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Conserved domains on  [gi|496089051|ref|WP_008813558|]
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MULTISPECIES: electron transport complex subunit RsxG [Hafnia]

Protein Classification

electron transport complex subunit G( domain architecture ID 10011734)

electron transport complex subunit G is part of a membrane complex that may be involved in transporting electrons to nitrogenase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01908 PRK01908
electron transport complex protein RnfG; Validated
5-205 2.15e-141

electron transport complex protein RnfG; Validated


:

Pssm-ID: 179350  Cd Length: 205  Bit Score: 392.70  E-value: 2.15e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   5 MRRHGTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTDKRLGSTAPHHLYLARK 84
Cdd:PRK01908   1 MRKHGITLALFAALCTGLTAVVNQLTKDTIAEQAALQQKALLDQVIPAERYDNDLQESCYLVTDPALGKDGPHRVYIARK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  85 DGVPVAAAVETTAPDGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWINRFRNQVVKGDNDPRWFVKKD 164
Cdd:PRK01908  81 DGKPVAAAIEATAPDGYSGAIQLLVGADFNGTVLGVRVLEHHETPGLGDKIELRISDWITHFSGKKISGENDKHWAVKKD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 496089051 165 GGMFDQFTGATITPRAVVNEVRHTVVFLQQNRDRLESMPRC 205
Cdd:PRK01908 161 GGDFDQFTGATITPRAVVNAVKRAALYAQTLPAQLSSLPAC 201
 
Name Accession Description Interval E-value
PRK01908 PRK01908
electron transport complex protein RnfG; Validated
5-205 2.15e-141

electron transport complex protein RnfG; Validated


Pssm-ID: 179350  Cd Length: 205  Bit Score: 392.70  E-value: 2.15e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   5 MRRHGTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTDKRLGSTAPHHLYLARK 84
Cdd:PRK01908   1 MRKHGITLALFAALCTGLTAVVNQLTKDTIAEQAALQQKALLDQVIPAERYDNDLQESCYLVTDPALGKDGPHRVYIARK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  85 DGVPVAAAVETTAPDGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWINRFRNQVVKGDNDPRWFVKKD 164
Cdd:PRK01908  81 DGKPVAAAIEATAPDGYSGAIQLLVGADFNGTVLGVRVLEHHETPGLGDKIELRISDWITHFSGKKISGENDKHWAVKKD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 496089051 165 GGMFDQFTGATITPRAVVNEVRHTVVFLQQNRDRLESMPRC 205
Cdd:PRK01908 161 GGDFDQFTGATITPRAVVNAVKRAALYAQTLPAQLSSLPAC 201
RnfG COG4659
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfG subunit [Energy production and ...
2-197 6.45e-93

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


Pssm-ID: 443697 [Multi-domain]  Cd Length: 192  Bit Score: 269.77  E-value: 6.45e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   2 LSTMRRHGTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTDKRlGSTAPHHLYL 81
Cdd:COG4659    1 MKSILKMALILGLIALVAGGLLALVYELTKPPIAANEAEALLAALKQVLPEASFDNDLLADTLTVTDPE-GSGGPLTVYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  82 ARKDGVPVAAAVETtAPDGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARiSDWINRFRNQVVkGDNDPRWFV 161
Cdd:COG4659   80 ARKGGEPVGYAFEA-APDGYGGPIKLLVGIDPDGTILGVRVLSHKETPGLGDKIEER-SDWILQFKGKSL-DNPDARWAV 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 496089051 162 KKDGGMFDQFTGATITPRAVVNEVRHTVVFLQQNRD 197
Cdd:COG4659  157 KKDGGEFDAITGATITSRAVVKAVNRALEFFKEHRA 192
rnfG TIGR01947
electron transport complex, RnfABCDGE type, G subunit; The six subunit complex RnfABCDGE in ...
9-194 8.69e-82

electron transport complex, RnfABCDGE type, G 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 A subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273889 [Multi-domain]  Cd Length: 186  Bit Score: 241.49  E-value: 8.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051    9 GTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTD-KRLGSTAPHHLYLARKDGV 87
Cdd:TIGR01947   1 GLLLGLFAAVSAGLLALVNQFTKEQIAEAEAKQQLEALKQVLPQGLYDNDLLESTVPEVDeDLLGLGTILPVYGAKKGGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   88 PVAAAVETTAPdGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWINRFRNQVVKGDNDPRWFVKKDGGM 167
Cdd:TIGR01947  81 VVAYVLEVSAP-GYSGPIQLLVGIDKDGTILGVRVLSHKETPGLGDKIELRISDWIEGFAGKSLADPDDDHWAVKKDGGQ 159
                         170       180
                  ....*....|....*....|....*..
gi 496089051  168 FDQFTGATITPRAVVNEVRHTVVFLQQ 194
Cdd:TIGR01947 160 FDQFTGATITPRAVVNAVKRALRYFKE 186
FMN_bind smart00900
This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR ...
100-186 3.65e-25

This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins;


Pssm-ID: 214897 [Multi-domain]  Cd Length: 86  Bit Score: 93.95  E-value: 3.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   100 GYSGAIQLLVA-ADFSGKVLGVRVLEHHETPGlgDKIDAriSDWINRFRNQVVkgDNDPRWFVKK-DGGMFDQFTGATIT 177
Cdd:smart00900   1 GYGGPITVLVTvKDDKGKITGVKVLEHKETPG--DGIDE--PKWIGQFAGKAL--EKLAKEIVKKqSGGDVDAISGATIT 74

                   ....*....
gi 496089051   178 PRAVVNEVR 186
Cdd:smart00900  75 SRAVKDAVK 83
FMN_bind pfam04205
FMN-binding domain; This conserved region includes the FMN-binding site of the NqrC protein as ...
100-186 1.75e-18

FMN-binding domain; This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins. This domain is post-translationally flavinylated that may facilitate electron transfer, and thus, resembles multiheme cytochromes.


Pssm-ID: 461226 [Multi-domain]  Cd Length: 71  Bit Score: 76.11  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  100 GYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWInrfrnqvvkgdndprwfvkKDGGMFDQFTGATITPR 179
Cdd:pfam04205   1 GYGGPITVLVGVDGDGTITGIKVLEHSETPGLGIKEQKVKKDKI-------------------EGGQDVDAISGATITSR 61

                  ....*..
gi 496089051  180 AVVNEVR 186
Cdd:pfam04205  62 AVVEAVK 68
 
Name Accession Description Interval E-value
PRK01908 PRK01908
electron transport complex protein RnfG; Validated
5-205 2.15e-141

electron transport complex protein RnfG; Validated


Pssm-ID: 179350  Cd Length: 205  Bit Score: 392.70  E-value: 2.15e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   5 MRRHGTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTDKRLGSTAPHHLYLARK 84
Cdd:PRK01908   1 MRKHGITLALFAALCTGLTAVVNQLTKDTIAEQAALQQKALLDQVIPAERYDNDLQESCYLVTDPALGKDGPHRVYIARK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  85 DGVPVAAAVETTAPDGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWINRFRNQVVKGDNDPRWFVKKD 164
Cdd:PRK01908  81 DGKPVAAAIEATAPDGYSGAIQLLVGADFNGTVLGVRVLEHHETPGLGDKIELRISDWITHFSGKKISGENDKHWAVKKD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 496089051 165 GGMFDQFTGATITPRAVVNEVRHTVVFLQQNRDRLESMPRC 205
Cdd:PRK01908 161 GGDFDQFTGATITPRAVVNAVKRAALYAQTLPAQLSSLPAC 201
RnfG COG4659
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfG subunit [Energy production and ...
2-197 6.45e-93

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


Pssm-ID: 443697 [Multi-domain]  Cd Length: 192  Bit Score: 269.77  E-value: 6.45e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   2 LSTMRRHGTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTDKRlGSTAPHHLYL 81
Cdd:COG4659    1 MKSILKMALILGLIALVAGGLLALVYELTKPPIAANEAEALLAALKQVLPEASFDNDLLADTLTVTDPE-GSGGPLTVYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  82 ARKDGVPVAAAVETtAPDGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARiSDWINRFRNQVVkGDNDPRWFV 161
Cdd:COG4659   80 ARKGGEPVGYAFEA-APDGYGGPIKLLVGIDPDGTILGVRVLSHKETPGLGDKIEER-SDWILQFKGKSL-DNPDARWAV 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 496089051 162 KKDGGMFDQFTGATITPRAVVNEVRHTVVFLQQNRD 197
Cdd:COG4659  157 KKDGGEFDAITGATITSRAVVKAVNRALEFFKEHRA 192
rnfG TIGR01947
electron transport complex, RnfABCDGE type, G subunit; The six subunit complex RnfABCDGE in ...
9-194 8.69e-82

electron transport complex, RnfABCDGE type, G 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 A subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273889 [Multi-domain]  Cd Length: 186  Bit Score: 241.49  E-value: 8.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051    9 GTTLALFAVLATGLTAVVNELTKDTIAHQAELQQKQLFDQVLPAEMYNNELQHECYVVTD-KRLGSTAPHHLYLARKDGV 87
Cdd:TIGR01947   1 GLLLGLFAAVSAGLLALVNQFTKEQIAEAEAKQQLEALKQVLPQGLYDNDLLESTVPEVDeDLLGLGTILPVYGAKKGGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   88 PVAAAVETTAPdGYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWINRFRNQVVKGDNDPRWFVKKDGGM 167
Cdd:TIGR01947  81 VVAYVLEVSAP-GYSGPIQLLVGIDKDGTILGVRVLSHKETPGLGDKIELRISDWIEGFAGKSLADPDDDHWAVKKDGGQ 159
                         170       180
                  ....*....|....*....|....*..
gi 496089051  168 FDQFTGATITPRAVVNEVRHTVVFLQQ 194
Cdd:TIGR01947 160 FDQFTGATITPRAVVNAVKRALRYFKE 186
FMN_bind smart00900
This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR ...
100-186 3.65e-25

This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins;


Pssm-ID: 214897 [Multi-domain]  Cd Length: 86  Bit Score: 93.95  E-value: 3.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   100 GYSGAIQLLVA-ADFSGKVLGVRVLEHHETPGlgDKIDAriSDWINRFRNQVVkgDNDPRWFVKK-DGGMFDQFTGATIT 177
Cdd:smart00900   1 GYGGPITVLVTvKDDKGKITGVKVLEHKETPG--DGIDE--PKWIGQFAGKAL--EKLAKEIVKKqSGGDVDAISGATIT 74

                   ....*....
gi 496089051   178 PRAVVNEVR 186
Cdd:smart00900  75 SRAVKDAVK 83
FMN_bind pfam04205
FMN-binding domain; This conserved region includes the FMN-binding site of the NqrC protein as ...
100-186 1.75e-18

FMN-binding domain; This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins. This domain is post-translationally flavinylated that may facilitate electron transfer, and thus, resembles multiheme cytochromes.


Pssm-ID: 461226 [Multi-domain]  Cd Length: 71  Bit Score: 76.11  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  100 GYSGAIQLLVAADFSGKVLGVRVLEHHETPGLGDKIDARISDWInrfrnqvvkgdndprwfvkKDGGMFDQFTGATITPR 179
Cdd:pfam04205   1 GYGGPITVLVGVDGDGTITGIKVLEHSETPGLGIKEQKVKKDKI-------------------EGGQDVDAISGATITSR 61

                  ....*..
gi 496089051  180 AVVNEVR 186
Cdd:pfam04205  62 AVVEAVK 68
NosR COG3901
Transcriptional regulator NosR of nitric oxide reductase [Transcription];
5-185 6.85e-06

Transcriptional regulator NosR of nitric oxide reductase [Transcription];


Pssm-ID: 443108 [Multi-domain]  Cd Length: 713  Bit Score: 46.08  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   5 MRRHGTTLALFAVLATGLTAVVNELTKDTIAHQAelqqkqLFDQVLPAEMYNnELQHECYVVTdkrlgstaphhlylARK 84
Cdd:COG3901    1 MRSLLLLALLLLLLLLAAAAAAASTLPDFLARVP------CAEVFPGATRFG-EREGDPPVAP--------------VYK 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051  85 DGVPVAAAVETT----APdGYSGA-IQLLVAADFSGKVLGVRVLEHHEtP----GLGdkiDARISDWINRFR------NQ 149
Cdd:COG3901   60 GGELLGYVFLTTdfvdTP-GYSGKpINTLVGIDTDGRIVGVKLLKHSE-PilliGIP---ESKLRAFIEQYVgldvkdEI 134
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 496089051 150 VVKGDNDPrwfvkkDGGMFDQFTGATITPRaVVNEV 185
Cdd:COG3901  135 EVGGSRDE------GAHGLDIISGATVTVM-VINDS 163
NqrC COG2869
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrC [Energy production and ...
117-186 1.70e-04

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrC [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrC is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442116  Cd Length: 257  Bit Score: 41.34  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051 117 VLGVRVLEHHETPGLGDKIDARisDWINRFRN------------QVVKGDNDPrwfvKKDGGmFDQFTGATITPRAVVNE 184
Cdd:COG2869  163 VKGLTFYHHGETPGLGAEIENP--KWQAQFVGkkifdedgfvaiRVVKGGADP----KDEHE-VDGLSGATLTSNGVTNM 235

                 ..
gi 496089051 185 VR 186
Cdd:COG2869  236 LK 237
PRK05346 PRK05346
Na(+)-translocating NADH-quinone reductase subunit C; Provisional
117-181 1.46e-03

Na(+)-translocating NADH-quinone reductase subunit C; Provisional


Pssm-ID: 235423  Cd Length: 256  Bit Score: 38.67  E-value: 1.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496089051 117 VLGVRVLEHHETPGLGDKIDARisDWINRFRN------------QVVKGDNDPrwfvKKDGGMfDQFTGATITPRAV 181
Cdd:PRK05346 161 VKGLTFYEHGETPGLGGEIENP--QWQAQWVGkklfdeqgkpaiKVVKGGASA----KDEHGV-DGLSGATLTSNGV 230
nqrC TIGR01938
NADH:ubiquinone oxidoreductase, Na(+)-translocating, C subunit; This model represents the NqrC ...
79-183 5.98e-03

NADH:ubiquinone oxidoreductase, Na(+)-translocating, C subunit; This model represents the NqrC subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273886  Cd Length: 251  Bit Score: 36.60  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089051   79 LYLARKDGVPVAAAVETTAPDGYSGAIQLLVAADFSGK-VLGVRVLEHHETPGLGDKIDAriSDWINRFRN--------- 148
Cdd:TIGR01938 124 VYLVKKDGGGITKVILPIYGFGLWGPIYGFVALEEDGNtVLGITYYQQGETPGLGAEIEN--PEWQAQFVGkklfdeqgq 201
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 496089051  149 ----QVVKGDNDPrwfvKKDGGMFDQFTGATITPRAVVN 183
Cdd:TIGR01938 202 alalEVVKGNGAS----AKAEHSVDGISGATLTSNGVQE 236
 
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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