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Conserved domains on  [gi|15832351|ref|NP_311124|]
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ferredoxin-type protein [Escherichia coli O157:H7 str. Sakai]

Protein Classification

similar to ferredoxin-type protein NapF( domain architecture ID 11484607)

protein similar to ferredoxin-type protein NapF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10194 PRK10194
ferredoxin-type protein NapF;
2-164 4.94e-111

ferredoxin-type protein NapF;


:

Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 312.34  E-value: 4.94e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351    2 KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 81
Cdd:PRK10194   1 KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351   82 SLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYL 161
Cdd:PRK10194  81 SLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYL 160


                 ...
gi 15832351  162 HAH 164
Cdd:PRK10194 161 HAH 163
 
Name Accession Description Interval E-value
PRK10194 PRK10194
ferredoxin-type protein NapF;
2-164 4.94e-111

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 312.34  E-value: 4.94e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351    2 KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 81
Cdd:PRK10194   1 KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351   82 SLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYL 161
Cdd:PRK10194  81 SLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYL 160


                 ...
gi 15832351  162 HAH 164
Cdd:PRK10194 161 HAH 163
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 23-157 3.77e-68

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 203.24  E-value: 3.77e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  23 RPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPESLFSPRHTRAWDLQFTIGDAC 102
Cdd:cd10564   1 RPPWAVDEALFLDLCTRCGDCVEACPEGIIVRGDGGFPELDFSRGECTFCGACAEACPEGALDPAREAPWPLRAEIGDSC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832351 103 LAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:cd10564  81 LALQGVECRSCQDACPTQAIRFRPRLGGIALPELDADACTGCGACVSVCPVGAIT 135
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 7-102 3.12e-50

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 156.65  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351     7 RRGILTGRWRKASNG-----IRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 81
Cdd:TIGR00402   1 RRGLLRGVFPATSSTiektqIRPPWSARESLFSAVCTRCGECASACENNILQLGQQGQPTVEFDNAECDFCGKCAEACPT 80

                          90       100
                  ....*....|....*....|.
gi 15832351    82 SLFSPRHTRAWDLQFTIGDAC 102
Cdd:TIGR00402  81 NAFHPRFPGDWLLRPQISSAC 101
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 108-157 5.96e-08

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.42  E-value: 5.96e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15832351 108 VECRRCQDSCEPMAIifrpTLSGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1149  14 IGCGLCVEVCPEGAI----KLDDGGAPVVDPDLCTGCGACVGVCPTGAIT 59
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 37-80 6.93e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 35.97  E-value: 6.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15832351    37 CTRCDACINACENNILQR----GAGGYPSVNFKNNECSFCYACAQACP 80
Cdd:pfam12838   1 CIGCGACVAACPVGAITLdevgEKKGTKTVVIDPERCVGCGACVAVCP 48
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 36-80 2.70e-03

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: 36.76  E-value: 2.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 15832351   36 HCTRCDACINAC-ENNIlqRGAGGYPSvnFKNNeCSFCYACAQACP 80
Cdd:NF038196 186 KCIGCGICAKVCpVNNI--EMEDGKPV--WGHN-CTHCLACIHRCP 226
 
Name Accession Description Interval E-value
PRK10194 PRK10194
ferredoxin-type protein NapF;
2-164 4.94e-111

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 312.34  E-value: 4.94e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351    2 KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 81
Cdd:PRK10194   1 KIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351   82 SLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYL 161
Cdd:PRK10194  81 SLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYL 160


                 ...
gi 15832351  162 HAH 164
Cdd:PRK10194 161 HAH 163
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 23-157 3.77e-68

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 203.24  E-value: 3.77e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  23 RPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPESLFSPRHTRAWDLQFTIGDAC 102
Cdd:cd10564   1 RPPWAVDEALFLDLCTRCGDCVEACPEGIIVRGDGGFPELDFSRGECTFCGACAEACPEGALDPAREAPWPLRAEIGDSC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832351 103 LAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:cd10564  81 LALQGVECRSCQDACPTQAIRFRPRLGGIALPELDADACTGCGACVSVCPVGAIT 135
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 7-102 3.12e-50

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 156.65  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351     7 RRGILTGRWRKASNG-----IRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 81
Cdd:TIGR00402   1 RRGLLRGVFPATSSTiektqIRPPWSARESLFSAVCTRCGECASACENNILQLGQQGQPTVEFDNAECDFCGKCAEACPT 80

                          90       100
                  ....*....|....*....|.
gi 15832351    82 SLFSPRHTRAWDLQFTIGDAC 102
Cdd:TIGR00402  81 NAFHPRFPGDWLLRPQISSAC 101
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 22-158 5.26e-23

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 88.85  E-value: 5.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  22 IRPPWSGDESHFLTHCTRCDACINACENNILQRG-------AGGYPSVNFKNNECSFCY-ACAQACPESLFSPRHTRAWD 93
Cdd:cd16373   1 LRPPGALDEEEFLALCIRCGLCVEACPTGVIQPAgledgleGGRTPYLDPREGPCDLCCdACVEVCPTGALRPLDLEEQK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832351  94 LQftIG------DACLAYQS-VECRRCQDSCEPMAIIFRPtLSGIYQPQLNSQLCNGCGACAASCPVSAITA 158
Cdd:cd16373  81 VK--MGvavidkDRCLAWQGgTDCGVCVEACPTEAIAIVL-EDDVLRPVVDEDKCVGCGLCEYVCPVEPPKA 149
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 37-156 1.14e-10

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 55.87  E-value: 1.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  37 CTRCDACINACENNILQRGAGGYPSVNFKNNE--CSFCYACAQACPESL--FSPRHTRA--WDLQFTIGDACLayqsVEC 110
Cdd:cd10549   8 CIGCGICVKACPTDAIELGPNGAIARGPEIDEdkCVFCGACVEVCPTGAieLTPEGKEYvpKEKEAEIDEEKC----IGC 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15832351 111 RRCQDSCEPMAIifrpTLSGIYQPQLNSQLCNGCGACAASCPVSAI 156
Cdd:cd10549  84 GLCVKVCPVDAI----TLEDELEIVIDKEKCIGCGICAEVCPVNAI 125
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 22-151 4.91e-08

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 50.78  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351   22 IRPPWSGDESHFLTHCTRCDACINACENNILQRG------AGGYPSVNFKNNECSFC--YACAQACPeslfsprhTRAWD 93
Cdd:PRK09476  46 LRPPGALNENDFLSACIRCGLCVQACPYDTLKLAtlasglSAGTPYFVARDIPCEMCedIPCVKACP--------SGALD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351   94 LQFT-IGDA------------CLAYQSVECRRCQDSCePM---AIIF---RPTLSGIYQ---PQLNSQLCNGCGACAASC 151
Cdd:PRK09476 118 RELVdIDDArmglavlvdqenCLNFQGLRCDVCYRVC-PLidkAITLeleRNERTGKHAfflPTVHSDACTGCGKCEKAC 196
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 108-157 5.96e-08

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.42  E-value: 5.96e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15832351 108 VECRRCQDSCEPMAIifrpTLSGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1149  14 IGCGLCVEVCPEGAI----KLDDGGAPVVDPDLCTGCGACVGVCPTGAIT 59
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 37-81 1.12e-06

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 43.93  E-value: 1.12e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15832351  37 CTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPE 81
Cdd:COG1146  10 CIGCGACVEVCPVDVLELDEEGKKALVINPEECIGCGACELVCPV 54
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
110-157 1.13e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.16  E-value: 1.13e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15832351 110 CRRCQDSCEPMAIifrpTLSGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1148 501 CGRCVEVCPYGAI----SIDEKGVAEVNPALCKGCGTCAAACPSGAIS 544
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 68-156 3.79e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 45.79  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351   68 ECSFCYACAQACPESlfspRHTRAWDLQFT-------IGDACLAYQSVECRRCQD-----SCEPMAIIFRPTlsgiyQPQ 135
Cdd:PRK12809  11 ECIGCHACEIACAVA----HNQENWPLSHSdfrprihVVGKGQAANPVACHHCNNapcvtACPVNALTFQSD-----SVQ 81

                         90       100
                 ....*....|....*....|.
gi 15832351  136 LNSQLCNGCGACAASCPVSAI 156
Cdd:PRK12809  82 LDEQKCIGCKRCAIACPFGVV 102
NapF COG1145
Ferredoxin [Energy production and conversion];
37-81 1.48e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 43.56  E-value: 1.48e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15832351  37 CTRCDACINACENNILQRGAGGyPSVNFKNNECSFCYACAQACPE 81
Cdd:COG1145 184 CIGCGLCVKVCPTGAIRLKDGK-PQIVVDPDKCIGCGACVKVCPV 227
NapF COG1145
Ferredoxin [Energy production and conversion];
110-157 3.98e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.40  E-value: 3.98e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15832351 110 CRRCQDSCEPMAIIFRPtlsGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1145 187 CGLCVKVCPTGAIRLKD---GKPQIVVDPDKCIGCGACVKVCPVGAIS 231
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 110-159 4.19e-05

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 40.03  E-value: 4.19e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15832351 110 CRRCQDSCEPMAIIFRPTLSGIyqpqlNSQLCNGCGACAASCPVSAITAE 159
Cdd:COG4231  27 CGACVKVCPADAIEEGDGKAVI-----DPDLCIGCGSCVQVCPVDAIKLE 71
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 37-81 9.01e-05

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 38.94  E-value: 9.01e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15832351  37 CTRCDACINACENNILQRGAGGYPSVNfkNNECSFCYACAQACPE 81
Cdd:COG1149  13 CIGCGLCVEVCPEGAIKLDDGGAPVVD--PDLCTGCGACVGVCPT 55
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 108-157 1.13e-04

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.88  E-value: 1.13e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15832351 108 VECRRCQDSCEPMAIIFRPtlsgIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1144  33 IGCGLCWIVCPDGAIRVDD----GKYYGIDYDYCKGCGICAEVCPVKAIE 78
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 100-164 1.62e-04

beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 40.45  E-value: 1.62e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832351 100 DACLayqsvECRR--CQDSCePMAIIFRPTLSGIYqpqLNSQLCNGCGACAASCP--VSAITAEYLHAH 164
Cdd:cd10560  76 DVCK-----HCTDagCLEAC-PTGAIFRTEFGTVY---IQPDICNGCGYCVAACPfgVIDRNEETGRAH 135
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
69-157 1.86e-04

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 39.26  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  69 CSFCYACAQACPESLFSPRHTRAWDLQFTIGDAcLAYQSVECRRCQD-----SCEPMAIIFRPTlsgiyQPQLNSQLCNG 143
Cdd:COG1142  12 CIGCRTCEAACAVAHEGEEGEPFLPRIRVVRKA-GVSAPVQCRHCEDapcaeVCPVGAITRDDG-----AVVVDEEKCIG 85

                        90
                ....*....|....
gi 15832351 144 CGACAASCPVSAIT 157
Cdd:COG1142  86 CGLCVLACPFGAIT 99
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 133-160 1.96e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 40.02  E-value: 1.96e-04
                         10        20
                 ....*....|....*....|....*...
gi 15832351  133 QPQLNSQLCNGCGACAASCPVSAITAEY 160
Cdd:PRK12387  32 KPEYNPQQCIGCAACVNACPSNALTVET 59
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
67-157 3.34e-04

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 40.01  E-value: 3.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  67 NECSFCYACAQACPESLFSPRHTRAWDLQFTIGDACLAYQS--VECRRCQDSCEPMAIIFRPTlsgiyQPQLNSQLCNGC 144
Cdd:COG4624  51 CPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEkcKNCYPCVRACPVKAIKVDDG-----KAEIDEEKCISC 125

                        90
                ....*....|...
gi 15832351 145 GACAASCPVSAIT 157
Cdd:COG4624 126 GQCVAVCPFGAIT 138
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 109-157 4.55e-04

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 39.29  E-value: 4.55e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15832351 109 ECRRCQDSCEPMAIIFRPTLSGIyqpqlNSQLCNGCGACAASCPVSAIT 157
Cdd:cd03110  68 RCGNCERVCKFGAILEFFQKLIV-----DESLCEGCGACVIICPRGAIY 111
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 108-159 5.77e-04

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 36.57  E-value: 5.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15832351 108 VECRRCQDSCEPMAIifrpTLSGiYQPQLNSQLCNGCGACAASCPVSAITAE 159
Cdd:COG2221  18 IGCGLCVAVCPTGAI----SLDD-GKLVIDEEKCIGCGACIRVCPTGAIKGE 64
PRK13795 PRK13795
hypothetical protein; Provisional
 37-80 6.24e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.21  E-value: 6.24e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15832351   37 CTRCDACINACENNILQRGAGGyPSVNFKNNECSFCYACAQACP 80
Cdd:PRK13795 583 CVGCGVCVGACPTGAIRIEEGK-RKISVDEEKCIHCGKCTEVCP 625
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 37-80 6.93e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 35.97  E-value: 6.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15832351    37 CTRCDACINACENNILQR----GAGGYPSVNFKNNECSFCYACAQACP 80
Cdd:pfam12838   1 CIGCGACVAACPVGAITLdevgEKKGTKTVVIDPERCVGCGACVAVCP 48
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 110-157 7.48e-04

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 36.26  E-value: 7.48e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15832351 110 CRRCQDSCePMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1143   7 CGLCVRVC-PVDAITIEDGEPGKVYVIDPDKCIGCGLCVEVCPTGAIS 53
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 130-157 8.95e-04

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 36.18  E-value: 8.95e-04
                        10        20
                ....*....|....*....|....*...
gi 15832351 130 GIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG2221   6 GTWPPKIDEEKCIGCGLCVAVCPTGAIS 33
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 32-81 1.06e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 37.94  E-value: 1.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15832351   32 HFLTHCTRCDACINACENNILQRGAGgypSVNFKNNE-CSFCYACAQACPE 81
Cdd:PRK00783 166 EVSEDCDECEKCVEACPRGVLELKEG---KLVVTDLLnCSLCKLCERACPG 213
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 66-156 1.38e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 36.87  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  66 NNECSFCYACAQACpeslfsprhTRAWDLQFTIGDACLAYQS----------VECRRCQD-----SCEPMAIIFRPTlsg 130
Cdd:cd16370   8 MERCIGCYSCMLAC---------SRRVHKSASLSKSAIRVRTrggleggftvVVCRACEDppcaeACPTGALEPRKG--- 75

                        90       100
                ....*....|....*....|....*.
gi 15832351 131 iYQPQLNSQLCNGCGACAASCPVSAI 156
Cdd:cd16370  76 -GGVVLDKEKCIGCGNCVKACIVGAI 100
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 32-157 1.48e-03

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 36.98  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832351  32 HFLTHCTRCDACINACENNILQRGAGGYPSV----------NFKNNECSFCY--ACAQACPESLFSPRHTRA--WDLQFT 97
Cdd:cd04410   3 VDLDRCIGCGTCEVACKQEHGLRPGPDWSRIkvieggglerAFLPVSCMHCEdpPCVKACPTGAIYKDEDGIvlIDEDKC 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832351  98 IGdaclayqsveCRRCQDSCePMAIIFRPTLSGIyqpqlnSQLCNGCG---------ACAASCPVSAIT 157
Cdd:cd04410  83 IG----------CGSCVEAC-PYGAIVFDPEPGK------AVKCDLCGdrldeglepACVKACPTGALT 134
Fer4_9 pfam13187
4Fe-4S dicluster domain;
37-80 1.51e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.22  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15832351    37 CTRCDACINACENNILQRGAGGYP-SVNFKNNECSFCYACAQACP 80
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPDLVGQTiRGDIAGLACIGCGACVDACP 46
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 110-159 1.88e-03

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 35.07  E-value: 1.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15832351 110 CRRCQDSCEpmAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAE 159
Cdd:COG1146  13 CGACVEVCP--VDVLELDEEGKKALVINPEECIGCGACELVCPVGAITVE 60
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
108-157 1.95e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 37.35  E-value: 1.95e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15832351 108 VECRRCQDSCePMAIIfrptlsgIYQPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG0348 213 IDCGLCVKVC-PMGID-------IRKGEINQSECINCGRCIDACPKDAIR 254
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 36-80 2.70e-03

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: 36.76  E-value: 2.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 15832351   36 HCTRCDACINAC-ENNIlqRGAGGYPSvnFKNNeCSFCYACAQACP 80
Cdd:NF038196 186 KCIGCGICAKVCpVNNI--EMEDGKPV--WGHN-CTHCLACIHRCP 226
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
37-81 6.31e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 35.99  E-value: 6.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15832351  37 CTRCDACINACENNILQRGAGGYPSVNfkNNECSFCYACAQACPE 81
Cdd:COG1148 498 CTGCGRCVEVCPYGAISIDEKGVAEVN--PALCKGCGTCAAACPS 540
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 108-155 7.19e-03

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 33.27  E-value: 7.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15832351   108 VECRRCQDSCEPMAIIFRPTL--SGIYQPQLNSQLCNGCGACAASCPVSA 155
Cdd:pfam12838   2 IGCGACVAACPVGAITLDEVGekKGTKTVVIDPERCVGCGACVAVCPTGA 51
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
108-159 7.51e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 33.55  E-value: 7.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15832351 108 VECRRCQDSCEPMAIIFRptlSGIYQpqLNSQLCNGCGACAASCPVSAITAE 159
Cdd:COG2768  14 IGCGACVKVCPVGAISIE---DGKAV--IDPEKCIGCGACIEVCPVGAIKIE 60
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
127-157 7.68e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 35.99  E-value: 7.68e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 15832351 127 TLSGIYqPQLNSQLCNGCGACAASCPVSAIT 157
Cdd:COG1148 485 GVEPSV-AEVDPEKCTGCGRCVEVCPYGAIS 514
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 37-81 7.94e-03

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 33.87  E-value: 7.94e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15832351  37 CTRCDACINACENNILQRGAGGYPSVNFknNECSFCYACAQACPE 81
Cdd:COG1144  32 CIGCGLCWIVCPDGAIRVDDGKYYGIDY--DYCKGCGICAEVCPV 74
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 130-159 9.21e-03

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 33.16  E-value: 9.21e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 15832351 130 GIYQPQLNSQLCNGCGACAASCPVSAITAE 159
Cdd:COG1149   2 KRKIPVIDEEKCIGCGLCVEVCPEGAIKLD 31
 
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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