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Conserved domains on  [gi|15831592|ref|NP_310365|]
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electron transport complex subunit C [Escherichia coli O157:H7 str. Sakai]

Protein Classification

electron transport complex subunit RsxC( domain architecture ID 11480330)

electron transport complex subunit RsxC is part of a membrane complex involved in electron transport and is required to maintain the reduced state of SoxR

EC:  7.-.-.-
Gene Ontology:  GO:0051539|GO:0009055|GO:0046872|GO:0016020
PubMed:  12773378|9154934

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-702 0e+00

electron transport complex protein RnfC; Provisional


:

Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 1060.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    7 AFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPT 85
Cdd:PRK05035   1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMsLPVHAPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   86 SGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKI 165
Cdd:PRK05035  81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  166 ETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSHDISMRVIPTKYPS 245
Cdd:PRK05035 161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  246 GGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDA 325
Cdd:PRK05035 241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  326 GFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQH 405
Cdd:PRK05035 321 GFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  406 DKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQP 485
Cdd:PRK05035 401 DKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEAR 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  486 AAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDAatvtDPRKTAVEAAIAR 565
Cdd:PRK05035 481 AAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKAAVAAAIAR 556

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  566 AKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQ---VDPRKAAVEAAIARAKARKLEQQQAnA 642
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQvaeVDPKKAAVAAAIARAKAKKAEQQAN-A 635

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  643 EPEEPVDPRKAAVEAAIARAKARKLEQQQANAEPEEPVDPRKAAVEAAITRAKARKLEQQ 702
Cdd:PRK05035 636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
 
Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-702 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 1060.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    7 AFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPT 85
Cdd:PRK05035   1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMsLPVHAPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   86 SGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKI 165
Cdd:PRK05035  81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  166 ETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSHDISMRVIPTKYPS 245
Cdd:PRK05035 161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  246 GGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDA 325
Cdd:PRK05035 241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  326 GFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQH 405
Cdd:PRK05035 321 GFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  406 DKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQP 485
Cdd:PRK05035 401 DKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEAR 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  486 AAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDAatvtDPRKTAVEAAIAR 565
Cdd:PRK05035 481 AAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKAAVAAAIAR 556

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  566 AKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQ---VDPRKAAVEAAIARAKARKLEQQQAnA 642
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQvaeVDPKKAAVAAAIARAKAKKAEQQAN-A 635

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  643 EPEEPVDPRKAAVEAAIARAKARKLEQQQANAEPEEPVDPRKAAVEAAITRAKARKLEQQ 702
Cdd:PRK05035 636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 12-462 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: 776.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  12 KIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPTSGTVT 90
Cdd:COG4656   2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVsAPVHAPVSGTVV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  91 AIAPHstAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLI 169
Cdd:COG4656  82 AIEPA--PHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDkKIDTLI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 170 INAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSHDISMRVIPTKYPSGGAK 249
Cdd:COG4656 160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDDIEVVVLPTKYPQGGEK 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 250 QLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCP 329
Cdd:COG4656 240 QLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGFK 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 330 SADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGePQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKAT 409
Cdd:COG4656 320 EEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVP-PPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831592 410 THNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEA 462
Cdd:COG4656 399 EYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARERFEA 451
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 14-447 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: 642.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    14 WDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGK-MLPVHAPTSGTVTAI 92
Cdd:TIGR01945   2 FTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFvSAPIHAPTSGTVVAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    93 APHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIIN 171
Cdd:TIGR01945  82 EERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNPPPEkKIETLIIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   172 AAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADShDISMRVIPTKYPSGGAKQL 251
Cdd:TIGR01945 162 GAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGGY-NIKVRVLPTKYPQGGEKQL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   252 TYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCPSA 331
Cdd:TIGR01945 241 IYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFREK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   332 DQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEpQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTH 411
Cdd:TIGR01945 321 PERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPE-SPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEEH 399

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 15831592   412 NIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIR 447
Cdd:TIGR01945 400 NLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLRAKK 435
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
139-283 3.42e-57

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 191.96  E-value: 3.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   139 IHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNK 217
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPKkKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   218 PQAISMLRAVLADS----HDISMRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVK 283
Cdd:pfam01512  81 PEAIAALEKAIAEAraagFDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 376-429 5.20e-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: 46.24  E-value: 5.20e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831592 376 SCIRCSACADACPADLLPQQLYwFSKGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:cd10549  41 KCVFCGACVEVCPTGAIELTPE-GKEYVPKEKEAEIDEEKCIGCGLCVKVCPVD 93
 
Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-702 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 1060.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    7 AFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPT 85
Cdd:PRK05035   1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMsLPVHAPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   86 SGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKI 165
Cdd:PRK05035  81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  166 ETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSHDISMRVIPTKYPS 245
Cdd:PRK05035 161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  246 GGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDA 325
Cdd:PRK05035 241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  326 GFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQH 405
Cdd:PRK05035 321 GFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  406 DKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQP 485
Cdd:PRK05035 401 DKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEAR 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  486 AAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDAatvtDPRKTAVEAAIAR 565
Cdd:PRK05035 481 AAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKAAVAAAIAR 556

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  566 AKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQ---VDPRKAAVEAAIARAKARKLEQQQAnA 642
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQvaeVDPKKAAVAAAIARAKAKKAEQQAN-A 635

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  643 EPEEPVDPRKAAVEAAIARAKARKLEQQQANAEPEEPVDPRKAAVEAAITRAKARKLEQQ 702
Cdd:PRK05035 636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 12-462 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: 776.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  12 KIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPTSGTVT 90
Cdd:COG4656   2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVsAPVHAPVSGTVV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  91 AIAPHstAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLI 169
Cdd:COG4656  82 AIEPA--PHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDkKIDTLI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 170 INAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSHDISMRVIPTKYPSGGAK 249
Cdd:COG4656 160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDDIEVVVLPTKYPQGGEK 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 250 QLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCP 329
Cdd:COG4656 240 QLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGFK 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 330 SADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGePQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKAT 409
Cdd:COG4656 320 EEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVP-PPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831592 410 THNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEA 462
Cdd:COG4656 399 EYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARERFEA 451
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 14-447 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: 642.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    14 WDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGK-MLPVHAPTSGTVTAI 92
Cdd:TIGR01945   2 FTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFvSAPIHAPTSGTVVAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    93 APHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIIN 171
Cdd:TIGR01945  82 EERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNPPPEkKIETLIIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   172 AAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADShDISMRVIPTKYPSGGAKQL 251
Cdd:TIGR01945 162 GAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGGY-NIKVRVLPTKYPQGGEKQL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   252 TYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCPSA 331
Cdd:TIGR01945 241 IYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFREK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   332 DQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEpQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTH 411
Cdd:TIGR01945 321 PERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPE-SPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEEH 399

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 15831592   412 NIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIR 447
Cdd:TIGR01945 400 NLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLRAKK 435
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
139-283 3.42e-57

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 191.96  E-value: 3.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   139 IHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNK 217
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPKkKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   218 PQAISMLRAVLADS----HDISMRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVK 283
Cdd:pfam01512  81 PEAIAALEKAIAEAraagFDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
RnfC_N pfam13375
RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid ...
 14-115 1.43e-39

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: 141.15  E-value: 1.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592    14 WDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRG-KMLPVHAPTSGTVTAI 92
Cdd:pfam13375   1 WTFKGGIHPPENKELSKDKPIEKLPLPKELVIPLSQHIGAPAEPIVKVGDRVLKGQKIAEADGfVSAPVHASVSGTVKAI 80

                          90       100
                  ....*....|....*....|...
gi 15831592    93 APHSTAHPSALaeLSVIIDADGE 115
Cdd:pfam13375  81 EPRPVPHGSGV--NCIVIENDGE 101
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 377-430 1.32e-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: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 54.45  E-value: 1.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15831592   377 CIRCSACADACPADLLPQQLYWFSKGQqhdKATTHNIADCIECGACAWVCPSNI 430
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGT---KTVVIDPERCVGCGACVAVCPTGA 51
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 377-431 2.87e-09

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: 53.62  E-value: 2.87e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   377 CIRCSACADACPADLL----PQQL-YWFSKGQQHDKATTHNIADCIECGACAWVCPSNIP 431
Cdd:pfam13534   2 CIQCGCCVDECPRYLLngdePKKLmRAAYLGDLEELQANKVANLCSECGLCEYACPMGLD 61
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 374-427 9.22e-09

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 52.40  E-value: 9.22e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831592 374 EQSCIRCSACADACPADLlpqqlywFSKGQQHDKATTHNIADCIECGACAWVCP 427
Cdd:COG1146   7 TDKCIGCGACVEVCPVDV-------LELDEEGKKALVINPEECIGCGACELVCP 53
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 377-430 4.43e-08

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: 50.39  E-value: 4.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831592   377 CIRCSACADACPAdLLPQQLYWFSK------GQQHDKATTHNIAD----CIECGACAWVCPSNI 430
Cdd:pfam13183   2 CIRCGACLAACPV-YLVTGGRFPGDprggaaALLGRLEALEGLAEglwlCTLCGACTEVCPVGI 64
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 377-427 6.37e-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: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 49.56  E-value: 6.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15831592   377 CIRCSACADACPADLLPQQLYWFSKGqqhDKATTHNIADCIECGACAWVCP 427
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIVERLE---GEAVRIGVWKCIGCGACVEACP 56
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 371-429 3.04e-07

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 49.72  E-value: 3.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831592   371 PQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:TIGR01971  39 PNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEINFGRCIFCGLCEEACPTD 97
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 377-429 3.76e-07

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 48.12  E-value: 3.76e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831592 377 CIRCSACADACPADLlpqqlywFSKGqqhDKATTHNIADCIECGACAWVCPSN 429
Cdd:COG4231  24 CTGCGACVKVCPADA-------IEEG---DGKAVIDPDLCIGCGSCVQVCPVD 66
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 377-429 4.72e-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: 47.43  E-value: 4.72e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15831592 377 CIRCSACADACPADLLpqqlywfsKGQQHDKATTHNI--ADCIECGACAWVCPSN 429
Cdd:COG1143   4 CIGCGLCVRVCPVDAI--------TIEDGEPGKVYVIdpDKCIGCGLCVEVCPTG 50
NapF COG1145
Ferredoxin [Energy production and conversion];
324-429 9.51e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.88  E-value: 9.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 324 DAGFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQ-EEQSCIRCSACADACPADLLpqqlywfsKG 402
Cdd:COG1145 130 EVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAViDAEKCIGCGLCVKVCPTGAI--------RL 201

                        90       100
                ....*....|....*....|....*..
gi 15831592 403 QQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:COG1145 202 KDGKPQIVVDPDKCIGCGACVKVCPVG 228
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 377-455 1.13e-06

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: 1.13e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831592 377 CIRCSACADACPADLLpqqlywfskGQQHDKATTHNIADCIECGACAWVCPSNiplvqyfrqekaeiaAIRQEEKRAAE 455
Cdd:COG1149  13 CIGCGLCVEVCPEGAI---------KLDDGGAPVVDPDLCTGCGACVGVCPTG---------------AITLEEREAGK 67
SLBB pfam10531
SLBB domain;
296-344 1.29e-06

SLBB domain;


Pssm-ID: 463136 [Multi-domain]  Cd Length: 56  Bit Score: 46.12  E-value: 1.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831592   296 VVTLTGEaIARPGNVWARLGTPVRHLLNDA-GFCPSADQMVI------MGGPLMGF 344
Cdd:pfam10531   1 VVTVTGE-VKRPGNYEVPIGTTLSDLIELAgGFTDDADLDINlrrlkrPGGPMMGI 55
PRK06991 PRK06991
electron transport complex subunit RsxB;
373-551 1.41e-06

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 50.56  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  373 EEQSCIRCSACADACPADLL---PQQLYWFskgqqhdkatthnIAD-CIECGACAWVCPSN-IPLVQYFRqEKAEIAAIR 447
Cdd:PRK06991  83 DEQLCIGCTLCMQACPVDAIvgaPKQMHTV-------------LADlCTGCDLCVPPCPVDcIDMVPVTG-ERTGWDAWS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  448 QEekRAAEAKARFEARLARLEREKAARlERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQPIVIKAgerpdnsAIIAA 527
Cdd:PRK06991 149 QA--QADAARARHDARQARLRREREAA-EARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAIIAA-------ALERA 218

                        170       180
                 ....*....|....*....|....
gi 15831592  528 REARKAQARAKQAELQQTNDAATV 551
Cdd:PRK06991 219 RKKKEELAAQGAGPKNTEGVSAAV 242
Fer4_9 pfam13187
4Fe-4S dicluster domain;
377-430 2.85e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 44.85  E-value: 2.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831592   377 CIRCSACADACPADLLpqqlywfskgQQHDKATTHNI----ADCIECGACAWVCPSNI 430
Cdd:pfam13187   2 CTGCGACVAACPAGAI----------VPDLVGQTIRGdiagLACIGCGACVDACPRGA 49
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
377-429 5.05e-06

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 44.79  E-value: 5.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831592   377 CIRCSACADACPADLLPQQLY-WFS-----------KGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGvLDArrcisyltiekKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 376-429 5.20e-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: 46.24  E-value: 5.20e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831592 376 SCIRCSACADACPADLLPQQLYwFSKGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:cd10549  41 KCVFCGACVEVCPTGAIELTPE-GKEYVPKEKEAEIDEEKCIGCGLCVKVCPVD 93
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 377-430 6.05e-06

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: 45.32  E-value: 6.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15831592   377 CIRCSACADACPADLLpqqlywfSKGQQHDKATTHNIADCIECGACAWVCPSNI 430
Cdd:TIGR00402  36 CTRCGECASACENNIL-------QLGQQGQPTVEFDNAECDFCGKCAEACPTNA 82
PRK05352 PRK05352
Na(+)-translocating NADH-quinone reductase subunit A; Provisional
 59-438 1.03e-05

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


Pssm-ID: 235426 [Multi-domain]  Cd Length: 448  Bit Score: 48.64  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   59 VSVGDKVLRGQPL-----TRGrgkmlpVH--APTSGTVTAIAphstahpsaLAE----LSVIIDADGEDcwipRDGWADY 127
Cdd:PRK05352  46 VKEGDKVKKGQPLfedkkNPG------VKftSPASGTVVAIN---------RGErrvlQSVVIEVEGDE----QVTFEKY 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  128 RSRR-----REELIERIHQfgvAGLGGA--GFPTgvklqgggDKIETL-------IINAAECEPyITADDRL-MQDCAAQ 192
Cdd:PRK05352 107 DAKDlaslsREQVKENLLE---SGLWTAlrTRPF--------SKVPAPdstpraiFVTAMDTNP-LAADPEViIAEQEEA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  193 VVEGIRILAHiLQPREILIGIEDNkpqaismLRAVLADSHDISMRVIPTKYPSGGA-KQLTYIL---TGKQVPHggrssd 268
Cdd:PRK05352 175 FQAGLTVLSR-LTDGKVHVCKAPG-------ASLPGENLKNVEVHTFSGPHPAGLVgTHIHFLDpvsAGKTVWT------ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  269 IGVlmQNVgtaYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLndAGFCPSADQMVIMGGPLMGFT--- 345
Cdd:PRK05352 241 IGY--QDV---IAIGKLFLTGELYTERVVALAGPAVKKPRLVRTRLGASLSELT--AGELKAGDNRVISGSVLTGRTakg 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  346 -----------------------LPWLdVPVVK---ITNCLL---------APSANELGepqEEQSCIRCSACADACPAD 390
Cdd:PRK05352 314 phaylgryhnqvsvlpegrerelFGWL-RPGFNkfsVTRTYLshlfkkklfNFTTNTNG---SERAMVPIGNYERVMPLD 389

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831592  391 LLPQQL--------YwfskgqqhDKATTHNIADCIE--CGACAWVCPSNIPLVQYFRQ 438
Cdd:PRK05352 390 ILPTQLlralivgdT--------DEAQALGALELDEedLALCTFVCPGKYEYGPILRD 439
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
377-427 1.08e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.95  E-value: 1.08e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15831592 377 CIRCSACADACPADLLpqqlywfskgQQHDKATTHNIADCIECGACAWVCP 427
Cdd:COG2768  13 CIGCGACVKVCPVGAI----------SIEDGKAVIDPEKCIGCGACIEVCP 53
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 376-472 1.61e-05

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: 1.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 376 SCIRCSACADACP---------------ADLLpQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSNIPLVQYFRQEK 440
Cdd:COG0247  79 ACVGCGFCRAMCPsykatgdekdsprgrINLL-REVLEGELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEAR 157

                        90       100       110
                ....*....|....*....|....*....|....
gi 15831592 441 AEIAairQEEKRAAEAKA--RFEARLARLEREKA 472
Cdd:COG0247 158 AQLV---ERGGRPLRDRLlrTFPDRVPAADKEGA 188
PTZ00121 PTZ00121
MAEBL; Provisional
 434-713 1.79e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   434 QYFRQEKAEiAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQPiVI 513
Cdd:PTZ00121 1207 KAEEERKAE-EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE-LK 1284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   514 KAGERPDNSAIIAAREARKA-QARAKQAELQQTNDAATVTDPRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVE 592
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   593 AAIARAKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQ-QQANAEPEEPVDPRKAAVEAAIARAKARKLEQQQ 671
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 15831592   672 ANAEPEEPVDPRKAAVEAAITRAKARKLEQQQANAEPEEQVD 713
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 369-479 2.35e-05

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 45.79  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  369 GEPQEE-QSCIRCSACADACPADLLPQQLywfsKGQQHDKATTHNIADCIECGACAWVCPSN-IPLVQYFrqekaEIAAI 446
Cdd:PRK12387  31 GKPEYNpQQCIGCAACVNACPSNALTVET----DLATGELAWEFNLGRCIFCGRCEEVCPTAaIKLSQEF-----ELAVW 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15831592  447 RqeeKRAAEAKARFEAR------------------LARLEREKAARLERHK 479
Cdd:PRK12387 102 K---KEDLLQQSEFALCncrvcgrpfavqkeidyaIALLKHNGDSRAENHR 149
PRK11278 PRK11278
NADH-quinone oxidoreductase subunit NuoF;
113-205 2.37e-05

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 236891 [Multi-domain]  Cd Length: 448  Bit Score: 47.49  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  113 DGEDCWI----PRDGWADYR----SRRREELIERIHQFGVAGLGGAGFPTGVKL----QGGGDKIETLIINAAECEPYIT 180
Cdd:PRK11278  21 DKQPVWLdeyrSKNGYEGARkaltGMSPDEIVNQVKDAGLKGRGGAGFSTGLKWslmpKDESMNIRYLLCNADEMEPGTY 100

                         90       100
                 ....*....|....*....|....*
gi 15831592  181 ADDRLMQDCAAQVVEGIRILAHILQ 205
Cdd:PRK11278 101 KDRLLMEQLPHLLVEGMLISAFALK 125
NuoF COG1894
NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and ...
 109-353 2.50e-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: 47.31  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 109 IIDADGEDCWIPRDGWADYR----SRRREELIERIHQFGVAGLGGAGFPTGVK-----LQGGGDKieTLIINAAECEPYi 179
Cdd:COG1894  13 IIDPESLEDYIARGGYQALRkaltEMTPEEVIEEVKDSGLRGRGGAGFPTGLKwsfvpKAPGDPK--YLVCNADEGEPG- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 180 TADDR-LMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLAD--------------SHDISMRViptkYP 244
Cdd:COG1894  90 TFKDRsLLEGDPHQLIEGMIIAAYAIGATKGYIYIRGEYPLAIERLEKAIEEareagllgknilgsGFDFDIEV----HR 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 245 SGGAkqltYI----------LTGK------------------------------QVPH----GGRS-SDIGVlMQNVGTa 279
Cdd:COG1894 166 GAGA----YIcgeetallesLEGKrgqprlkppfpavsglwgkptvvnnvetlaNVPHiirnGAEWfASIGT-EKSKGT- 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831592 280 yavkravidgepiteRVVTLTGeAIARPGNVWARLGTPVRHLLND-AGFCPSADQ--MVIMGGPLMGFtLP--WLDVPV 353
Cdd:COG1894 240 ---------------KLFSLSG-HVKNPGLYEVPMGTTLRELIYDiGGGIRGGRKlkAVQPGGPSGGC-LPaeHLDTPM 301
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 436-643 2.51e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 436 FRQEKAEIAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQpaakdKDAIAAALARVKEKQAQATQPIVIKA 515
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-----LEELEEELEEAEEELEEAEAELAEAE 364

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 516 GERPDNSAIIAAREARKAQARAKQAELQQTNDAATVTDPRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAAI 595
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15831592 596 ARAKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAE 643
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 377-430 2.92e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 44.31  E-value: 2.92e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831592 377 CIRCSACADACPADLLpqqlywfSKGQQHDKATTHNI--ADCIECGACAWVCPSNI 430
Cdd:cd10549   8 CIGCGICVKACPTDAI-------ELGPNGAIARGPEIdeDKCVFCGACVEVCPTGA 56
PTZ00121 PTZ00121
MAEBL; Provisional
 440-771 3.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   440 KAEIAAIRQEEKRAAEAKARFEARLA----RLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAqatqpiVIKA 515
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAeavkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA------AIKA 1274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   516 GERPDNSAIIAAREARKAQARAKQAELQQTNDAATVTDPRKTAVEA-AIARAKARKLEQQQANAEPEQQVDPRKAAVEAA 594
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   595 IARAKARKLEQQQAnAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEEPVDP-RKAAVEAAIARAKARKLEQQQAN 673
Cdd:PTZ00121 1355 AADEAEAAEEKAEA-AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKA 1433

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   674 AEPEEPVDPRKAAVEAAITRAKARKLEQQQANAEPEEQVDPRKAAVAAAIARAkarklEQQQANAEPEEQVDPRKAAVAA 753
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEEAKKKADEAKKAAEA 1508

                         330
                  ....*....|....*...
gi 15831592   754 AIARVQAKKAVQQKVVNE 771
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADE 1526
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 377-427 5.36e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.96  E-value: 5.36e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15831592 377 CIRCSACADACPADLLpqqlyWFSKGqqhdKATTHNiADCIECGACAWVCP 427
Cdd:COG2221  17 CIGCGLCVAVCPTGAI-----SLDDG----KLVIDE-EKCIGCGACIRVCP 57
PRK13596 PRK13596
NADH-quinone oxidoreductase subunit NuoF;
117-199 6.13e-05

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 237441  Cd Length: 433  Bit Score: 46.12  E-value: 6.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  117 CWiprDGWADYRSRRREELIERIHQFGVAGLGGAGFPTGVKL----QGGGDKIETLIINAAECEPYITADDRLMQDCAAQ 192
Cdd:PRK13596  28 DW---DGTKAILDKGRDWIIEEMKASGLRGRGGAGFPTGLKWsfmpKESDGRPHYLVVNADESEPGTCKDRDILRHDPHK 104


                 ....*..
gi 15831592  193 VVEGIRI 199
Cdd:PRK13596 105 LIEGCLI 111
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
373-430 2.82e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 43.51  E-value: 2.82e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831592 373 EEQSCIRCSACADACPADLLPqqlywfSKGQQHDkatthniADCIECGACAWVCPSNI 430
Cdd:COG0348 208 DRGDCIDCGLCVKVCPMGIDI------RKGEINQ-------SECINCGRCIDACPKDA 252
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 369-436 4.69e-04

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 41.66  E-value: 4.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  369 GEPQ-EEQSCIRCSACADACPADLLPQQlywfSKGQQHDKATTHNIADCIECGACAWVCPSN-IPLVQYF 436
Cdd:PRK08222  31 GKPDlMPSQCIACGACTCACPANALTIQ----TDDQQNSRTWQLYLGRCIYCGRCEEVCPTRaIQLTNNF 96
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
370-427 5.83e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 41.41  E-value: 5.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831592  370 EPQEEQSCIRCSACADACPADLLpqQLYWfSKGQQHDKATTH---NIADCIECGACAWVCP 427
Cdd:PRK05888  53 DPNGEERCIACKLCAAICPADAI--TIEA-AEREDGRRRTTRydiNFGRCIFCGFCEEACP 110
PTZ00121 PTZ00121
MAEBL; Provisional
 438-772 6.97e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   438 QEKAEIAAIRQEE--KRAAEAKARFEARLARLEREKAARLERHKSAAVQPAAKDKDAIAAalARVKEKQAQATQPIVIKA 515
Cdd:PTZ00121 1363 EEKAEAAEKKKEEakKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEKKKADEAKKKA 1440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   516 GE-RPDNSAIIAAREARKAQARAKQAELQQTNDAAtvtdpRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAA 594
Cdd:PTZ00121 1441 EEaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA-----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   595 IARAKARKLEQQQaNAEPEQQVDPRKAAVEAAIARAKARKLEQQQanAEPEEPVDPRKAAVEAAIARAKARKLEQQQANA 674
Cdd:PTZ00121 1516 KKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   675 EPEEPVDPRKAavEAAITRAKARKLEQQQANAepeEQVDPRKAAVAAAIARAKARKLEQQQA-NAEPEEQVDPRKAAVAA 753
Cdd:PTZ00121 1593 RIEEVMKLYEE--EKKMKAEEAKKAEEAKIKA---EELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEA 1667

                         330
                  ....*....|....*....
gi 15831592   754 AIARVQAKKAVQQKVVNED 772
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEED 1686
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 376-429 8.01e-04

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 38.77  E-value: 8.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15831592  376 SCIRCSACADACPADLLPQQLYWFSKGQQhdKATTHNIADCIECGACAWVCPSN 429
Cdd:PLN00071  10 TCIGCTQCVRACPTDVLEMIPWDGCKAKQ--IASAPRTEDCVGCKRCESACPTD 61
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 363-449 8.84e-04

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: 42.78  E-value: 8.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 363 PSANELGEpqEEQSCIRCSACADACPADL-LPQQLYWFSKGQQHDKATTHNIadCIECGACAWVCPSNIPLVQYFrqEKA 441
Cdd:cd01916 355 PTDEEFQE--LAAKCTDCGWCTRACPNSLrIKEAMEAAKEGDFSGLADLFDQ--CVGCGRCEQECPKEIPIINMI--EKA 428


                ....*...
gi 15831592 442 EIAAIRQE 449
Cdd:cd01916 429 ARERIKEE 436
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 375-440 9.35e-04

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


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 40.75  E-value: 9.35e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 375 QSCIRCS--ACADACPADLLpqqlywfskgqQHDK--ATTHNIADCIECGACAWVCPSNIPlvQYFRQEK 440
Cdd:cd10562  68 RQCMHCTdaACVKVCPTGAL-----------YKTEngAVVVDEDKCIGCGYCVAACPFDVP--RYDETTN 124
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
373-446 1.03e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.54  E-value: 1.03e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831592 373 EEQSCIRCSACADACPadllpqqlywFSKGQQHDKATTH-NIADCIECGACAWVCPSNIPLVQYFRQE--KAEIAAI 446
Cdd:COG1148 494 DPEKCTGCGRCVEVCP----------YGAISIDEKGVAEvNPALCKGCGTCAAACPSGAISLKGFTDDqiLAQIDAL 560
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-544 1.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 437 RQEKAEIAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQPAAKDKDA--IAAALARVKEKQAQATQPIVIK 514
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeAAEEEAELEEEEEALLELLAEL 468

                        90       100       110
                ....*....|....*....|....*....|
gi 15831592 515 AGERPDNSAIIAAREARKAQARAKQAELQQ 544
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLE 498
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 374-427 1.19e-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: 39.56  E-value: 1.19e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831592 374 EQSCIRCSACADACPADllpqQLYWfskgqqhdKATTHNIADCIECGACAWVCP 427
Cdd:cd16370  82 KEKCIGCGNCVKACIVG----AIFW--------DEETNKPIICIHCGYCARYCP 123
PRK09898 PRK09898
ferredoxin-like protein;
373-428 1.20e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 40.97  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831592  373 EEQSCIRCSACADACP---ADLLPQqlywfskgqqhDKATThniaDCIECGACAWVCPS 428
Cdd:PRK09898 152 DHKRCIGCSACTTACPwmmATVNTE-----------SKKSS----KCVLCGECANACPT 195
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 377-449 1.24e-03

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 41.27  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 377 CIRCSACADACP---ADLL---PQ---QLYWF---SKGQQHDK-----ATTHNIADCIECGACAWVCPSNIPLvqyfrqE 439
Cdd:COG0479 144 CILCGACVAACPnvwANPDflgPAalaQAYRFaldPRDEETEErlealEDEEGVWRCTTCGNCTEVCPKGIPP------T 217

                        90
                ....*....|
gi 15831592 440 KAeIAAIRQE 449
Cdd:COG0479 218 KA-IAKLKRE 226
PTZ00121 PTZ00121
MAEBL; Provisional
 440-767 1.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   440 KAEIAAIRQE-EKRAAEAKARFEARLARLER--EKAARLERHKSaaVQPAAKDKDAIAAALARVKE--KQAQATQpiviK 514
Cdd:PTZ00121 1110 KAEEARKAEEaKKKAEDARKAEEARKAEDARkaEEARKAEDAKR--VEIARKAEDARKAEEARKAEdaKKAEAAR----K 1183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   515 AGERPDNSAIIAAREARKAQARAKQAELQQTNDAATVTDPRKtaVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAA 594
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKK--AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   595 IARAKArklEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEEPVDPRKAAVEAAIARAKARKLEQQQANA 674
Cdd:PTZ00121 1262 MAHFAR---RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592   675 EPEEpvdpRKAAVEAAITRAKARKLEQQQANAEPEEQVDPRKAAVAAAIARAKARKLEQQQANAEPEEQvdpRKAAVAAA 754
Cdd:PTZ00121 1339 EEAK----KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED---KKKADELK 1411

                         330
                  ....*....|...
gi 15831592   755 IARVQAKKAVQQK 767
Cdd:PTZ00121 1412 KAAAAKKKADEAK 1424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-704 1.59e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 437 RQEKAEIAAIRQEEKRAAEAKARFEARLARLEREKAARLERHKSAAVQpaakdKDAIAAALARVKEKQAQATQpivikag 516
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----LEELEEELAELEEELEELEE------- 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 517 erpDNSAIIAAREARKAQARAKQAELQQTNDAATVTDPRKTAVEAAIARAKARKLEQQQANAEPEQQVDpRKAAVEAAIA 596
Cdd:COG1196 338 ---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-ELEEAEEALL 413

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 597 RAKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEEPVDPRKAAVEAAIARAKARKLEQQQANAEp 676
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR- 492

                       250       260
                ....*....|....*....|....*...
gi 15831592 677 EEPVDPRKAAVEAAITRAKARKLEQQQA 704
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLR 520
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 377-429 1.64e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 39.24  E-value: 1.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831592 377 CIRCSACADACPADLLpqqlywfskgQQHDKATTHniADCIECGACAWVCPSN 429
Cdd:cd16372  79 CVGCLMCVGFCPEGAM----------FKHEDYPEP--FKCIACGICVKACPTG 119
psaC CHL00065
photosystem I subunit VII
 376-429 1.79e-03

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 37.82  E-value: 1.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15831592  376 SCIRCSACADACPADLLPQQLYWFSKGQQhdKATTHNIADCIECGACAWVCPSN 429
Cdd:CHL00065  10 TCIGCTQCVRACPTDVLEMIPWDGCKAKQ--IASAPRTEDCVGCKRCESACPTD 61
PRK12472 PRK12472
hypothetical protein; Provisional
 439-558 1.84e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.39  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592  439 EKAEIAAIRQEEKRAAEAKARFEARLA----RLEREKAARLERHKSAavqpaakdkdaiAAALARVKEKQAQAtqpiviK 514
Cdd:PRK12472 198 EAEDAARAADEAKTAAAAAAREAAPLKaslrKLERAKARADAELKRA------------DKALAAAKTDEAKA------R 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15831592  515 AGERPDNSAIIAAR-----EARKAQARAKQAELQQTNDAATVTDPRKTA 558
Cdd:PRK12472 260 AEERQQKAAQQAAEaatqlDTAKADAEAKRAAAAATKEAAKAAAAKKAE 308
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 377-429 2.43e-03

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 37.72  E-value: 2.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831592 377 CIRCSACADACPADLLpqqlywfskGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:COG1144  32 CIGCGLCWIVCPDGAI---------RVDDGKYYGIDYDYCKGCGICAEVCPVK 75
ndhI CHL00014
NADH dehydrogenase subunit I
 373-429 2.48e-03

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 39.36  E-value: 2.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831592  373 EEQSCIRCSACADACPADlLPQQLYWFSKGQQHDKATTHNI--ADCIECGACAWVCPSN 429
Cdd:CHL00014  57 EFDKCIACEVCVRVCPID-LPVVDWKLETDIRKKRLLNYSIdfGVCIFCGNCVEYCPTN 114
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 376-431 3.04e-03

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


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 39.68  E-value: 3.04e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831592 376 SCIRCS--ACADACPAdllPQQLYWFSKGQ---QHDKatthniadCIECGACAWVCPSNIP 431
Cdd:cd10558  69 GCMHCAdpGCLKACPS---PGAIVQYANGIvdfQSDK--------CIGCGYCIKGCPFDIP 118
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 375-430 4.28e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 38.38  E-value: 4.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831592 375 QSCIRCSACADACP-------ADLLPQqlYWFSKGQqhdkatthniadCIECGACAWVCPSNI 430
Cdd:cd10564  13 DLCTRCGDCVEACPegiivrgDGGFPE--LDFSRGE------------CTFCGACAEACPEGA 61
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 376-427 4.91e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 37.93  E-value: 4.91e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831592 376 SCIRCS--ACADACPADLlpqqlywFSKgqQHDKATTHNIADCIECGACAWVCP 427
Cdd:cd16371  53 SCNHCEnpACVKVCPTGA-------ITK--REDGIVVVDQDKCIGCGYCVWACP 97
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 375-429 6.86e-03

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 39.11  E-value: 6.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15831592  375 QSCIRCSACADACPAdllPQQLYWFSKGQQHDKATTHniADCIECGACAWVCPSN 429
Cdd:PRK09477 208 QKCTRCMDCFHVCPE---PQVLRPPLKGKQSPSQVTS--GDCITCGRCIDVCSED 257
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
374-451 7.26e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 39.62  E-value: 7.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 374 EQSCIRCSACADACPADLLpqqlywfskGQQHDKATTHNiADCIECGACAWVCPSNiplvqyFRQEKAEI----AAIRQE 449
Cdd:COG4624  90 KEKCKNCYPCVRACPVKAI---------KVDDGKAEIDE-EKCISCGQCVAVCPFG------AITEKSDIekvkKALKDP 153


                ..
gi 15831592 450 EK 451
Cdd:COG4624 154 EK 155
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 358-429 9.91e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 36.93  E-value: 9.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831592 358 NCLLAPSANELGEPQEEQSCIR---------------CSACADACPADLL---PQQLYWFSKgqqhdkatthniADCIEC 419
Cdd:cd16372  15 QCEEACSKTFFKEEDREKSCIRiteteggyainvcnqCGECIDVCPTGAItrdANGVVMINK------------KLCVGC 82

                        90
                ....*....|
gi 15831592 420 GACAWVCPSN 429
Cdd:cd16372  83 LMCVGFCPEG 92
 
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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