
Cdd:pfam03358   2 KILAISGSprKGSNTRKLARWAAElleeGAEVELIDLaDLILPLCDEDLeeeqgdpddvqelrEKIAAADAIIIVTPEYN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036094196  62 GSYPWQFKKFVDATSKVWFTMGWKDKVFGGFTNSGSLNGDKQVTLISMQTLASQH----GGIWVSLG 124
Cdd:pfam03358  82 GSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGaivvPSGQVAVG 148
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 6-60 5.73e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 45.24  E-value: 5.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1036094196   6 VIYFSGYGHTKKVAEFVADGANAQLIAIDENgdIKDTDwDALNNADAIIFGAPTY 60
Cdd:NF038196    1 IFYFSGTGNSLYVAKRIAEELGDELISISKA--IKEGD-FKLKEDEPIGFVFPVY 52
 
Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-183 1.32e-34

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 120.03  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFS--GYGHTKKVAEFVADGA-----NAQLIAIDE-----------NGDIKDTD-----WDALNNADAIIFGAPT 59
Cdd:COG0655     1 KILVINGSprKNGNTAALAEAVAEGAeeagaEVELIRLADldikpcigcggTGKCVIKDdmnaiYEKLLEADGIIFGSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  60 YMGSYPWQFKKFVDATSKVWFTMG-WKDKVFGGFTNSGslNGDKQVTLISMQTLASQHGGIWVSLGLppanklestrqdi 138
Cdd:COG0655    81 YFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG--HGGAEATLLSLNTFLLHHGMIVVGLPP------------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1036094196 139 nnLGGSVGVLVQSPTDADEtaipsgdLETARLYGERVAKIAKRLK 183
Cdd:COG0655   146 --YGAVGGGGPGDVLDEEG-------LATARELGKRLAELAKKLK 181
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-183 3.50e-24

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 93.83  E-value: 3.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAQLIA----------------------IDENGDIKDTDwdALNNADAIIFGAP 58
Cdd:PRK03767    1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAevtikrvpetvpeevakkaggkTDQAAPVATPD--ELADYDAIIFGTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  59 TYMGSYPWQFKKFVDATSKVWFTMGWKDKVFGGFTNSGSLNGDKQVTLISMQTLASQHGGIWVslGLPPANKLESTRQDI 138
Cdd:PRK03767   79 TRFGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQHGGQETTITSTHTTLLHHGMVIV--GLPYAFQGQMDVDEV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036094196 139 NnlGGsvgvlvqSP------TDADETAIPSG-DLETARLYGERVAKIAKRLK 183
Cdd:PRK03767  157 T--GG-------SPygattiAGGDGSRQPSEnELAGARYQGRHVAEIAAKLA 199
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 3-182 1.45e-23

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: 92.27  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFSGYGHTKKVAEFVA------DGANAQLIAIDE-------NGDIKDTDWDA-------LNNADAIIFGAPTYMG 62
Cdd:TIGR01755   2 KVLVLYYSMYGHIETMARAVAegarevDGAEVVVKRVPEtvpeevaEKSHGKTDQTApvatpqeLADYDAIIFGTPTRFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196  63 SYPWQFKKFVDATSKVWFTMGWKDKVFGGFTNSGSLNGDKQVTLISMQTLASQHGGIWVslGLPPANKlESTRQDINNLG 142
Cdd:TIGR01755  82 NMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQHGGQESTILSTWTTLLHHGMIIV--PLPYAAQ-EQMGVDEVRGG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1036094196 143 GSVGvlVQSPTDADETAIPSG-DLETARLYGERVAKIAKRL 182
Cdd:TIGR01755 159 SPYG--ATTIAGGDGSRQPSAeELDIARYQGRHVAGLAAKL 197
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 4-74 8.54e-15

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 67.62  E-value: 8.54e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036094196   4 VAVIYFSGYGHTKKVAEFVADGANAQLIAIDengDIKDTDWDALNNADAIIFGAPTYMGSYPWQFKKFVDA 74
Cdd:COG0716     1 ILIVYGSTTGNTEKVAEAIAEALGAAGVDLF---EIEDADLDDLEDYDLLILGTPTWAGELPDDWEDFLEE 68
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 3-80 8.58e-12

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


Pssm-ID: 443673  Cd Length: 179  Bit Score: 60.68  E-value: 8.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFSGYGHTKKVAEFVAD-----GANAQLIAIDENGDIkdtdwdALNNADAIIFGAPTYMGSYPWQFKKFVD---- 73
Cdd:COG4635     2 KVLILYASRDGQTRKIAERIAEvlreaGHDVDLVDLEDAPDL------DLAGYDAVVIGASIRYGKWLPEAVRFVRrhrd 75


                  ....*....
gi 1036094196  74 --ATSKVWF 80
Cdd:COG4635    76 alAARPVAF 84
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-124 8.84e-12

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 59.94  E-value: 8.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFS--GYGHTKKVAEFVAD----GANAQLIAI-DENGDIKDTDW--------------DALNNADAIIFGAPTYM 61
Cdd:pfam03358   2 KILAISGSprKGSNTRKLARWAAElleeGAEVELIDLaDLILPLCDEDLeeeqgdpddvqelrEKIAAADAIIIVTPEYN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036094196  62 GSYPWQFKKFVDATSKVWFTMGWKDKVFGGFTNSGSLNGDKQVTLISMQTLASQH----GGIWVSLG 124
Cdd:pfam03358  82 GSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGaivvPSGQVAVG 148
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 6-72 4.39e-11

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: 58.04  E-value: 4.39e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036094196   6 VIYFSGYGHTKKVAEFVAD--GANAQLIAIDENGDIKDtdwdaLNNADAIIFGAPTYMGSYPWQFKKFV 72
Cdd:pfam12724   2 ILYSSRDGQTKKIAERIAEelREEGELVDVEDVEAGED-----LSSYDAVVIGASIYYGKHLPELRQFV 65
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-96 7.54e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 47.90  E-value: 7.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFSGYGHTKKVAEFVADGANAQLIAIdENGDIKDTDW----DALNNADAIIFGAPTYMGSYpwqFKKFVDATSKV 78
Cdd:COG0426   248 KVVIVYASMYGNTEKMAEAIAEGLTEEGVKV-KLYDLEKTDPseiiTEIFDAKGIVIGSPTYNGGA---FPPIADLLGYL 323

                          90
                  ....*....|....*...
gi 1036094196  79 wFTMGWKDKVFGGFTNSG 96
Cdd:COG0426   324 -KGLAPKNKLAGAFGSYG 340
PRK05568 PRK05568
flavodoxin; Provisional
 1-62 1.48e-06

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 45.57  E-value: 1.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAqliaidENGDIK-----DTDWDALNNADAIIFGAPTyMG 62
Cdd:PRK05568    1 MKKINIIYWSGTGNTEAMANLIAEGAKE------NGAEVKllnvsEASVDDVKGADVVALGSPA-MG 60
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 45-108 1.54e-06

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: 46.17  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036094196  45 DALNNADAIIFGAPTYMGSYPWQFKKFVDatskVWFTMGWKDKVFGGFTNSGSLNGdKQVTLIS 108
Cdd:pfam02525  69 EELLAADVIVFQFPLYWFSVPALLKGWID----RVLRAGFAFKYEEGGPGGGGLLG-KKVLVIV 127
PRK09267 PRK09267
flavodoxin FldA; Validated
 1-60 4.91e-06

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 44.44  E-value: 4.91e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVAD---GANAQLIaidengDIKDTDWDALNNADAIIFGAPTY 60
Cdd:PRK09267    1 MAKIGIFFGSDTGNTEDIAKMIQKklgKDVADVV------DIAKASKEDFEAYDLLILGIPTW 57
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 6-60 5.73e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 45.24  E-value: 5.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1036094196   6 VIYFSGYGHTKKVAEFVADGANAQLIAIDENgdIKDTDwDALNNADAIIFGAPTY 60
Cdd:NF038196    1 IFYFSGTGNSLYVAKRIAEELGDELISISKA--IKEGD-FKLKEDEPIGFVFPVY 52
PRK06242 PRK06242
flavodoxin; Provisional
 3-78 3.28e-05

flavodoxin; Provisional


Pssm-ID: 180484 [Multi-domain]  Cd Length: 150  Bit Score: 41.82  E-value: 3.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036094196   3 KVAVIYFS-GYGHTKKVAEFVADGANAQLIaidengDIKDTDWDALNNADAIIFGAPTYMGSYPWQFKKFVDATSKV 78
Cdd:PRK06242    2 KALIVYASvHHGNTEKIAKAIAEVLDAEVI------DPGDVNPEDLSEYDLIGFGSGIYFGKFHKSLLKLIEKLPPV 72
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 4-60 5.16e-05

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: 41.17  E-value: 5.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036094196   4 VAVIYFSGYGHTKKVAEFVADGANAQLIAIDENgDIKDTDWDALNNADAIIFGAPTY 60
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLL-EVADADAEDLLSYDAVLLGCSTW 56
Flavodoxin_1 pfam00258
Flavodoxin;
6-73 1.51e-04

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 40.05  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036094196   6 VIYFSGYGHTKKVAEFVADGANAQLIAIDENgDIKDTD--WDALNNADAIIFGAPTYM-GSYPWQFKKFVD 73
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVV-DLDDVDetLSEIEEEDLLLVVVSTWGeGEPPDNAKPFVD 70
PRK07116 PRK07116
flavodoxin; Provisional
 1-33 8.57e-04

flavodoxin; Provisional


Pssm-ID: 180850  Cd Length: 160  Bit Score: 38.12  E-value: 8.57e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAQLIAI 33
Cdd:PRK07116    2 NNKTLVAYFSATGTTKKVAEKLAEVTGADLFEI 34
PRK06756 PRK06756
flavodoxin; Provisional
 1-90 1.05e-03

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 37.94  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAQLIAIDENGDIKDTDWDALNNADAIIFGAPTYM-GSYPWQFKKFVDATSKVW 79
Cdd:PRK06756    1 MSKLVMIFASMSGNTEEMADHIAGVIRETENEIEVIDIMDSPEASILEQYDGIILGAYTWGdGDLPDDFLDFYDAMDSID 80

                          90
                  ....*....|.
gi 1036094196  80 FTmGWKDKVFG 90
Cdd:PRK06756   81 LT-GKKAAVFG 90
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
3-100 2.88e-03

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 36.67  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   3 KVAVIYFS--GYGHTKKVAEFVAD-----GANAQLIAIDE------NGDIKDTDW--------DALNNADAIIFGAPTYM 61
Cdd:COG0431     2 KILVISGSlrPGSFNRKLARAAAElapaaGAEVELIDLRDldlplyDEDLEADGAppavkalrEAIAAADGVVIVTPEYN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1036094196  62 GSYPWQFKKFVDATSKVwftmGWKDKVFGGFTNSGSLNG 100
Cdd:COG0431    82 GSYPGVLKNALDWLSRS----ELAGKPVALVSTSGGARG 116
PRK06703 PRK06703
flavodoxin; Provisional
 1-90 4.03e-03

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 36.28  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAQLIAIDENgDIKDTDWDALNNADAIIFGAPTYM-GSYPWQFKKFVDATSKVW 79
Cdd:PRK06703    1 MAKILIAYASMSGNTEDIADLIKVSLDAFDHEVVLQ-EMDGMDAEELLAYDGIILGSYTWGdGDLPYEAEDFHEDLENID 79

                          90
                  ....*....|.
gi 1036094196  80 FTmGWKDKVFG 90
Cdd:PRK06703   80 LS-GKKVAVFG 89
PRK05569 PRK05569
flavodoxin; Provisional
 1-89 4.57e-03

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 35.97  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036094196   1 MSKVAVIYFSGYGHTKKVAEFVADGANAQLIAIdengDIKDTDWDALNN---ADAIIFGAP---------TYMGSYPWQF 68
Cdd:PRK05569    1 MKKVSIIYWSCGGNVEVLANTIADGAKEAGAEV----TIKHVADAKVEDvleADAVAFGSPsmdnnnieqEEMAPFLDQF 76

                          90       100
                  ....*....|....*....|...
gi 1036094196  69 KKFVDATSKV--WFTMGWKDKVF 89
Cdd:PRK05569   77 KLTPNENKKCilFGSYGWDNGEF 99
 
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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