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Conserved domains on  [gi|491457394|ref|WP_005315173|]
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4Fe-4S dicluster domain-containing protein [Aeromonas salmonicida]

Protein Classification

4Fe-4S dicluster domain-containing protein( domain architecture ID 11586809)

4Fe-4S dicluster domain-containing protein similar to Escherichia coli formate hydrogenlyase subunit 2 (HycB), a probable electron transfer protein for hydrogenase 3

Gene Ontology:  GO:0051539|GO:0009061|GO:0046872|GO:0019645
SCOP:  3000020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-175 2.14e-55

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


:

Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 173.98  E-value: 2.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   4 FVIADPKLCIGCGTCMAACSTVH--------KAQGLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCV 75
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHsgkgifeaGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  76 QLNESLCIGCNLCAVACPFGAIQsggsrpvaMANSYdtyipcsirssnpstsaglrcfgEDLLSWEPGVRSIAVKCDLCE 155
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIE--------MAPTT-----------------------VPGVDWERGPRAVAVKCDLCA 129

                        170       180
                 ....*....|....*....|
gi 491457394 156 FRAEGPACVSACPSQSLSIV 175
Cdd:cd10554  130 GREGGPACVEACPTKALTLV 149
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-175 2.14e-55

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 173.98  E-value: 2.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   4 FVIADPKLCIGCGTCMAACSTVH--------KAQGLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCV 75
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHsgkgifeaGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  76 QLNESLCIGCNLCAVACPFGAIQsggsrpvaMANSYdtyipcsirssnpstsaglrcfgEDLLSWEPGVRSIAVKCDLCE 155
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIE--------MAPTT-----------------------VPGVDWERGPRAVAVKCDLCA 129

                        170       180
                 ....*....|....*....|
gi 491457394 156 FRAEGPACVSACPSQSLSIV 175
Cdd:cd10554  130 GREGGPACVEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-175 1.25e-50

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 161.36  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTVHKA-QGLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCVQLNE 79
Cdd:COG1142    1 MNKFIIADPEKCIGCRTCEAACAVAHEGeEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAVVVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  80 SLCIGCNLCAVACPFGAIQSGGSRPvamansydtyipcsirssnpstsaglrcfgedllswepgvRSIAVKCDLCEFRAE 159
Cdd:COG1142   81 EKCIGCGLCVLACPFGAITMVGEKS----------------------------------------RAVAVKCDLCGGREG 120

                        170
                 ....*....|....*.
gi 491457394 160 GPACVSACPSQSLSIV 175
Cdd:COG1142  121 GPACVEACPTGALRLV 136
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-200 4.75e-42

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 150.67  E-value: 4.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTVH-------KAQGLQqaPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGD 73
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACVMAHndeqhvlSQHHFH--PRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  74 CVQLNESLCIGCNLCAVACPFGAIQSgGSRPVAMANsydtyipcsirssnpstsaglrcfgedllswepgVRSIAVKCDL 153
Cdd:PRK12769  79 SIQVNQQKCIGCKSCVVACPFGTMQI-VLTPVAAGK----------------------------------VKATAHKCDL 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491457394 154 CEFRAEGPACVSACPSQSLSIVNDTACANAARDRRLQAANAHPQGAP 200
Cdd:PRK12769 124 CAGRENGPACVENCPADALQLVTEQALSGMAKSRRLRTARQEHQPWH 170
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 50-100 2.18e-07

archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 49.87  E-value: 2.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491457394   50 QCRHCDDapCIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAIQSG 100
Cdd:TIGR02700 149 RCKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAIHGG 197
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 48-96 7.57e-07

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 46.09  E-value: 7.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491457394   48 PVQCRHCDDAPCIKVCPVEAIAQTGD--CVQLNESLCIGCNLCAVACPFGA 96
Cdd:pfam13247   7 PEQCRHCLNPPCKASCPVGAIYKDEEtgAVLLDEKTCRGWRECVSACPYNI 57
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-175 2.14e-55

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 173.98  E-value: 2.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   4 FVIADPKLCIGCGTCMAACSTVH--------KAQGLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCV 75
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHsgkgifeaGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  76 QLNESLCIGCNLCAVACPFGAIQsggsrpvaMANSYdtyipcsirssnpstsaglrcfgEDLLSWEPGVRSIAVKCDLCE 155
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIE--------MAPTT-----------------------VPGVDWERGPRAVAVKCDLCA 129

                        170       180
                 ....*....|....*....|
gi 491457394 156 FRAEGPACVSACPSQSLSIV 175
Cdd:cd10554  130 GREGGPACVEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-175 1.25e-50

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 161.36  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTVHKA-QGLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCVQLNE 79
Cdd:COG1142    1 MNKFIIADPEKCIGCRTCEAACAVAHEGeEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAVVVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  80 SLCIGCNLCAVACPFGAIQSGGSRPvamansydtyipcsirssnpstsaglrcfgedllswepgvRSIAVKCDLCEFRAE 159
Cdd:COG1142   81 EKCIGCGLCVLACPFGAITMVGEKS----------------------------------------RAVAVKCDLCGGREG 120

                        170
                 ....*....|....*.
gi 491457394 160 GPACVSACPSQSLSIV 175
Cdd:COG1142  121 GPACVEACPTGALRLV 136
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-200 4.75e-42

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 150.67  E-value: 4.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTVH-------KAQGLQqaPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGD 73
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACVMAHndeqhvlSQHHFH--PRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  74 CVQLNESLCIGCNLCAVACPFGAIQSgGSRPVAMANsydtyipcsirssnpstsaglrcfgedllswepgVRSIAVKCDL 153
Cdd:PRK12769  79 SIQVNQQKCIGCKSCVVACPFGTMQI-VLTPVAAGK----------------------------------VKATAHKCDL 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491457394 154 CEFRAEGPACVSACPSQSLSIVNDTACANAARDRRLQAANAHPQGAP 200
Cdd:PRK12769 124 CAGRENGPACVENCPADALQLVTEQALSGMAKSRRLRTARQEHQPWH 170
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-196 6.36e-35

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 130.92  E-value: 6.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTVHKAQGLQQA-----PRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCV 75
Cdd:PRK12809   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLShsdfrPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  76 QLNESLCIGCNLCAVACPFGAIQSggsrpvamansydtyipcsirssnpstsaglrcfgedllswepgVRSIAVKCDLCE 155
Cdd:PRK12809  81 QLDEQKCIGCKRCAIACPFGVVEM--------------------------------------------VDTIAQKCDLCN 116

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491457394 156 FRAEGP-ACVSACPSQSLSIVNDTACANAARDRRLQAANAHP 196
Cdd:PRK12809 117 QRSSGTqACIEVCPTQALRLMDDKGLQQIKVARQRKTAAGKA 158
PRK10330 PRK10330
electron transport protein HydN;
1-192 3.78e-30

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 110.36  E-value: 3.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTVHKAQ----GLQQA---PRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGD 73
Cdd:PRK10330   1 MNRFIIADASKCIGCRTCEVACVVSHQENqdcaSLTPEtflPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  74 CVQLNESLCIGCNLCAVACPFGAIQSgGSRPVamansydtyipcsIRSSnpstSAGLRCFGEdllswepgvRSIAVKCDL 153
Cdd:PRK10330  81 FVHVMQERCIGCKTCVVACPYGAMEV-VVRPV-------------IRNS----GAGLNVRAE---------KAEANKCDL 133

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491457394 154 CEFRAEGPACVSACPSQSLSIVNDTACANAARDRRLQAA 192
Cdd:PRK10330 134 CNHREDGPACMAACPTHALICVDRNKLEQLSAEKRRRAA 172
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-172 8.10e-29

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 106.95  E-value: 8.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIaDPKLCIGCGTCMAACSTVHkaqGLQQAPRLTVMRH---------EQATMPVQCRHCDDAPCIKVCPVEAIAQT 71
Cdd:COG0437    5 RYGMVI-DLTKCIGCRACVVACKEEN---NLPVGVTWRRVRRyeegefpnvEWLFVPVLCNHCDDPPCVKVCPTGATYKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  72 GD-CVQLNESLCIGCNLCAVACPFGAIQsggsrpvamansydtyipcsirssnpstsaglrcfgedlLSWEPGVrsiAVK 150
Cdd:COG0437   81 EDgIVLVDYDKCIGCRYCVAACPYGAPR---------------------------------------FNPETGV---VEK 118

                        170       180
                 ....*....|....*....|....*
gi 491457394 151 CDLCEFR---AEGPACVSACPSQSL 172
Cdd:COG0437  119 CTFCADRldeGLLPACVEACPTGAL 143
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 8-175 5.38e-27

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: 100.54  E-value: 5.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTVHKAQGLQQAPRL---TVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGD-CVQLNESLCI 83
Cdd:cd04410    4 DLDRCIGCGTCEVACKQEHGLRPGPDWSRIkviEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDgIVLIDEDKCI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  84 GCNLCAVACPFGAIQsggsrpvamansydtyipcsirssnpstsaglrcfgedlLSWEPGVrsiAVKCDLCEFRAE---G 160
Cdd:cd04410   84 GCGSCVEACPYGAIV---------------------------------------FDPEPGK---AVKCDLCGDRLDeglE 121

                        170
                 ....*....|....*
gi 491457394 161 PACVSACPSQSLSIV 175
Cdd:cd04410  122 PACVKACPTGALTFG 136
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-175 6.13e-27

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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 100.34  E-value: 6.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   5 VIADPKLCIGCGTCMAACSTVHKAQGLQQAPRLTVMRHEQA--TMPVQCRHCDDAPCIKVCPVEAI---AQTGdCVQLNE 79
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKHEGVFNPSLSRIRVVRFEPEglDVPVVCRQCEDAPCVEACPVGAIsrdEETG-AVVVDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  80 SLCIGCNLCAVACPFGAIqsggsrpvamansydTYIPcsirssnpstsaglrcfgedllswepgVRSIAVKCDLCEfraE 159
Cdd:cd10550   80 DKCIGCGMCVEACPFGAI---------------RVDP---------------------------ETGKAIKCDLCG---G 114

                        170
                 ....*....|....*.
gi 491457394 160 GPACVSACPSQSLSIV 175
Cdd:cd10550  115 DPACVKVCPTGALEFV 130
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-172 9.71e-27

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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 100.04  E-value: 9.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   5 VIADPKLCIGCGTCMAACSTVHKAQglqqaPRLTVMRHEQ-ATMPVQCRHCDDAPCIKVCPVEAIAQTGD-CVQLNESLC 82
Cdd:cd16374    1 VYVDPERCIGCRACEIACAREHSGK-----PRISVEVVEDlASVPVRCRHCEDAPCMEVCPTGAIYRDEDgAVLVDPDKC 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  83 IGCNLCAVACPFGAIqsggsrpvamanSYDTYipcsirssnpstsaglrcfgedllswepgvRSIAVKCDLC-EFRAEG- 160
Cdd:cd16374   76 IGCGMCAMACPFGVP------------RFDPS------------------------------LKVAVKCDLCiDRRREGk 113

                        170
                 ....*....|...
gi 491457394 161 -PACVSACPSQSL 172
Cdd:cd16374  114 lPACVEACPTGAL 126
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 4-170 1.23e-26

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 101.07  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   4 FVIaDPKLCIGCGTCMAACSTVHKAQGLQQapRLTVMRHEQAT--------MPVQCRHCDDAPCIKVCPVEAIAQTGD-C 74
Cdd:cd10551    1 MVI-DLRKCIGCGACVVACKAENNVPPGVF--RNRVLEYEVGEypnvkrtfLPVLCNHCENPPCVKVCPTGATYKREDgI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  75 VQLNESLCIGCNLCAVACPFGAiqsggsrpvamansydtyipcsiRSSNPstsaglrcfGEDLLSWEPGVRS--IAVKCD 152
Cdd:cd10551   78 VLVDYDKCIGCRYCMAACPYGA-----------------------RYFNP---------EEPHEFGEVPVRPkgVVEKCT 125

                        170       180
                 ....*....|....*....|.
gi 491457394 153 LC-EFRAEG--PACVSACPSQ 170
Cdd:cd10551  126 FCyHRLDEGllPACVEACPTG 146
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 5-175 2.39e-25

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 96.56  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   5 VIADPKLCIGCGTCMAACSTVH---------KAQGLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVEAI---AQTG 72
Cdd:cd10563    2 IFIDEEKCLGCKLCEVACAVAHskskdlikaKLEKERPRPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAMhkdPETG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  73 dCVQLNESLCIGCNLCAVACPFGAIQSGGSRPVAMansydtyipcsirssnpstsaglrcfgedllswepgvrsiavKCD 152
Cdd:cd10563   82 -IVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVAL------------------------------------------KCD 118

                        170       180
                 ....*....|....*....|...
gi 491457394 153 LCEFRaEGPACVSACPSQSLSIV 175
Cdd:cd10563  119 LCPDR-ETPACVEACPTGALVLE 140
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-174 1.76e-24

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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 94.17  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTVHKAQGLQQAPRLTVMRHE------QATMPVQCRHCDDAPCIKVCPVEAIAQTGD-CVQLNES 80
Cdd:cd16371    5 DQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGefpevfAYFLSMSCNHCENPACVKVCPTGAITKREDgIVVVDQD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  81 LCIGCNLCAVACPFGAIQsggsrpvamansydtyipcsirssnpstsaglrcFGEDllswepgvRSIAVKCDLC-EFRAE 159
Cdd:cd16371   85 KCIGCGYCVWACPYGAPQ----------------------------------YNPE--------TGKMDKCDMCvDRLDE 122

                        170
                 ....*....|....*..
gi 491457394 160 G--PACVSACPSQSLSI 174
Cdd:cd16371  123 GekPACVAACPTRALDF 139
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-172 2.30e-18

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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 78.97  E-value: 2.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTVHKAQGLQQAPRLTVMRHEQ-ATMPVQCRHCDDAPCIKVCPVEAIAQTGDCVQL--NESLCIG 84
Cdd:cd16369    7 DPSRCIGCRACVAACRECGTHRGKSMIHVDYIDRGEStQTAPTVCMHCEDPTCAEVCPADAIKVTEDGVVQsaLKPRCIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  85 CNLCAVACPFGaiqsggsrpvamansydtyIPCSIRSSNpstsaglrcfgedllswepgvrsIAVKCDLCEFR-AEG--P 161
Cdd:cd16369   87 CSNCVNACPFG-------------------VPKYDEERN-----------------------LMMKCDMCYDRtSVGkaP 124

                        170
                 ....*....|.
gi 491457394 162 ACVSACPSQSL 172
Cdd:cd16369  125 MCASVCPSGAL 135
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 8-172 4.20e-18

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 79.18  E-value: 4.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTVHK--------AQGLQQAPRLT------VMRHE-------QATMPVQCRHCDDAPCIKVCPVE 66
Cdd:cd10561    5 DTTRCIGCRACEVACKEWNGlpaedtafGPGWDNPRDLSaktytvIKRYEvetggkgFVFVKRQCMHCLDPACVSACPVG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  67 AIAQTGD-CVQLNESLCIGCNLCAVACPFGAIQSggsrpvamanSYDtyipcsirssnpstsaglrcfgedllSWEPGVR 145
Cdd:cd10561   85 ALRKTPEgPVTYDEDKCIGCRYCMVACPFNIPKY----------EWD--------------------------SANPKIR 128

                        170       180       190
                 ....*....|....*....|....*....|
gi 491457394 146 siavKCDLCEFR-AEG--PACVSACPSQSL 172
Cdd:cd10561  129 ----KCTMCYDRlKEGkqPACVEACPTGAL 154
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 2-176 1.54e-17

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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 76.19  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   2 NRFVIADPKLCIGCGTCMAACSTVHKAQglqqaPRL--TVMRHEQATMPVQCRHCDDAPCIKVCPVEAIAQTGDCVQLNE 79
Cdd:cd16367   11 TNLLVIDLDRCIRCDNCEKACADTHDGH-----SRLdrNGLRFGNLLVPTACRHCVDPVCMIGCPTGAIHRDDGGEVVIS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  80 SLCIGCNLCAVACPFGAIQSggsrpvamansydtyipcsirssnpstsaglrcfgedllswepgvrSIAVKCDLCEFRAe 159
Cdd:cd16367   86 DACCGCGNCASACPYGAIQM----------------------------------------------VRAVKCDLCAGYA- 118

                        170
                 ....*....|....*..
gi 491457394 160 GPACVSACPSQSLSIVN 176
Cdd:cd16367  119 GPACVSACPTGAAIRVN 135
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 8-172 1.34e-15

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 71.57  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAAC-------STVHKAQGLQQAPR------LTVMR---HEQATMPV-------QCRHCDDAPCIKVCP 64
Cdd:cd10562    4 DTSKCTACRGCQVACkqwnqlpAEKTPFTGSYQNPPdltpntWTLIRfyeHEEDNGGIrwlfrkrQCMHCTDAACVKVCP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  65 VEAIAQTGD-CVQLNESLCIGCNLCAVACPFGAIQsggsrpvamansYDTYIPcsirssnpstsaglrcfgedllswepg 143
Cdd:cd10562   84 TGALYKTENgAVVVDEDKCIGCGYCVAACPFDVPR------------YDETTN--------------------------- 124

                        170       180       190
                 ....*....|....*....|....*....|..
gi 491457394 144 vrsIAVKCDLCEFRAEG---PACVSACPSQSL 172
Cdd:cd10562  125 ---KITKCTLCFDRIENgmqPACVKTCPTGAL 153
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 12-172 3.19e-15

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 70.51  E-value: 3.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  12 CIGCGTCMAACS--------TVHKAQGLQQAPRLTVMR------HEQAT---------MPVQCRHCDDAPCIKVCPVEAI 68
Cdd:cd16366    8 CTGCRACQVACKqwnglpaeKTEFTGSYQNPPDLTAHTwtlvrfYEVEKpggdlswlfRKDQCMHCTDAGCLAACPTGAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  69 AQT-GDCVQLNESLCIGCNLCAVACPFGAIQsggsrpvamansydtyipcsirssnpstsaglrcfgedlLSWEPGVrsi 147
Cdd:cd16366   88 IRTeTGTVVVDPETCIGCGYCVNACPFDIPR---------------------------------------FDEETGR--- 125

                        170       180
                 ....*....|....*....|....*...
gi 491457394 148 AVKCDLCEFRAEG---PACVSACPSQSL 172
Cdd:cd16366  126 VAKCTLCYDRISNglqPACVKTCPTGAL 153
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 8-173 2.92e-14

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 68.95  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACS-------TVHKAQGLQQAPR------LTVMRHEQATMP---------VQCRHCDDAPCIKVCPV 65
Cdd:cd10558    5 DVSKCIGCKACQVACKewndlraEVGHNVGTYQNPAdlspetWTLMKFREVEDNgklewlirkDGCMHCADPGCLKACPS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  66 E-AIAQTGD-CVQLNESLCIGCNLCAVACPFGaiqsggsrpvamansydtyIPCSIRSSNPstsaglrcfgedllswepg 143
Cdd:cd10558   85 PgAIVQYANgIVDFQSDKCIGCGYCIKGCPFD-------------------IPRISKDDNK------------------- 126

                        170       180       190
                 ....*....|....*....|....*....|...
gi 491457394 144 vrsiAVKCDLCEFR---AEGPACVSACPSQSLS 173
Cdd:cd10558  127 ----MYKCTLCSDRvsvGLEPACVKTCPTGALH 155
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 8-198 3.59e-13

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: 66.26  E-value: 3.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACS---------TVHKAQGLQQAPRLT--VMRH----EQAT---------------MPVQCRHCDDA 57
Cdd:cd10560    5 DTSICIGCKACEVACKqwnqlpadgYDFSGMSYDNTGDLSasTWRHvkfiERPTedgpaneggdlqwlfMSDVCKHCTDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  58 PCIKVCPVEAIAQTG-DCVQLNESLCIGCNLCAVACPFGAIQSGgsrpvamansydtyipcsirssnpstsaglrcfGED 136
Cdd:cd10560   85 GCLEACPTGAIFRTEfGTVYIQPDICNGCGYCVAACPFGVIDRN---------------------------------EET 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491457394 137 LLSWepgvrsiavKCDLCEFR-AEG--PACVSACPSQSLSIVNDTACANAARDRrlqAANAHPQG 198
Cdd:cd10560  132 GRAH---------KCTLCYDRlKDGlePACAKACPTGSIQFGPLEELRERARAR---VEQLHEQG 184
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 3-97 4.22e-13

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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 63.89  E-value: 4.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   3 RFVIADPKLCIGCGTCMAACSTVHKAQGLQQAPRLTVMRHEQATMPVQCRHCDDapCIKVCPVEAIAQT-GDCVQLNESL 81
Cdd:cd16372    1 KLLVTDPEKCIGCLQCEEACSKTFFKEEDREKSCIRITETEGGYAINVCNQCGE--CIDVCPTGAITRDaNGVVMINKKL 78

                         90
                 ....*....|....*.
gi 491457394  82 CIGCNLCAVACPFGAI 97
Cdd:cd16372   79 CVGCLMCVGFCPEGAM 94
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
6-98 6.56e-13

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 66.97  E-value: 6.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   6 IADPKLCIGCGTCMAACSTVHKAQGLQQAPRLTVMRHEQATMPVQ--CRHCDdaPCIKVCPVEAIAQTGDCVQLNESLCI 83
Cdd:COG4624   46 SACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKekCKNCY--PCVRACPVKAIKVDDGKAEIDEEKCI 123

                         90
                 ....*....|....*
gi 491457394  84 GCNLCAVACPFGAIQ 98
Cdd:COG4624  124 SCGQCVAVCPFGAIT 138
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 3-98 7.55e-13

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: 63.45  E-value: 7.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   3 RFVIADPKLCIGCGTCMAACSTVHKAQGLQQAPRLTVMRH---EQATMPVQCRHCDDAPCIKVCPVEAIAQ-TGDCVQLN 78
Cdd:cd16370    2 RLRVKDMERCIGCYSCMLACSRRVHKSASLSKSAIRVRTRgglEGGFTVVVCRACEDPPCAEACPTGALEPrKGGGVVLD 81

                         90       100
                 ....*....|....*....|
gi 491457394  79 ESLCIGCNLCAVACPFGAIQ 98
Cdd:cd16370   82 KEKCIGCGNCVKACIVGAIF 101
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
8-168 1.18e-12

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 65.85  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTV------HKAQGLQQAP--------------RLTVMRH------EQATMPVQCRHCDDAPCIK 61
Cdd:PRK10882  43 DSTLCVGCQACVTKCQEInfpernPQGEQTWDNPdklspytnniikvwKSGTGVNkdqeenGYAYIKKQCMHCVDPNCVS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  62 VCPVEAI---AQTGdCVQLNESLCIGCNLCAVACPFGAIQSGgsrpvamansYDTYIPcSIrssnpstsaglrcfgedll 138
Cdd:PRK10882 123 VCPVSALtkdPKTG-IVHYDKDVCTGCRYCMVACPFNVPKYD----------YNNPFG-AI------------------- 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491457394 139 swepgvrsiaVKCDLCEFRA-------EGPACVSACP 168
Cdd:PRK10882 172 ----------HKCELCNQKGverldkgGLPGCVEVCP 198
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
8-96 2.97e-12

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 64.13  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTvhKAQGLQQAPRLTVMRHEQAT----------MPVQCRHCDDAPCIKVCPVEAIAQTGD-CVQ 76
Cdd:PRK14993  49 DLRRCIGCQSCTVSCTI--ENQTPQGAFRTTVNQYQVQRegsqevtnvlLPRLCNHCDNPPCVPVCPVQATFQREDgIVV 126

                         90       100
                 ....*....|....*....|
gi 491457394  77 LNESLCIGCNLCAVACPFGA 96
Cdd:PRK14993 127 VDNKRCVGCAYCVQACPYDA 146
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 8-175 7.43e-11

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of 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: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 58.14  E-value: 7.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAACSTVHkaqGLQQAPRLTVMRHEQATMP----------VQCRHCDDAPCIKVCPVEAIA--QTGDCV 75
Cdd:cd10553    8 DSKRCIGCLACEVHCKVKN---NLPVGPRLCRIFAVGPKMVggkprlkfvyMSCFHCENPWCVKACPTGAMQkrEKDGIV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  76 QLNESLCIGCNLCAVACPFGAIQsggsrpvamansydtyipcsirsSNPSTSAglrcfgedllswepgvrsiAVKCDLCE 155
Cdd:cd10553   85 YVDQELCIGCKACIEACPWGIPQ-----------------------WNPATGK-------------------VVKCDYCM 122

                        170       180
                 ....*....|....*....|...
gi 491457394 156 FR---AEGPACVSACPSQSLSIV 175
Cdd:cd10553  123 DRidqGLKPACVTGCTTHALSFV 145
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 4-97 8.48e-11

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 58.88  E-value: 8.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   4 FVIaDPKLCIGCGTCMAACSTVH---------KAQ--------GLQQAPRLTVMRHEQATMPVQCRHCDDAPCIKVCPVE 66
Cdd:cd10552    1 LVI-DVAKCNGCYNCFLACKDEHvgndwpgyaAPQprhghfwmRILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDG 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491457394  67 AIAQTGD-CVQLNESLCIGCNLCAVACPFGAI 97
Cdd:cd10552   80 AVYKRDDgIVIIDPEKAKGQKQLVDACPYGAI 111
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-174 1.08e-09

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: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 56.28  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  47 MPVQCRHCDDAPCIKVCPVEAIAQTGD-CVQLNESLCIGCNLCAVACPFGAiqsggsrpvamansydtyipcsirssnPS 125
Cdd:cd16368   87 IPRRCMHCDNPPCAKLCPFGAARKTPEgAVYIDDDLCFGGAKCRDVCPWHI---------------------------PQ 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491457394 126 TSAGLRCFgedlLSWEPGVRSIAV--KCDLCEFR-AEG--PACVSACPSQSLSI 174
Cdd:cd16368  140 RQAGVGIY----LHLAPEYAGGGVmyKCDLCKDLlAQGkpPACIEACPKGAQYF 189
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 51-98 1.64e-09

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 52.74  E-value: 1.64e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 491457394  51 CRHCDDapCIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG4231   24 CTGCGA--CVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIK 69
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
51-98 1.76e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 52.81  E-value: 1.76e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 491457394  51 CRHCDDapCIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG2768   13 CIGCGA--CVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGAIK 58
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 1-97 4.04e-09

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: 53.17  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   1 MNRFVIADPKLCIGCGTCMAACSTvhKAQGLQQAPRLTVMRHEQATM-PVQCRHCDDapCIKVCPVEAIAQTGD-CVQLN 78
Cdd:cd10549   31 IARGPEIDEDKCVFCGACVEVCPT--GAIELTPEGKEYVPKEKEAEIdEEKCIGCGL--CVKVCPVDAITLEDElEIVID 106

                         90
                 ....*....|....*....
gi 491457394  79 ESLCIGCNLCAVACPFGAI 97
Cdd:cd10549  107 KEKCIGCGICAEVCPVNAI 125
PRK09898 PRK09898
ferredoxin-like protein;
12-95 1.87e-08

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 52.92  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  12 CIGCGTCMAACSTVHKAQGLQQAPRLTVMRH----------------EQATMPVQCRHCDDAPCIKVCPVEAIA--QTGD 73
Cdd:PRK09898  68 CTGCHRCEISCTNFNDGSVGTFFSRIKIHRNyffgdngvgsggglygDLNYTADTCRQCKEPQCMNVCPIGAITwqQKEG 147

                         90       100
                 ....*....|....*....|..
gi 491457394  74 CVQLNESLCIGCNLCAVACPFG 95
Cdd:PRK09898 148 CITVDHKRCIGCSACTTACPWM 169
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 48-98 1.77e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 50.94  E-value: 1.77e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491457394  48 PVQCRHcddaPCIKVCPV-----EAI--AQTGDCVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG1245   14 PKKCNY----ECIKYCPVnrtgkEAIeiDEDDGKPVISEELCIGCGICVKKCPFDAIS 67
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 50-100 2.18e-07

archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 49.87  E-value: 2.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491457394   50 QCRHCDDapCIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAIQSG 100
Cdd:TIGR02700 149 RCKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAIHGG 197
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 51-97 2.88e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 46.58  E-value: 2.88e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 491457394  51 CRHCDDapCIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAI 97
Cdd:COG2221   17 CIGCGL--CVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGAI 61
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 59-98 6.86e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 45.49  E-value: 6.86e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 491457394  59 CIKVCPVEAIAQTGDC-VQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG1149   19 CVEVCPEGAIKLDDGGaPVVDPDLCTGCGACVGVCPTGAIT 59
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
48-97 7.39e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.42  E-value: 7.39e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491457394  48 PVQCRHcddaPCIKVCPV-----EAIAQTGDC--VQLNESLCIGCNLCAVACPFGAI 97
Cdd:PRK13409  14 PKKCNY----ECIKYCPVvrtgeETIEIDEDDgkPVISEELCIGCGICVKKCPFDAI 66
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 48-96 7.57e-07

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 46.09  E-value: 7.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491457394   48 PVQCRHCDDAPCIKVCPVEAIAQTGD--CVQLNESLCIGCNLCAVACPFGA 96
Cdd:pfam13247   7 PEQCRHCLNPPCKASCPVGAIYKDEEtgAVLLDEKTCRGWRECVSACPYNI 57
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
51-98 1.97e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.93  E-value: 1.97e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 491457394  51 CRHCddAPCIKVCPVEAIAQTGDCV-QLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG1148  498 CTGC--GRCVEVCPYGAISIDEKGVaEVNPALCKGCGTCAAACPSGAIS 544
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
2-98 2.07e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.24  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   2 NRFVIADPKLCIGCGTCMAACstvhkaqglqqaPR-LTVMRHEQATMPVQCRHCDDAP---------------CIKVCPV 65
Cdd:PRK07118 160 NGLPVVDEDKCTGCGACVKAC------------PRnVIELIPKSARVFVACNSKDKGKavkkvcevgcigcgkCVKACPA 227

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491457394  66 EAIAQTGDCVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:PRK07118 228 GAITMENNLAVIDQEKCTSCGKCVEKCPTKAIR 260
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 6-97 3.52e-06

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: 45.08  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   6 IADPKLCIGCGTCMAACSTvhkaQGLQQAPRLTVMRHEQATmPVQCRHCddAPCIKVCPVEAIAQTGDC---------VQ 76
Cdd:cd10549    2 KYDPEKCIGCGICVKACPT----DAIELGPNGAIARGPEID-EDKCVFC--GACVEVCPTGAIELTPEGkeyvpkekeAE 74

                         90       100
                 ....*....|....*....|.
gi 491457394  77 LNESLCIGCNLCAVACPFGAI 97
Cdd:cd10549   75 IDEEKCIGCGLCVKVCPVDAI 95
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 51-97 5.33e-06

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: 43.50  E-value: 5.33e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 491457394  51 CRHCDdaPCIKVCPVEAIAQT-GDCVQLNESLCIGCNLCAVACPFGAI 97
Cdd:COG1144   32 CIGCG--LCWIVCPDGAIRVDdGKYYGIDYDYCKGCGICAEVCPVKAI 77
NapF COG1145
Ferredoxin [Energy production and conversion];
51-98 8.94e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 45.48  E-value: 8.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 491457394  51 CRHCDdaPCIKVCPVEAI--AQTGDCVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG1145  184 CIGCG--LCVKVCPTGAIrlKDGKPQIVVDPDKCIGCGACVKVCPVGAIS 231
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 51-98 9.01e-06

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: 42.43  E-value: 9.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491457394  51 CRHCDDapCIKVCPVEAIAQTGD----CVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG1143    4 CIGCGL--CVRVCPVDAITIEDGepgkVYVIDPDKCIGCGLCVEVCPTGAIS 53
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 48-98 1.65e-05

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: 43.15  E-value: 1.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491457394  48 PVQCRHCddAPCIKVCPVEAI-----AQTGDCVQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:cd10549    5 PEKCIGC--GICVKACPTDAIelgpnGAIARGPEIDEDKCVFCGACVEVCPTGAIE 58
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 10-97 2.37e-05

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: 43.01  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  10 KLCIGCGTCMAACST-----VHKAQGLQQA--PRLTVmrHEQAtmpvqCRHCDDApCIKVCPVEAI---AQTGDCVQ--- 76
Cdd:cd16373   14 ALCIRCGLCVEACPTgviqpAGLEDGLEGGrtPYLDP--REGP-----CDLCCDA-CVEVCPTGALrplDLEEQKVKmgv 85

                         90       100
                 ....*....|....*....|....*....
gi 491457394  77 --LNESLCI------GCNLCAVACPFGAI 97
Cdd:cd16373   86 avIDKDRCLawqggtDCGVCVEACPTEAI 114
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 51-97 3.01e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.85  E-value: 3.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 491457394  51 CRHCDDapCIKVCPVEAIAQTGD---CVQLNESLCIGCNLCAVACPFGAI 97
Cdd:COG1146   10 CIGCGA--CVEVCPVDVLELDEEgkkALVINPEECIGCGACELVCPVGAI 57
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 12-94 3.69e-05

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 43.46  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  12 CIGCGTCMAAC--STVHKAQGLQQAPRLT---VMRHeqatmpVQCRHCDDAPCIKVCPVEAI---------AQTGDCVQL 77
Cdd:PRK09476  61 CIRCGLCVQACpyDTLKLATLASGLSAGTpyfVARD------IPCEMCEDIPCVKACPSGALdrelvdiddARMGLAVLV 134

                         90       100
                 ....*....|....*....|..
gi 491457394  78 NESLCIG-----CNLCAVACPF 94
Cdd:PRK09476 135 DQENCLNfqglrCDVCYRVCPL 156
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 50-100 4.96e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 43.71  E-value: 4.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491457394  50 QCRHCDDapCIKVCPVEAIAQ--TGDCVQLNESLCIGCNLCAVACPFGAIQSG 100
Cdd:PRK12771 511 NCFECDN--CYGACPQDAIIKlgPGRRYHFDYDKCTGCHICADVCPCGAIEMG 561
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 59-97 6.00e-05

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: 42.76  E-value: 6.00e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 491457394  59 CIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAI 97
Cdd:cd03110   72 CERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGAI 110
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
50-98 7.58e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 42.74  E-value: 7.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 491457394  50 QCRHCDDapCIKVCPVEAIAQTGdcvQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:COG0348  211 DCIDCGL--CVKVCPMGIDIRKG---EINQSECINCGRCIDACPKDAIR 254
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
50-103 4.95e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 40.78  E-value: 4.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491457394  50 QCRHCDDAPCIKVCPVEAIAQTGDCVQLNESLCIGCNLCAVACPFGAIQSGGSR 103
Cdd:COG4624   61 CCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGK 114
PRK06273 PRK06273
ferredoxin; Provisional
 79-116 6.01e-04

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 39.31  E-value: 6.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 491457394  79 ESLCIGCNLCAVACPFGAIQSGGSRPVAMANSY-DTYIP 116
Cdd:PRK06273  48 EELCIGCGGCANVCPTKAIEMIPVEPVKITEGYvKTKIP 86
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 59-98 6.94e-04

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 39.59  E-value: 6.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491457394  59 CIKVCPVEAIaqTGDCVQL---NESLCIGCNLCAVACPFGAIQ 98
Cdd:COG2878  145 CIKACPFDAI--VGAAKGMhtvDEDKCTGCGLCVEACPVDCIE 185
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 12-98 1.15e-03

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: 37.99  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  12 CIGCGTCMAACSTvhkaqGLQQAPRLTVMRHE-------QATMPVQCRHCDDApcikvCPVEAIA---QTGDCVQ--LNE 79
Cdd:cd10564   47 CTFCGACAEACPE-----GALDPAREAPWPLRaeigdscLALQGVECRSCQDA-----CPTQAIRfrpRLGGIALpeLDA 116

                         90
                 ....*....|....*....
gi 491457394  80 SLCIGCNLCAVACPFGAIQ 98
Cdd:cd10564  117 DACTGCGACVSVCPVGAIT 135
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 47-168 1.50e-03

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 38.82  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394  47 MPVQCRHCDDAPCIKVCPVEAI---AQTGdCVQLNESLCIGCNLCAVACPFGAIqsggsrpvamansydtYIpcsirssN 123
Cdd:cd10555  129 LPRICNHCTNPACLAACPRKAIykrEEDG-IVLVDQDRCRGYRYCVEACPYKKI----------------YF-------N 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491457394 124 PstsaglrcfgedllswepgVRSIAVKCDLCEFRAE---GPACVSACP 168
Cdd:cd10555  185 P-------------------VEQKSEKCIFCYPRIEkgvAPACARQCV 213
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
82-98 1.82e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.94  E-value: 1.82e-03
                         10
                 ....*....|....*..
gi 491457394  82 CIGCNLCAVACPFGAIQ 98
Cdd:PRK05888  60 CIACKLCAAICPADAIT 76
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
8-93 2.62e-03

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 38.39  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491457394   8 DPKLCIGCGTCMAAC-STVHkaqglqQAPRLTVMRHEQatmpvqcrhcddapcikvcpveaiaqtgdcVQLNESLCIGCN 86
Cdd:PRK08318 340 DQDKCIGCGRCYIACeDTSH------QAIEWDEDGTRT------------------------------PEVIEEECVGCN 383


                 ....*..
gi 491457394  87 LCAVACP 93
Cdd:PRK08318 384 LCAHVCP 390
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 75-98 2.79e-03

4Fe-4S binding 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.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 34.15  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....
gi 491457394   75 VQLNESLCIGCNLCAVACPFGAIQ 98
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 75-105 3.98e-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: 35.09  E-value: 3.98e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 491457394  75 VQLNESLCIGCNLCAVACPFGAIQSGGSRPV 105
Cdd:COG1149    6 PVIDEEKCIGCGLCVEVCPEGAIKLDDGGAP 36
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 59-99 3.99e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 36.70  E-value: 3.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 491457394   59 CIKVCPVEAIAQTGDCVQ-LNESLCIGCNLCAVACPFGAIQS 99
Cdd:TIGR01944 121 CIQACPVDAIVGAAKAMHtVIADECTGCDLCVEPCPTDCIEM 162
PRK13795 PRK13795
hypothetical protein; Provisional
 59-93 5.44e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 37.67  E-value: 5.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 491457394  59 CIKVCPVEAIAQTG--DCVQLNESLCIGCNLCAVACP 93
Cdd:PRK13795 589 CVGACPTGAIRIEEgkRKISVDEEKCIHCGKCTEVCP 625
PRK13984 PRK13984
putative oxidoreductase; Provisional
 4-63 6.49e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 37.44  E-value: 6.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491457394   4 FVIADPKLCIGCGTCMAACSTvhKAQGLQQAPRLTVMRHEQATMPV----QCRHCddAPCIKVC 63
Cdd:PRK13984  39 FHINDWEKCIGCGTCSKICPT--DAITMVEVPDLPQEYGKKPQRPVidygRCSFC--ALCVDIC 98
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 51-96 7.37e-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: 33.65  E-value: 7.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491457394   51 CRHCDDapCIKVCPVEAI-------AQTGDCVQLNESLCIGCNLCAVACPFGA 96
Cdd:pfam12838   1 CIGCGA--CVAACPVGAItldevgeKKGTKTVVIDPERCVGCGACVAVCPTGA 51
 
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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