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Conserved domains on  [gi|520913022|ref|WP_020332579|]
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MULTISPECIES: cytochrome c oxidase accessory protein CcoG [Vibrio]

Protein Classification

cytochrome c oxidase accessory protein CcoG( domain architecture ID 11494955)

cytochrome c oxidase accessory protein CcoG is a RdxA/RdxB/FixG family protein similar to Sinorhizobium meliloti nitrogen fixation protein FixG and Rhodobacter sphaeroides RdxB and is required for the formation of a high-affinity cbb3-type cytochrome oxidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ccoG_rdxA_fixG TIGR02745
cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are ...
 44-471 0e+00

cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum.


:

Pssm-ID: 274278 [Multi-domain]  Cd Length: 434  Bit Score: 633.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022   44 YQKLRRYGGWFLLLLFGLVPWISYGDRQAILLDIGHQQFNFFGTTLYPQDLTLLALLFMIAAFGLFFITTFLGRVWCGYL 123
Cdd:TIGR02745   1 FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITTLAGRVWCGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  124 CPQTVWTFMYIWFEEKLEGSANKRRKQDGSKMTANLAMRKTAKHIAWFAIALATGFTFVGYFVPVRDLVIDFFTFNSTFW 203
Cdd:TIGR02745  81 CPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIFYFVPAPDLFAYLFTGPADHP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  204 PVFWVMFFAVCTYGNAGWMRSIMCIHMCPYARFQSAMFDKDTFIVGYNTERGEQRGPRSRKADKKALG-LGDCIDCDLCV 282
Cdd:TIGR02745 161 AYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEKRGEPRGPRKGKKDPKAPGpLGDCIDCNLCV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  283 QVCPTGIDIRDGLQYECINCGACIDACDTTMERMGYDKGLISYTTEHRLSGKHTK-VMRPKLLGYGAVLLVMIGLFFAQV 361
Cdd:TIGR02745 241 QVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGLISYTSEAALEGRKKVrLLRPRTIGYAAVLAIVIGLLAIAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  362 AAVDPAGLSVIRDRNQLFRTNSSGEIENTYTLKVINKTQHIQTYKLDVSGLTDVSWYG-KQTVQVEPGEVLNLPMSLGVK 440
Cdd:TIGR02745 321 STREPMDLNVLRDRNLLYVRNSDGVVENTYTLKILNKTEQPHEYYLSVLGLPGIKIEGpGAPIHVKAGEKVKLPVFLRTP 400

                         410       420       430
                  ....*....|....*....|....*....|...
gi 520913022  441 PDNLSSPVA--TIQFILTDDSNQFTMQVESRFI 471
Cdd:TIGR02745 401 PDALKSGITsiEIRAYAEDDSEGIRVERESVFV 433
 
Name Accession Description Interval E-value
ccoG_rdxA_fixG TIGR02745
cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are ...
 44-471 0e+00

cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum.


Pssm-ID: 274278 [Multi-domain]  Cd Length: 434  Bit Score: 633.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022   44 YQKLRRYGGWFLLLLFGLVPWISYGDRQAILLDIGHQQFNFFGTTLYPQDLTLLALLFMIAAFGLFFITTFLGRVWCGYL 123
Cdd:TIGR02745   1 FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITTLAGRVWCGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  124 CPQTVWTFMYIWFEEKLEGSANKRRKQDGSKMTANLAMRKTAKHIAWFAIALATGFTFVGYFVPVRDLVIDFFTFNSTFW 203
Cdd:TIGR02745  81 CPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIFYFVPAPDLFAYLFTGPADHP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  204 PVFWVMFFAVCTYGNAGWMRSIMCIHMCPYARFQSAMFDKDTFIVGYNTERGEQRGPRSRKADKKALG-LGDCIDCDLCV 282
Cdd:TIGR02745 161 AYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEKRGEPRGPRKGKKDPKAPGpLGDCIDCNLCV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  283 QVCPTGIDIRDGLQYECINCGACIDACDTTMERMGYDKGLISYTTEHRLSGKHTK-VMRPKLLGYGAVLLVMIGLFFAQV 361
Cdd:TIGR02745 241 QVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGLISYTSEAALEGRKKVrLLRPRTIGYAAVLAIVIGLLAIAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  362 AAVDPAGLSVIRDRNQLFRTNSSGEIENTYTLKVINKTQHIQTYKLDVSGLTDVSWYG-KQTVQVEPGEVLNLPMSLGVK 440
Cdd:TIGR02745 321 STREPMDLNVLRDRNLLYVRNSDGVVENTYTLKILNKTEQPHEYYLSVLGLPGIKIEGpGAPIHVKAGEKVKLPVFLRTP 400

                         410       420       430
                  ....*....|....*....|....*....|...
gi 520913022  441 PDNLSSPVA--TIQFILTDDSNQFTMQVESRFI 471
Cdd:TIGR02745 401 PDALKSGITsiEIRAYAEDDSEGIRVERESVFV 433
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
36-330 7.37e-85

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 261.92  E-value: 7.37e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  36 YVRESKGTYQKLRRYGGWFLLLLFGLVPWISYGDRQAILLDIGHQQFNFFGTTLypqDLTLLALLFMIAAFGLFFITTFL 115
Cdd:COG0348    3 YPRLVKGRFRRLRRLVQLLFLLLFLLGPWLRWLGDPAVLLDLAERRFYLFGLFW---DFYLLALLLIGAALALFLLTLLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 116 GRVWCGYLCPQTVWTFMYIWFEEKLeGSANKRRKQDGSKmtanlaMRKTAKH---IAWFAIALATGFTFVGYFVPVRDLV 192
Cdd:COG0348   80 GRVWCGWVCPQGVLTELFSWLERKL-GDRRLKLPWSLSK------ILRWLKYiilALWLLLALLTGLTFFGYFSPIGTLL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 193 IDFFTFNSTFWpvfWVMFFAVCTYGNAGWMRSIMCIHMCPYARFQSAMFDKDTFIVGYNTergeqrgprsrkadkkalgl 272
Cdd:COG0348  153 RLLLFGVLGLW---LLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDR-------------------- 209

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 273 GDCIDCDLCVQVCPTGIDIRDGL--QYECINCGACIDACDTTMermgydkglISYTTEHR 330
Cdd:COG0348  210 GDCIDCGLCVKVCPMGIDIRKGEinQSECINCGRCIDACPKDA---------IRFSSRGE 260
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 222-328 1.43e-53

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404610 [Multi-domain]  Cd Length: 114  Bit Score: 175.28  E-value: 1.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  222 MRSIMCIHMCPYARFQSAMFDKDTFIVGYNTERGEQRGPRSR-------KADKKALGLGDCIDCDLCVQVCPTGIDIRDG 294
Cdd:pfam13746   1 ARENFCIYACPYGRFQSVMYDEDTLTVVYDAVRGEGIYGRKPpkaglktKELRQQKGVGDCIDCESCVQVCPTGIDIRKG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 520913022  295 LQYECINCGACIDACDTTMERMGYDKGLISYTTE 328
Cdd:pfam13746  81 LQLECINCGLCIDACNTIMGKLGKPRGLIRYSSE 114
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 256-311 3.23e-08

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: 52.01  E-value: 3.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520913022 256 EQRGPRSRKADKKALGLGD-CIDCDLCVQVCPTG-IDIRDGLQYE-----CINCGACIDACDT 311
Cdd:cd10549   60 TPEGKEYVPKEKEAEIDEEkCIGCGLCVKVCPVDaITLEDELEIVidkekCIGCGICAEVCPV 122
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
227-311 5.26e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 48.01  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 227 CIHMCPYARFQSAMFDKDTFIVGYNTERGeqrgprsrKADKKALGLGdCIDCDLCVQVCPTG-IDIRDGLQY----ECIN 301
Cdd:PRK07118 176 CVKACPRNVIELIPKSARVFVACNSKDKG--------KAVKKVCEVG-CIGCGKCVKACPAGaITMENNLAVidqeKCTS 246

                         90
                 ....*....|
gi 520913022 302 CGACIDACDT 311
Cdd:PRK07118 247 CGKCVEKCPT 256
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 274-309 9.26e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 41.00  E-value: 9.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 520913022 274 DCIDCDLCVQVCPTG-IDIRDGL---QYECINCGACIDAC 309
Cdd:NF038196 186 KCIGCGICAKVCPVNnIEMEDGKpvwGHNCTHCLACIHRC 225
 
Name Accession Description Interval E-value
ccoG_rdxA_fixG TIGR02745
cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are ...
 44-471 0e+00

cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum.


Pssm-ID: 274278 [Multi-domain]  Cd Length: 434  Bit Score: 633.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022   44 YQKLRRYGGWFLLLLFGLVPWISYGDRQAILLDIGHQQFNFFGTTLYPQDLTLLALLFMIAAFGLFFITTFLGRVWCGYL 123
Cdd:TIGR02745   1 FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITTLAGRVWCGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  124 CPQTVWTFMYIWFEEKLEGSANKRRKQDGSKMTANLAMRKTAKHIAWFAIALATGFTFVGYFVPVRDLVIDFFTFNSTFW 203
Cdd:TIGR02745  81 CPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIFYFVPAPDLFAYLFTGPADHP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  204 PVFWVMFFAVCTYGNAGWMRSIMCIHMCPYARFQSAMFDKDTFIVGYNTERGEQRGPRSRKADKKALG-LGDCIDCDLCV 282
Cdd:TIGR02745 161 AYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEKRGEPRGPRKGKKDPKAPGpLGDCIDCNLCV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  283 QVCPTGIDIRDGLQYECINCGACIDACDTTMERMGYDKGLISYTTEHRLSGKHTK-VMRPKLLGYGAVLLVMIGLFFAQV 361
Cdd:TIGR02745 241 QVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGLISYTSEAALEGRKKVrLLRPRTIGYAAVLAIVIGLLAIAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  362 AAVDPAGLSVIRDRNQLFRTNSSGEIENTYTLKVINKTQHIQTYKLDVSGLTDVSWYG-KQTVQVEPGEVLNLPMSLGVK 440
Cdd:TIGR02745 321 STREPMDLNVLRDRNLLYVRNSDGVVENTYTLKILNKTEQPHEYYLSVLGLPGIKIEGpGAPIHVKAGEKVKLPVFLRTP 400

                         410       420       430
                  ....*....|....*....|....*....|...
gi 520913022  441 PDNLSSPVA--TIQFILTDDSNQFTMQVESRFI 471
Cdd:TIGR02745 401 PDALKSGITsiEIRAYAEDDSEGIRVERESVFV 433
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
36-330 7.37e-85

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 261.92  E-value: 7.37e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  36 YVRESKGTYQKLRRYGGWFLLLLFGLVPWISYGDRQAILLDIGHQQFNFFGTTLypqDLTLLALLFMIAAFGLFFITTFL 115
Cdd:COG0348    3 YPRLVKGRFRRLRRLVQLLFLLLFLLGPWLRWLGDPAVLLDLAERRFYLFGLFW---DFYLLALLLIGAALALFLLTLLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 116 GRVWCGYLCPQTVWTFMYIWFEEKLeGSANKRRKQDGSKmtanlaMRKTAKH---IAWFAIALATGFTFVGYFVPVRDLV 192
Cdd:COG0348   80 GRVWCGWVCPQGVLTELFSWLERKL-GDRRLKLPWSLSK------ILRWLKYiilALWLLLALLTGLTFFGYFSPIGTLL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 193 IDFFTFNSTFWpvfWVMFFAVCTYGNAGWMRSIMCIHMCPYARFQSAMFDKDTFIVGYNTergeqrgprsrkadkkalgl 272
Cdd:COG0348  153 RLLLFGVLGLW---LLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDR-------------------- 209

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 273 GDCIDCDLCVQVCPTGIDIRDGL--QYECINCGACIDACDTTMermgydkglISYTTEHR 330
Cdd:COG0348  210 GDCIDCGLCVKVCPMGIDIRKGEinQSECINCGRCIDACPKDA---------IRFSSRGE 260
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 222-328 1.43e-53

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404610 [Multi-domain]  Cd Length: 114  Bit Score: 175.28  E-value: 1.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  222 MRSIMCIHMCPYARFQSAMFDKDTFIVGYNTERGEQRGPRSR-------KADKKALGLGDCIDCDLCVQVCPTGIDIRDG 294
Cdd:pfam13746   1 ARENFCIYACPYGRFQSVMYDEDTLTVVYDAVRGEGIYGRKPpkaglktKELRQQKGVGDCIDCESCVQVCPTGIDIRKG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 520913022  295 LQYECINCGACIDACDTTMERMGYDKGLISYTTE 328
Cdd:pfam13746  81 LQLECINCGLCIDACNTIMGKLGKPRGLIRYSSE 114
FixG_C pfam11614
IG-like fold at C-terminal of FixG, putative oxidoreductase; This domain is part of a ...
 361-471 1.64e-34

IG-like fold at C-terminal of FixG, putative oxidoreductase; This domain is part of a transmembrane protein, FixG, itself part of the FixGHIS operon closely associated with the FixNOPQ operon that is the symbiotically essential cbb3-type haem-copper oxidase complex. FixG expression is induced by oxygen-deprivation. This C-terminal domain adopts an E-set Ig-like fold.


Pssm-ID: 431960 [Multi-domain]  Cd Length: 116  Bit Score: 125.03  E-value: 1.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  361 VAAVDPAGLSVIRDRNQLFRTNSSGEIENTYTLKVINKTQHIQTYKLDVSGLTDVSWY-GKQTVQVEPGEVLNLPMSLGV 439
Cdd:pfam11614   3 LATREPLELDVLRDRGPLFVELSDGSIENVYTLKIINKTEEPRRYTLSVEGLPGLKLEgGPQEIEVAPGEVRTLPVFVTV 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 520913022  440 KPDNLSSPVATIQFILT-DDSNQFTMQVESRFI 471
Cdd:pfam11614  83 PPEAAKSGSTPITFTVTaDDDGGETVTEKSRFL 115
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 275-311 1.35e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 54.29  E-value: 1.35e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGLQY----ECINCGACIDACDT 311
Cdd:COG2221   17 CIGCGLCVAVCPTGaISLDDGKLVideeKCIGCGACIRVCPT 58
NapF COG1145
Ferredoxin [Energy production and conversion];
225-309 2.62e-09

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 57.81  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 225 IMCIHMCPYARFQSAMFDKDTFIVGYNTERGEQRGPRSRKADKKALGLGD---CIDCDLCVQVCPTG-IDIRDG------ 294
Cdd:COG1145  131 VLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDaekCIGCGLCVKVCPTGaIRLKDGkpqivv 210

                         90
                 ....*....|....*
gi 520913022 295 LQYECINCGACIDAC 309
Cdd:COG1145  211 DPDKCIGCGACVKVC 225
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
274-309 5.45e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 52.81  E-value: 5.45e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 520913022 274 DCIDCDLCVQVCPTG-IDIRDGLQY----ECINCGACIDAC 309
Cdd:COG2768   12 KCIGCGACVKVCPVGaISIEDGKAVidpeKCIGCGACIEVC 52
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 275-309 1.11e-08

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: 51.67  E-value: 1.11e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 520913022 275 CIDCDLCVQVCPTG----IDIRDGLQYE-----CINCGACIDAC 309
Cdd:COG1143    4 CIGCGLCVRVCPVDaitiEDGEPGKVYVidpdkCIGCGLCVEVC 47
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 275-309 1.75e-08

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 50.86  E-value: 1.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGL-------QYECINCGACIDAC 309
Cdd:COG1146   10 CIGCGACVEVCPVDvLELDEEGkkalvinPEECIGCGACELVC 52
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 251-315 2.84e-08

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: 50.82  E-value: 2.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520913022 251 NTERGEQRGPRSRK----ADKkalglgdCIDCDLCVQVCPTG-IDIRDGLQYE-----CINCGACIDACDT---TMER 315
Cdd:COG1144   11 GTAAYKTGGWRVERpvvdEDK-------CIGCGLCWIVCPDGaIRVDDGKYYGidydyCKGCGICAEVCPVkaiEMVP 81
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 275-309 3.13e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 50.50  E-value: 3.13e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGLQYE-----CINCGACIDAC 309
Cdd:COG1149   13 CIGCGLCVEVCPEGaIKLDDGGAPVvdpdlCTGCGACVGVC 53
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 256-311 3.23e-08

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: 52.01  E-value: 3.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520913022 256 EQRGPRSRKADKKALGLGD-CIDCDLCVQVCPTG-IDIRDGLQYE-----CINCGACIDACDT 311
Cdd:cd10549   60 TPEGKEYVPKEKEAEIDEEkCIGCGLCVKVCPVDaITLEDELEIVidkekCIGCGICAEVCPV 122
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 269-311 1.78e-07

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: 50.32  E-value: 1.78e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 520913022 269 ALGLGDCIDCDLCVQVCPTGI-----------DIRDGlqyECINCGACIDACDT 311
Cdd:cd10564    9 ALFLDLCTRCGDCVEACPEGIivrgdggfpelDFSRG---ECTFCGACAEACPE 59
Fer4_9 pfam13187
4Fe-4S dicluster domain;
274-309 2.16e-07

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 47.55  E-value: 2.16e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 520913022  274 DCIDCDLCVQVCPTGIDIRDGLQYE---------CINCGACIDAC 309
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVGQTirgdiaglaCIGCGACVDAC 45
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
275-311 2.90e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 52.72  E-value: 2.90e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGLQY----ECINCGACIDACDT 311
Cdd:COG4624   93 CKNCYPCVRACPVKaIKVDDGKAEideeKCISCGQCVAVCPF 134
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 275-309 5.11e-07

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 46.47  E-value: 5.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 520913022  275 CIDCDLCVQVCPTGIDIRDGLQ------------YECINCGACIDAC 309
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIVerlegeavrigvWKCIGCGACVEAC 55
napH_ TIGR02163
ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, ...
 96-309 6.29e-07

ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, found next to NapG,in operons that encode the periplasmic nitrate reductase. Some species with this reductase lack NapC but accomplish electron transfer to NapAB in some other manner, likely to involve NapH, NapG, and/or some other protein. A few members of this protein are designated MauN and are found in methylamine utilization operons in species that appear to lack a periplasmic nitrate reductase.


Pssm-ID: 274004 [Multi-domain]  Cd Length: 255  Bit Score: 50.43  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022   96 LLALLFMIAAFG-LFFITTFLGRVWCGYLCPQTVWTFMYIWFEEKLeGSANKRRkqdgskmtanlaMRKTAKHIAWFAI- 173
Cdd:TIGR02163  57 SPPTNALIGALIiVAFYALFGGRAFCSWVCPVNLVTDFAAWLRRKL-GINKIIK------------LPRNLRYWVLVLFl 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  174 --ALATGFTFVGYFVPV----RDLVidfFTFNSTFWPVFWVMFFAVCTYGNaGWmrsimCIHMCPYARFQSamfdkdtfI 247
Cdd:TIGR02163 124 llSFLSGLLIWEWFNPVgilhRGII---FGMGAGIWLILLVFLFDLLFSER-GW-----CGHLCPLGAFYG--------L 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520913022  248 VGyntergeQRGPRSRKADKKAlglgDCIDCDLCVQVCP-------TGIDIRDG--LQYECINCGACIDAC 309
Cdd:TIGR02163 187 IG-------RKSLIKIAASDRE----KCTNCMDCFNVCPepqvlrmPLKKGGSTlvLSGDCTLCGRCIDVC 246
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 275-309 1.21e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 46.19  E-value: 1.21e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGL----QYECINCGACIDAC 309
Cdd:COG4231   24 CTGCGACVKVCPADaIEEGDGKavidPDLCIGCGSCVQVC 63
Fer4_5 pfam12801
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 97-128 1.98e-06

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: 432796 [Multi-domain]  Cd Length: 48  Bit Score: 44.47  E-value: 1.98e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 520913022   97 LALLFMIAAFGLFFITTFLGRVWCGYLCPQTV 128
Cdd:pfam12801   1 LGPAGLILFLAVLVLTLLFGRVFCGWLCPFGA 32
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 275-309 2.30e-06

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: 44.44  E-value: 2.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 520913022  275 CIDCDLCVQVCPT------------GIDIRDGLQYECINCGACIDAC 309
Cdd:pfam12838   1 CIGCGACVAACPVgaitldevgekkGTKTVVIDPERCVGCGACVAVC 47
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 272-309 2.64e-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: 46.62  E-value: 2.64e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520913022 272 LGDCIDCDLCVQVCPTG-IDIRDGL-------------QYECINCGACIDAC 309
Cdd:cd10549   39 EDKCVFCGACVEVCPTGaIELTPEGkeyvpkekeaeidEEKCIGCGLCVKVC 90
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
227-311 5.26e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 48.01  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 227 CIHMCPYARFQSAMFDKDTFIVGYNTERGeqrgprsrKADKKALGLGdCIDCDLCVQVCPTG-IDIRDGLQY----ECIN 301
Cdd:PRK07118 176 CVKACPRNVIELIPKSARVFVACNSKDKG--------KAVKKVCEVG-CIGCGKCVKACPAGaITMENNLAVidqeKCTS 246

                         90
                 ....*....|
gi 520913022 302 CGACIDACDT 311
Cdd:PRK07118 247 CGKCVEKCPT 256
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 91-310 5.59e-06

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 47.97  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022  91 PQDLTLLALLFMIAAFGLFfittfLGRVWCGYLCPQTVWTFMYIWFeeklegsankRRKqdgskmtanLAMRKTAK---H 167
Cdd:PRK09477  65 PATVALIGALIITVFYALA-----GGRAFCSWVCPVNLVTDLANWL----------RRK---------LGLNQSATlprN 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 168 IAWFAIAL------ATGFTFVGYFVPV----RDLVidfFTFNSTFWPVFWVMFFAVCTYGNaGWmrsimCIHMCPYARFQ 237
Cdd:PRK09477 121 LRYWLLVLvlvgsaLTGTLAWEWINPVsmlhRGLV---FGFGSGWWLILAIFLFDLFVVEH-GW-----CGHLCPLGAFY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 238 SAMFDKDTFIVgyntergeqrgprsrkadkKALGLGDCIDCDLCVQVCP-------------TGIDIRDGlqyECINCGA 304
Cdd:PRK09477 192 GLIGKKSLIRV-------------------KAHDRQKCTRCMDCFHVCPepqvlrpplkgkqSPSQVTSG---DCITCGR 249


                 ....*.
gi 520913022 305 CIDACD 310
Cdd:PRK09477 250 CIDVCS 255
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 275-309 6.30e-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: 45.47  E-value: 6.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGLQYE---------CINCGACIDAC 309
Cdd:cd10549    8 CIGCGICVKACPTDaIELGPNGAIArgpeidedkCVFCGACVEVC 52
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
271-320 7.59e-06

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 46.03  E-value: 7.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520913022 271 GLGDCIDCDLCVQVCPTG-IDI---------RDGLQYE-----CINCGACIDAC--------------DTTMERMGYDK 320
Cdd:PRK05888  56 GEERCIACKLCAAICPADaITIeaaeredgrRRTTRYDinfgrCIFCGFCEEACptdaivetpdfelaTETREELIYDK 134
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 275-309 1.15e-05

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: 45.05  E-value: 1.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 520913022 275 CIDCD--LCVQVCPTGIDIR---DGLQY----ECINCGACIDAC 309
Cdd:cd10553   58 CFHCEnpWCVKACPTGAMQKrekDGIVYvdqeLCIGCKACIEAC 101
PRK13795 PRK13795
hypothetical protein; Provisional
 275-309 1.28e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 47.68  E-value: 1.28e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 520913022 275 CIDCDLCVQVCPTG-IDIRDGLQY------ECINCGACIDAC 309
Cdd:PRK13795 583 CVGCGVCVGACPTGaIRIEEGKRKisvdeeKCIHCGKCTEVC 624
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 275-325 2.17e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 43.67  E-value: 2.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 520913022 275 CIDCDLCVQVCPTGI-----DIRDGLQY--ECINCGACIDACDTTMERMGYDKGLISY 325
Cdd:PRK08348  44 CVGCRMCVTVCPAGVfvylpEIRKVALWtgRCVFCGQCVDVCPTGALQMSDDFLLASY 101
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 275-309 4.92e-05

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: 44.99  E-value: 4.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 520913022 275 CIDCDLCVQVCPTG-IDI-RDGL----QYECINCGACIDAC 309
Cdd:COG2878  139 CIGCGDCIKACPFDaIVGaAKGMhtvdEDKCTGCGLCVEAC 179
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 275-321 1.88e-04

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: 41.41  E-value: 1.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 520913022 275 CIDCD--LCVQVCPTG---IDIRDGL----QYECINCGACIDACDTTMERMGYDKG 321
Cdd:cd10550   49 CRQCEdaPCVEACPVGaisRDEETGAvvvdEDKCIGCGMCVEACPFGAIRVDPETG 104
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 276-315 2.15e-04

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: 41.47  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 520913022 276 IDCDLCVQVCPTG---IDIRDGLQY------ECINCGACIDACDTTMER 315
Cdd:cd16373  100 TDCGVCVEACPTEaiaIVLEDDVLRpvvdedKCVGCGLCEYVCPVEPPK 148
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 275-311 3.05e-04

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: 41.09  E-value: 3.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 520913022 275 CIDCDLCVQVCPTGI----DIRDGL------------QYeCI-NCGACIDACDT 311
Cdd:cd16373   16 CIRCGLCVEACPTGViqpaGLEDGLeggrtpyldpreGP-CDlCCDACVEVCPT 68
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 281-309 3.37e-04

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: 41.36  E-value: 3.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 520913022 281 CVQVCPTG-IDIR-DGL----QYECINCGACIDAC 309
Cdd:cd10551   61 CVKVCPTGaTYKReDGIvlvdYDKCIGCRYCMAAC 95
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 275-311 4.01e-04

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 40.50  E-value: 4.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 520913022 275 CIDCDLCVQVCP-TGIDIRD----GLQYE-CINCGACIDACDT 311
Cdd:PRK09625  61 CINCFNCWVYCPdAAILSRDkklkGVDYShCKGCGVCVEVCPT 103
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 275-313 4.17e-04

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


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 39.54  E-value: 4.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 520913022  275 CIDCDLCVQVCPTGIDIRDGLQY--------ECINCGACIDACDTTM 313
Cdd:TIGR00402  36 CTRCGECASACENNILQLGQQGQptvefdnaECDFCGKCAEACPTNA 82
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 274-311 5.82e-04

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: 39.63  E-value: 5.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 520913022 274 DCIDCDLCVQVCPTGIDIRDGLQYE---CINCGACIDACDT 311
Cdd:cd16372   78 LCVGCLMCVGFCPEGAMFKHEDYPEpfkCIACGICVKACPT 118
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 275-309 5.84e-04

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


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 38.06  E-value: 5.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 520913022  275 CIDCDLCVQVCPT--------GIDIRDGLQ----------------YECINCGACIDAC 309
Cdd:pfam13183   2 CIRCGACLAACPVylvtggrfPGDPRGGAAallgrlealeglaeglWLCTLCGACTEVC 60
PRK09898 PRK09898
ferredoxin-like protein;
275-311 8.00e-04

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 40.59  E-value: 8.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 520913022 275 CIDCDLCVQVCPTG---IDIRDGLQYECINCGACIDACDT 311
Cdd:PRK09898 156 CIGCSACTTACPWMmatVNTESKKSSKCVLCGECANACPT 195
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 274-309 9.26e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 41.00  E-value: 9.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 520913022 274 DCIDCDLCVQVCPTG-IDIRDGL---QYECINCGACIDAC 309
Cdd:NF038196 186 KCIGCGICAKVCPVNnIEMEDGKpvwGHNCTHCLACIHRC 225
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
270-309 9.32e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.07  E-value: 9.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 520913022 270 LGLGDCidcdlcVQVCPTG-IDIRDGL----QYECINCGACIDAC 309
Cdd:PRK07118 142 LGLGSC------VAACPFDaIHIENGLpvvdEDKCTGCGACVKAC 180
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
275-309 1.06e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 39.26  E-value: 1.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 520913022 275 CIDCDL--CVQVCPTG-IDIRDGLQY----ECINCGACIDAC 309
Cdd:COG1142   52 CRHCEDapCAEVCPVGaITRDDGAVVvdeeKCIGCGLCVLAC 93
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 274-311 1.11e-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: 39.78  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 520913022  274 DCIDCDLCVQVCPTgiDIRDG--------LQYECINCGACIDACDT 311
Cdd:TIGR01944 114 NCIGCTKCIQACPV--DAIVGaakamhtvIADECTGCDLCVEPCPT 157
ndhI CHL00014
NADH dehydrogenase subunit I
 275-332 1.26e-03

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 39.74  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520913022 275 CIDCDLCVQVCPT---------GIDIRDG--LQYE-----CINCGACIDACDTTmermgydkgLISYTTEHRLS 332
Cdd:CHL00014  61 CIACEVCVRVCPIdlpvvdwklETDIRKKrlLNYSidfgvCIFCGNCVEYCPTN---------CLSMTEEYELS 125
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 275-309 1.33e-03

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


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 38.91  E-value: 1.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 520913022 275 CIDCD--LCVQVCPTG--IDIRDGL----QYECINCGACIDAC 309
Cdd:cd04410   50 CMHCEdpPCVKACPTGaiYKDEDGIvlidEDKCIGCGSCVEAC 92
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
275-311 1.50e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.87  E-value: 1.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 520913022 275 CIDCDLCVQVCPTG-IDIRD----GLQYECINCG------ACIDACDT 311
Cdd:COG1142   83 CIGCGLCVLACPFGaITMVGeksrAVAVKCDLCGgreggpACVEACPT 130
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 217-311 1.56e-03

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: 39.31  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520913022 217 GNAGW-MRSIMCIHM----CPYARFQSAMFDKDTFIVGYNTERgeqrgprsrkadkkalglgdCIDCDLCVQVCPTGI-- 289
Cdd:cd16366   59 GDLSWlFRKDQCMHCtdagCLAACPTGAIIRTETGTVVVDPET--------------------CIGCGYCVNACPFDIpr 118

                         90       100       110
                 ....*....|....*....|....*....|..
gi 520913022 290 -DIRDGLQYECINC---------GACIDACDT 311
Cdd:cd16366  119 fDEETGRVAKCTLCydrisnglqPACVKTCPT 150
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 274-309 2.55e-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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 36.10  E-value: 2.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 520913022  274 DCIDCDLCVQVCP-TGID--IRDGLQY------ECINCGACIDAC 309
Cdd:pfam14697   7 TCIGCGKCYIACPdTSHQaiVGDGKRHhtviedECTGCNLCVSVC 51
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 227-289 3.11e-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: 35.58  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520913022  227 CIHMCPYARFqsaMFDkdtfivgyntERGEQRGprsrkADKKALGLGDCIDCDLCVQVCPTGI 289
Cdd:pfam12838   7 CVAACPVGAI---TLD----------EVGEKKG-----TKTVVIDPERCVGCGACVAVCPTGA 51
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 277-309 3.39e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 38.01  E-value: 3.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520913022 277 DCDLCVQVCPTG------IDIRD---GLQY----ECIN------CGACIDAC 309
Cdd:cd16373   58 CCDACVEVCPTGalrpldLEEQKvkmGVAVidkdRCLAwqggtdCGVCVEAC 109
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 275-309 3.73e-03

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 37.64  E-value: 3.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 520913022 275 CIDCD--LCVQVCPTG---IDIRDGLQYE---CINCGACIDAC 309
Cdd:cd16374   43 CRHCEdaPCMEVCPTGaiyRDEDGAVLVDpdkCIGCGMCAMAC 85
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 273-317 4.46e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.47  E-value: 4.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520913022 273 GDCIDCDLCVQVCPTG--IDIRDGLQYE-----CINCGACIDACDTTMERMG 317
Cdd:PRK12771 510 GNCFECDNCYGACPQDaiIKLGPGRRYHfdydkCTGCHICADVCPCGAIEMG 561
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 274-298 4.62e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 35.84  E-value: 4.62e-03
                         10        20
                 ....*....|....*....|....*.
gi 520913022 274 DCIDCDLCVQVCPTG-IDIRDGLQYE 298
Cdd:COG1146   41 ECIGCGACELVCPVGaITVEDDEPEE 66
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 272-288 6.72e-03

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: 35.11  E-value: 6.72e-03
                         10
                 ....*....|....*..
gi 520913022 272 LGDCIDCDLCVQVCPTG 288
Cdd:COG1143   34 PDKCIGCGLCVEVCPTG 50
 
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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