NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499658383|ref|WP_011339117|]
View 

electron transport complex subunit RsxC [Cereibacter sphaeroides]

Protein Classification

RnfC family protein( domain architecture ID 11468676)

RnfC family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 14-463 0e+00

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


:

Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 696.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  14 QFFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTSGRVI 93
Cdd:COG4656    2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVSAPVHAPVSGTVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  94 AVGhfAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKYDLHTLV 173
Cdd:COG4656   82 AIE--PAPHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDKKIDTLI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 174 INGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQRFDRALDiPLRVQVVPTQYPMGSE 253
Cdd:COG4656  160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDD-DIEVVVLPTKYPQGGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 254 KHLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVAHCGGY 333
Cdd:COG4656  239 KQLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 334 AEEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDTMPCIRCGRCAQACPVGLTPFELNARIQSEDLEGAG 413
Cdd:COG4656  319 KEEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVPPPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 499658383 414 RIGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAEAEGRRHQQEETKRL 463
Cdd:COG4656  399 EYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARER 448
 
Name Accession Description Interval E-value
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 14-463 0e+00

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


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 696.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  14 QFFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTSGRVI 93
Cdd:COG4656    2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVSAPVHAPVSGTVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  94 AVGhfAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKYDLHTLV 173
Cdd:COG4656   82 AIE--PAPHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDKKIDTLI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 174 INGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQRFDRALDiPLRVQVVPTQYPMGSE 253
Cdd:COG4656  160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDD-DIEVVVLPTKYPQGGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 254 KHLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVAHCGGY 333
Cdd:COG4656  239 KQLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 334 AEEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDTMPCIRCGRCAQACPVGLTPFELNARIQSEDLEGAG 413
Cdd:COG4656  319 KEEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVPPPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 499658383 414 RIGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAEAEGRRHQQEETKRL 463
Cdd:COG4656  399 EYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARER 448
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 15-449 0e+00

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


Pssm-ID: 273888 [Multi-domain]  Cd Length: 435  Bit Score: 685.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383   15 FFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTSGRVIA 94
Cdd:TIGR01945   1 LFTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFVSAPIHAPTSGTVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383   95 VGHFAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKYDLHTLVI 174
Cdd:TIGR01945  81 IEERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNPPPEKKIETLII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  175 NGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQRFDRALdiPLRVQVVPTQYPMGSEK 254
Cdd:TIGR01945 161 NGAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGGY--NIKVRVLPTKYPQGGEK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  255 HLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVAHCGGYA 334
Cdd:TIGR01945 239 QLIYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  335 EEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDTMPCIRCGRCAQACPVGLTPFELNARIQSEDLEGAGR 414
Cdd:TIGR01945 319 EKPERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPESPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEE 398

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 499658383  415 IGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAE 449
Cdd:TIGR01945 399 HNLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLRA 433
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 10-495 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 573.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  10 FRPSQFFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTS 89
Cdd:PRK05035   2 IRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMSLPVHAPTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  90 GRVIAVGHFAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKyDL 169
Cdd:PRK05035  82 GTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGD-KI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 170 HTLVINGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQR-FDRALDIplRVQVVPTQY 248
Cdd:PRK05035 161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAaLAGADDI--RVRVIPTKY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 249 PMGSEKHLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVA 328
Cdd:PRK05035 239 PSGGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 329 HCGGYAEEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDT-MPCIRCGRCAQACPVGLTPFELNARIQSE 407
Cdd:PRK05035 319 QAGFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPeQPCIRCGACADACPASLLPQQLYWFAKAE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 408 DLEGAGRIGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAEAEGRRHQQEETK-----RLaaarkareeaaaeakrQMM 482
Cdd:PRK05035 399 EHDKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKarfeaRQ----------------ARL 462

                        490
                 ....*....|...
gi 499658383 483 AKRKAEMEARKQR 495
Cdd:PRK05035 463 EREKAAREARHKK 475
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
142-288 2.50e-61

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 198.12  E-value: 2.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  142 VAEAGIVGMGGATFPSAVKLNLRAKYDLHTLVINGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNK 221
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPKKKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  222 AEAISAMQRF---DRALDIPLRVQVVPTQYPMGSEKHLVKILTGRETPARALTADLGVVVHNAATAHAVH 288
Cdd:pfam01512  81 PEAIAALEKAiaeARAAGFDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 381-443 1.51e-06

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 50.87  E-value: 1.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499658383 381 CIRCGRCAQACPVGLTPFELNARIQSEDLEGAgrIGLLD-CITCGCCSFTCPSNLPLVQTIHYA 443
Cdd:cd01916  367 CTDCGWCTRACPNSLRIKEAMEAAKEGDFSGL--ADLFDqCVGCGRCEQECPKEIPIINMIEKA 428
 
Name Accession Description Interval E-value
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 14-463 0e+00

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


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 696.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  14 QFFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTSGRVI 93
Cdd:COG4656    2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVSAPVHAPVSGTVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  94 AVGhfAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKYDLHTLV 173
Cdd:COG4656   82 AIE--PAPHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDKKIDTLI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 174 INGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQRFDRALDiPLRVQVVPTQYPMGSE 253
Cdd:COG4656  160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDD-DIEVVVLPTKYPQGGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 254 KHLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVAHCGGY 333
Cdd:COG4656  239 KQLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 334 AEEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDTMPCIRCGRCAQACPVGLTPFELNARIQSEDLEGAG 413
Cdd:COG4656  319 KEEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVPPPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 499658383 414 RIGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAEAEGRRHQQEETKRL 463
Cdd:COG4656  399 EYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARER 448
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 15-449 0e+00

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


Pssm-ID: 273888 [Multi-domain]  Cd Length: 435  Bit Score: 685.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383   15 FFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTSGRVIA 94
Cdd:TIGR01945   1 LFTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFVSAPIHAPTSGTVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383   95 VGHFAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKYDLHTLVI 174
Cdd:TIGR01945  81 IEERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNPPPEKKIETLII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  175 NGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQRFDRALdiPLRVQVVPTQYPMGSEK 254
Cdd:TIGR01945 161 NGAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGGY--NIKVRVLPTKYPQGGEK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  255 HLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVAHCGGYA 334
Cdd:TIGR01945 239 QLIYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  335 EEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDTMPCIRCGRCAQACPVGLTPFELNARIQSEDLEGAGR 414
Cdd:TIGR01945 319 EKPERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPESPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEE 398

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 499658383  415 IGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAE 449
Cdd:TIGR01945 399 HNLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLRA 433
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 10-495 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 573.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  10 FRPSQFFGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTS 89
Cdd:PRK05035   2 IRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMSLPVHAPTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  90 GRVIAVGHFAAPHPSGLPIPTITIRTDGQDSWGPRLGRLRPENATPEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKyDL 169
Cdd:PRK05035  82 GTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGD-KI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 170 HTLVINGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNKAEAISAMQR-FDRALDIplRVQVVPTQY 248
Cdd:PRK05035 161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAaLAGADDI--RVRVIPTKY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 249 PMGSEKHLVKILTGRETPARALTADLGVVVHNAATAHAVHLAVRYGEPLLSRVVTVSGRAVRRPANVRVLIGTPVSEVVA 328
Cdd:PRK05035 239 PSGGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 329 HCGGYAEEPDRLLLGGPMMGQPIQNLRVPVVKGTSGILALTRAETPGVDT-MPCIRCGRCAQACPVGLTPFELNARIQSE 407
Cdd:PRK05035 319 QAGFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPeQPCIRCGACADACPASLLPQQLYWFAKAE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 408 DLEGAGRIGLLDCITCGCCSFTCPSNLPLVQTIHYAKGKLAEAEGRRHQQEETK-----RLaaarkareeaaaeakrQMM 482
Cdd:PRK05035 399 EHDKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKarfeaRQ----------------ARL 462

                        490
                 ....*....|...
gi 499658383 483 AKRKAEMEARKQR 495
Cdd:PRK05035 463 EREKAAREARHKK 475
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
142-288 2.50e-61

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 198.12  E-value: 2.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  142 VAEAGIVGMGGATFPSAVKLNLRAKYDLHTLVINGAECEPYLTCDDRLMRERAEEIADGVGIMARALGVTQIVVAIESNK 221
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPKKKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  222 AEAISAMQRF---DRALDIPLRVQVVPTQYPMGSEKHLVKILTGRETPARALTADLGVVVHNAATAHAVH 288
Cdd:pfam01512  81 PEAIAALEKAiaeARAAGFDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
RnfC_N pfam13375
RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid ...
 16-118 1.13e-41

RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid superfamily. It is found at the N-terminus of the RnfC Electron transport complex protein. It appears to be most related to the N-terminal NQRA domain (pfam05896).


Pssm-ID: 433157 [Multi-domain]  Cd Length: 101  Bit Score: 144.62  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383   16 FGIRGGVHPETRKHLSSESPIEDMPIPTLIRVPLQQHIGAEAEPLVRRDDLVVKGQLIGRARGPVSANIHAPTSGRVIAV 95
Cdd:pfam13375   1 WTFKGGIHPPENKELSKDKPIEKLPLPKELVIPLSQHIGAPAEPIVKVGDRVLKGQKIAEADGFVSAPVHASVSGTVKAI 80

                          90       100
                  ....*....|....*....|...
gi 499658383   96 GHFAAPHPSGLpiPTITIRTDGQ 118
Cdd:pfam13375  81 EPRPVPHGSGV--NCIVIENDGE 101
SLBB pfam10531
SLBB domain;
301-348 1.87e-10

SLBB domain;


Pssm-ID: 463136 [Multi-domain]  Cd Length: 56  Bit Score: 56.13  E-value: 1.87e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499658383  301 VVTVSGrAVRRPANVRVLIGTPVSEVVAHCGGYAEEPDR-------LLLGGPMMG 348
Cdd:pfam10531   1 VVTVTG-EVKRPGNYEVPIGTTLSDLIELAGGFTDDADLdinlrrlKRPGGPMMG 54
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 381-431 5.65e-10

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: 54.95  E-value: 5.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499658383  381 CIRCGRCAQACPVGLTPfelNARIQSEDLEGAGRIGLLDCITCGCCSFTCP 431
Cdd:pfam13237   9 CIGCGRCTAACPAGLTR---VGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 381-434 7.51e-09

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: 51.93  E-value: 7.51e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499658383  381 CIRCGRCAQACPV---------GLTPFELNARIQSEDLEGAGRIGLLDCITCGCCSFTCPSNL 434
Cdd:pfam13183   2 CIRCGACLAACPVylvtggrfpGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 381-435 3.89e-08

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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 49.77  E-value: 3.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383  381 CIRCGRCAQACPV----GLTPFELNARIQSEDLEGA-GRIGLLDCITCGCCSFTCPSNLP 435
Cdd:pfam13534   2 CIQCGCCVDECPRyllnGDEPKKLMRAAYLGDLEELqANKVANLCSECGLCEYACPMGLD 61
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 381-433 1.02e-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: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 48.29  E-value: 1.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499658383  381 CIRCGRCAQACPVGLTPFElnaRIQSEDLEGAGRIGLLDCITCGCCSFTCPSN 433
Cdd:pfam12838   1 CIGCGACVAACPVGAITLD---EVGEKKGTKTVVIDPERCVGCGACVAVCPTG 50
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 381-433 4.66e-07

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: 47.05  E-value: 4.66e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499658383 381 CIRCGRCAQACPVgltpfelNA-RIQSEDLEGAGRIGLLDCITCGCCSFTCPSN 433
Cdd:COG1143    4 CIGCGLCVRVCPV-------DAiTIEDGEPGKVYVIDPDKCIGCGLCVEVCPTG 50
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 376-433 7.07e-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: 46.64  E-value: 7.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499658383 376 VDTMPCIRCGRCAQACPVG-LTPFELNARIQSEDLegagriglldCITCGCCSFTCPSN 433
Cdd:COG1149    8 IDEEKCIGCGLCVEVCPEGaIKLDDGGAPVVDPDL----------CTGCGACVGVCPTG 56
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
381-433 1.10e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 50.06  E-value: 1.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499658383 381 CIRCGRCAQACPVGLTPFElnariqsedlegaGRIGLLDCITCGCCSFTCPSN 433
Cdd:COG0348  212 CIDCGLCVKVCPMGIDIRK-------------GEINQSECINCGRCIDACPKD 251
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 381-443 1.51e-06

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 50.87  E-value: 1.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499658383 381 CIRCGRCAQACPVGLTPFELNARIQSEDLEGAgrIGLLD-CITCGCCSFTCPSNLPLVQTIHYA 443
Cdd:cd01916  367 CTDCGWCTRACPNSLRIKEAMEAAKEGDFSGL--ADLFDqCVGCGRCEQECPKEIPIINMIEKA 428
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
374-431 1.60e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.88  E-value: 1.60e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499658383 374 PGVDTMPCIRCGRCAQACPVG-LTPFELNARIQSEdlegagrigllDCITCGCCSFTCP 431
Cdd:COG2768    6 PYVDEEKCIGCGACVKVCPVGaISIEDGKAVIDPE-----------KCIGCGACIEVCP 53
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 381-451 3.13e-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: 3.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499658383 381 CIRCGRCAQACPVG---LTPFELNARIQSEDLEgagrigllDCITCGCCSFTCPSN-LPLVQTIHYAKGKLAEAE 451
Cdd:cd10549    8 CIGCGICVKACPTDaieLGPNGAIARGPEIDED--------KCVFCGACVEVCPTGaIELTPEGKEYVPKEKEAE 74
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 381-449 4.56e-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: 45.85  E-value: 4.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499658383 381 CIRCGRCAQACPVG---LTPFELNARIQSEDLEgagrIGLLDCITCGCCSFTCPsnlplVQTIHYAKGKLAE 449
Cdd:cd10549   42 CVFCGACVEVCPTGaieLTPEGKEYVPKEKEAE----IDEEKCIGCGLCVKVCP-----VDAITLEDELEIV 104
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 374-431 7.79e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 43.54  E-value: 7.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499658383 374 PGVDTMPCIRCGRCAQACPVG---LTPFELNARIQSEDlegagrigllDCITCGCCSFTCP 431
Cdd:COG1146    3 PVIDTDKCIGCGACVEVCPVDvleLDEEGKKALVINPE----------ECIGCGACELVCP 53
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 376-433 9.13e-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: 9.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 376 VDTMPCIRCGRCAQACPVG--LTPFELNARIQSEdlegagrigllDCITCGCCSFTCPSN 433
Cdd:cd10549   75 IDEEKCIGCGLCVKVCPVDaiTLEDELEIVIDKE-----------KCIGCGICAEVCPVN 123
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 381-462 9.26e-06

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 48.15  E-value: 9.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 381 CIRCGRCAQACPV-GLTPFELN---ARIQ--SEDLEGAGRIGL-------LD-CITCGCCSFTCPSNLPLVQTIhyakgk 446
Cdd:COG0247   80 CVGCGFCRAMCPSyKATGDEKDsprGRINllREVLEGELPLDLseevyevLDlCLTCKACETACPSGVDIADLI------ 153

                         90
                 ....*....|....*.
gi 499658383 447 laeAEGRRHQQEETKR 462
Cdd:COG0247  154 ---AEARAQLVERGGR 166
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 367-431 1.96e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 42.35  E-value: 1.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499658383 367 ALTRAETPGVDTMPCIRCGRCAQACPVG-LTPFELNARIQSEdlegagrigllDCITCGCCSFTCP 431
Cdd:COG2221    3 GIIGTWPPKIDEEKCIGCGLCVAVCPTGaISLDDGKLVIDEE-----------KCIGCGACIRVCP 57
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
381-433 2.03e-05

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 42.48  E-value: 2.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499658383  381 CIRCGRCAQACPVG---LTPFELNAR-------IQSEDLEGAGRIGLL--DCITCGCCSFTCPSN 433
Cdd:pfam13484   1 CGSCGKCIDACPTGaivGPEGVLDARrcisyltIEKKGLIPDELRCLLgnRCYGCDICQDVCPWN 65
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 369-433 3.88e-05

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: 41.96  E-value: 3.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499658383 369 TRAETPGVDTMPCIRCGRCAQACPVGltpfelnaRIQSEDlEGAGRIGLLDCITCGCCSFTCPSN 433
Cdd:COG1144   20 WRVERPVVDEDKCIGCGLCWIVCPDG--------AIRVDD-GKYYGIDYDYCKGCGICAEVCPVK 75
NapF COG1145
Ferredoxin [Energy production and conversion];
376-433 4.35e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 45.10  E-value: 4.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 376 VDTMPCIRCGRCAQACPVG-LTPFELNARIQ-SEDlegagrigllDCITCGCCSFTCPSN 433
Cdd:COG1145  179 IDAEKCIGCGLCVKVCPTGaIRLKDGKPQIVvDPD----------KCIGCGACVKVCPVG 228
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 381-424 6.07e-05

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 43.87  E-value: 6.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 499658383 381 CIRCGRCAQACPVG---LTP-FELnARIQSEDLEGAGRIGLLDCITCG 424
Cdd:PRK12387  75 CIFCGRCEEVCPTAaikLSQeFEL-AVWKKEDLLQQSEFALCNCRVCG 121
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 376-433 6.38e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 41.18  E-value: 6.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499658383 376 VDTMPCIRCGRCAQACPVGLtpFELNariqsedlEGAGRIGLLDCITCGCCSFTCPSN 433
Cdd:COG4231   19 IDEDKCTGCGACVKVCPADA--IEEG--------DGKAVIDPDLCIGCGSCVQVCPVD 66
NuoF COG1894
NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and ...
 134-236 6.41e-05

NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and conversion]; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 441498 [Multi-domain]  Cd Length: 418  Bit Score: 45.39  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 134 TPEEIAAKVAEAGIVGMGGATFPSAVKLNL--RAKYDLHTLVINGAECEPYlTCDDR-LMReraeeiAD------GVGIM 204
Cdd:COG1894   39 TPEEVIEEVKDSGLRGRGGAGFPTGLKWSFvpKAPGDPKYLVCNADEGEPG-TFKDRsLLE------GDphqlieGMIIA 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499658383 205 ARALGVTQIVVAIesnKAEAISAMQRFDRALD 236
Cdd:COG1894  112 AYAIGATKGYIYI---RGEYPLAIERLEKAIE 140
PRK09898 PRK09898
ferredoxin-like protein;
367-432 1.46e-04

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 43.29  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499658383 367 ALTRAETPG---VDTMPCIRCGRCAQACPVGLtpfelnARIQSEDLEGAgrigllDCITCGCCSFTCPS 432
Cdd:PRK09898 139 AITWQQKEGcitVDHKRCIGCSACTTACPWMM------ATVNTESKKSS------KCVLCGECANACPT 195
Fer4_9 pfam13187
4Fe-4S dicluster domain;
381-433 2.49e-04

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 38.69  E-value: 2.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499658383  381 CIRCGRCAQACPVGLTpfelnaRIQSEDLEGAGRIGLLDCITCGCCSFTCPSN 433
Cdd:pfam13187   2 CTGCGACVAACPAGAI------VPDLVGQTIRGDIAGLACIGCGACVDACPRG 48
PLN03132 PLN03132
NADH dehydrogenase (ubiquinone) flavoprotein 1; Provisional
 135-341 4.19e-04

NADH dehydrogenase (ubiquinone) flavoprotein 1; Provisional


Pssm-ID: 178678 [Multi-domain]  Cd Length: 461  Bit Score: 42.94  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 135 PEEIAAKVAEAGIVGMGGATFPSAVKLNLRAKYD---LHTLVINGAECEPYlTCDDR-LMRERAEEIAD-----GVGIMA 205
Cdd:PLN03132  71 PDWIVNEMKKSGLRGRGGAGFPSGLKWSFMPKVSdgrPSYLVVNADESEPG-TCKDReIMRHDPHKLLEgcliaGVGMRA 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 206 RALGV------TQIVVAIESNKAEAISAMQRFDRA----LDIPLRVQVVPTQYPMGSEKHLVKILTGRETPAR---ALTA 272
Cdd:PLN03132 150 RAAYIyirgeyVNERLNLERARHEAYAAGLLGKNAcgsgYDFDVYIHYGAGAYICGEETALLESLEGKQGKPRlkpPFPA 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 273 DLGV-----VVHNAATAHAVHLAVRYGEPLLS----------RVVTVSGRaVRRPANVRVLIGTPVSEVVA-HCGGYAEE 336
Cdd:PLN03132 230 NVGLygcptTVTNVETVAVSPTILRRGPEWFAsfgrknnagtKLFCISGH-VNKPCTVEEEMSIPLKELIErHCGGVRGG 308


                 ....*
gi 499658383 337 PDRLL 341
Cdd:PLN03132 309 WDNLL 313
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 366-433 4.64e-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: 40.01  E-value: 4.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499658383 366 LALTRAeTPGV---DTMPCIRCGRCAQACPVGltpfelnARIQSEDLEGAGRiglldCITCGCCSFTCPSN 433
Cdd:cd16372   62 GAITRD-ANGVvmiNKKLCVGCLMCVGFCPEG-------AMFKHEDYPEPFK-----CIACGICVKACPTG 119
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
381-444 5.88e-04

Heterodisulfide reductase, subunit C [Energy production and conversion];


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 38.73  E-value: 5.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499658383 381 CIRCGRCAQACPVG----LTPFELNARIQSEDLEGA-GRIGLLDCITCGCCSFTCPSNLPLVQTIHYAK 444
Cdd:COG1150    5 CYQCGTCTASCPVAramdYNPRKIIRLAQLGLKEEVlKSDSIWLCVSCYTCTERCPRGIDIADVMDALR 73
PTZ00304 PTZ00304
NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional
 132-209 7.96e-04

NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional


Pssm-ID: 185547 [Multi-domain]  Cd Length: 461  Bit Score: 42.08  E-value: 7.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658383 132 NATPEEIAAKVAEAGIVGMGGATFPSAVKLNL--------RAKYdlhtLVINGAECEPYlTCDDR-LMRERAEEIADGVG 202
Cdd:PTZ00304  57 LKGHDWIIDEIKKSGLRGRGGAGFPSGLKWSFmpkvkpdgRPSY----LVVNADESEPG-TCKDReIMRHDPHKLVEGAL 131


                 ....*..
gi 499658383 203 IMARALG 209
Cdd:PTZ00304 132 LAGFAMR 138
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 376-407 1.58e-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: 37.03  E-value: 1.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 499658383 376 VDTMPCIRCGRCAQACPVG---LTPFELNARIQSE 407
Cdd:COG1143   32 IDPDKCIGCGLCVEVCPTGaisMTPFELAVEDREE 66
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
367-394 2.44e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.48  E-value: 2.44e-03
                         10        20
                 ....*....|....*....|....*....
gi 499658383 367 ALTRAE-TPGVDTMPCIRCGRCAQACPVG 394
Cdd:COG1142   68 AITRDDgAVVVDEEKCIGCGLCVLACPFG 96
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 367-431 2.68e-03

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 38.02  E-value: 2.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499658383 367 ALTRAETPGV--DTMPCIRCGRCAQACPVGLtpfelnarIQSEDLEGAGRIglldCITCGCCSFTCP 431
Cdd:cd16370   69 ALEPRKGGGVvlDKEKCIGCGNCVKACIVGA--------IFWDEETNKPII----CIHCGYCARYCP 123
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
381-433 2.83e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 40.01  E-value: 2.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499658383 381 CIRCGRCAQACPVG-LTPFELNARIQSEdlegagrigllDCITCGCCSFTCPSN 433
Cdd:COG4624   93 CKNCYPCVRACPVKaIKVDDGKAEIDEE-----------KCISCGQCVAVCPFG 135
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 376-394 2.87e-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: 35.30  E-value: 2.87e-03
                          10
                  ....*....|....*....
gi 499658383  376 VDTMPCIRCGRCAQACPVG 394
Cdd:pfam00037   3 IDEEKCIGCGACVEVCPVG 21
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 403-432 4.29e-03

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 39.01  E-value: 4.29e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499658383 403 RIQS-EDLEgagRI-GLLDCITCGCCSFTCPS 432
Cdd:PRK05950 127 RLQSpEDRE---KLdGLYECILCACCSTSCPS 155
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
373-433 5.13e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.46  E-value: 5.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499658383 373 TPGVDTMPCIRCGRCAQACPVGltpfelnarIQSEDLEGAGRIGLLDCITCGCCSFTCPSN 433
Cdd:COG1148  490 VAEVDPEKCTGCGRCVEVCPYG---------AISIDEKGVAEVNPALCKGCGTCAAACPSG 541
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
364-431 7.49e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.55  E-value: 7.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499658383 364 GILALTRAETPGVDtmpCIRCGRCAQACPVgltpfelNA-RIQSEDLEGAGR------IGLLDCITCGCCSFTCP 431
Cdd:PRK05888  46 GRHALRRDPNGEER---CIACKLCAAICPA-------DAiTIEAAEREDGRRrttrydINFGRCIFCGFCEEACP 110
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 376-393 7.68e-03

4Fe-4S binding domain; This 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: 463711 [Multi-domain]  Cd Length: 22  Bit Score: 33.91  E-value: 7.68e-03
                          10
                  ....*....|....*...
gi 499658383  376 VDTMPCIRCGRCAQACPV 393
Cdd:pfam12797   5 IDADKCIGCGACVSACPA 22
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 381-430 9.00e-03

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: 36.22  E-value: 9.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499658383  381 CIRCGRCAQACPVGLtpfelnariqseDLegagRIGL-LDCITCGCCSFTC 430
Cdd:pfam13746  61 CIDCESCVQVCPTGI------------DI----RKGLqLECINCGLCIDAC 95
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH