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Conserved domains on  [gi|1352185129|gb|AVI56145|]
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electron transporter RsxC [Escherichia coli str. K-12 substr. MG1655]

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
 7-684 0e+00

electron transport complex protein RnfC; Provisional


:

Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 1043.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129   7 AFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPT 85
Cdd:PRK05035    1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMsLPVHAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  86 SGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKI 165
Cdd:PRK05035   81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 166 ETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPS 245
Cdd:PRK05035  161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 246 GGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDA 325
Cdd:PRK05035  241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 326 GFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQH 405
Cdd:PRK05035  321 GFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEH 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 406 DKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQP 485
Cdd:PRK05035  401 DKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEAR 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 486 AAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDaatvADPRKTAVEAAIAR 565
Cdd:PRK05035  481 AAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAA----ADPKKAAVAAAIAR 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 566 AKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQ---VDPRKAAVEAAIARAKARKLEQQQAnA 642
Cdd:PRK05035  557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQvaeVDPKKAAVAAAIARAKAKKAEQQAN-A 635

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 1352185129 643 EPEQQVDPRKAAVEAAIARAKARKREQQPANAEPEEQVDPRK 684
Cdd:PRK05035  636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKK 677
 
Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-684 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 1043.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129   7 AFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPT 85
Cdd:PRK05035    1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMsLPVHAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  86 SGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKI 165
Cdd:PRK05035   81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 166 ETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPS 245
Cdd:PRK05035  161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 246 GGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDA 325
Cdd:PRK05035  241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 326 GFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQH 405
Cdd:PRK05035  321 GFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEH 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 406 DKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQP 485
Cdd:PRK05035  401 DKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEAR 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 486 AAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDaatvADPRKTAVEAAIAR 565
Cdd:PRK05035  481 AAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAA----ADPKKAAVAAAIAR 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 566 AKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQ---VDPRKAAVEAAIARAKARKLEQQQAnA 642
Cdd:PRK05035  557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQvaeVDPKKAAVAAAIARAKAKKAEQQAN-A 635

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 1352185129 643 EPEQQVDPRKAAVEAAIARAKARKREQQPANAEPEEQVDPRK 684
Cdd:PRK05035  636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKK 677
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: 784.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  12 KIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPTSGTVT 90
Cdd:COG4656     2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVsAPVHAPVSGTVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  91 AIAPHstAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLI 169
Cdd:COG4656    82 AIEPA--PHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDkKIDTLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 170 INAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPSGGAK 249
Cdd:COG4656   160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDDIEVVVLPTKYPQGGEK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 250 QLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCP 329
Cdd:COG4656   240 QLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGFK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 330 SADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGePQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKAT 409
Cdd:COG4656   320 EEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVP-PPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352185129 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: 648.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  14 WDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGK-MLPVHAPTSGTVTAI 92
Cdd:TIGR01945   2 FTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFvSAPIHAPTSGTVVAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  93 APHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIIN 171
Cdd:TIGR01945  82 EERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNPPPEkKIETLIIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 172 AAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNdISLRVIPTKYPSGGAKQL 251
Cdd:TIGR01945 162 GAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGGYN-IKVRVLPTKYPQGGEKQL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 252 TYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCPSA 331
Cdd:TIGR01945 241 IYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFREK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 332 DQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEpQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTH 411
Cdd:TIGR01945 321 PERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPE-SPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEEH 399

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1352185129 412 NIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIR 447
Cdd:TIGR01945 400 NLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLRAKK 435
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
139-283 1.64e-58

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 195.04  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 139 IHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNK 217
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPKkKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 218 PQAISMLRAVLADSN----DISLRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVK 283
Cdd:pfam01512  81 PEAIAALEKAIAEARaagfDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 376-429 5.68e-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: 5.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 376 SCIRCSACADACPADLLPQQLYwFSKGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:cd10549    41 KCVFCGACVEVCPTGAIELTPE-GKEYVPKEKEAEIDEEKCIGCGLCVKVCPVD 93
 
Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-684 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 1043.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129   7 AFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPT 85
Cdd:PRK05035    1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRMsLPVHAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  86 SGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKI 165
Cdd:PRK05035   81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 166 ETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPS 245
Cdd:PRK05035  161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 246 GGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDA 325
Cdd:PRK05035  241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 326 GFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQH 405
Cdd:PRK05035  321 GFKPDADQRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEEH 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 406 DKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQP 485
Cdd:PRK05035  401 DKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEAR 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 486 AAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDaatvADPRKTAVEAAIAR 565
Cdd:PRK05035  481 AAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAA----ADPKKAAVAAAIAR 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 566 AKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQ---VDPRKAAVEAAIARAKARKLEQQQAnA 642
Cdd:PRK05035  557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQvaeVDPKKAAVAAAIARAKAKKAEQQAN-A 635

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 1352185129 643 EPEQQVDPRKAAVEAAIARAKARKREQQPANAEPEEQVDPRK 684
Cdd:PRK05035  636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKK 677
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: 784.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  12 KIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKM-LPVHAPTSGTVT 90
Cdd:COG4656     2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGFVsAPVHAPVSGTVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  91 AIAPHstAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLI 169
Cdd:COG4656    82 AIEPA--PHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDkKIDTLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 170 INAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPSGGAK 249
Cdd:COG4656   160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDDIEVVVLPTKYPQGGEK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 250 QLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCP 329
Cdd:COG4656   240 QLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLEQAGGFK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 330 SADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGePQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKAT 409
Cdd:COG4656   320 EEPGKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVP-PPEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDKAE 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352185129 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: 648.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  14 WDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGK-MLPVHAPTSGTVTAI 92
Cdd:TIGR01945   2 FTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGFvSAPIHAPTSGTVVAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  93 APHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIIN 171
Cdd:TIGR01945  82 EERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNPPPEkKIETLIIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 172 AAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNdISLRVIPTKYPSGGAKQL 251
Cdd:TIGR01945 162 GAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGGYN-IKVRVLPTKYPQGGEKQL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 252 TYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCPSA 331
Cdd:TIGR01945 241 IYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILAFCGGFREK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 332 DQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEpQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTH 411
Cdd:TIGR01945 321 PERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPE-SPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEAEEH 399

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1352185129 412 NIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIR 447
Cdd:TIGR01945 400 NLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLRAKK 435
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
139-283 1.64e-58

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 195.04  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 139 IHQFGVAGLGGAGFPTGVKLQGGGD-KIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNK 217
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPKkKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 218 PQAISMLRAVLADSN----DISLRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVK 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 8.48e-40

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: 141.54  E-value: 8.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  14 WDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRG-KMLPVHAPTSGTVTAI 92
Cdd:pfam13375   1 WTFKGGIHPPENKELSKDKPIEKLPLPKELVIPLSQHIGAPAEPIVKVGDRVLKGQKIAEADGfVSAPVHASVSGTVKAI 80

                          90       100
                  ....*....|....*....|...
gi 1352185129  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 1.80e-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: 53.68  E-value: 1.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 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 4.03e-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: 53.23  E-value: 4.03e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 377 CIRCSACADACPADLL----PQQL-YWFSKGQQHDKATTHNIADCIECGACAWVCPSNIP 431
Cdd:pfam13534   2 CIQCGCCVDECPRYLLngdePKKLmRAAYLGDLEELQANKVANLCSECGLCEYACPMGLD 61
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 374-427 1.03e-08

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 52.02  E-value: 1.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 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 6.15e-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: 50.00  E-value: 6.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 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 8.44e-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: 49.17  E-value: 8.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352185129 377 CIRCSACADACPADLLPQQLYWFSKGqqhDKATTHNIADCIECGACAWVCP 427
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIVERLE---GEAVRIGVWKCIGCGACVEACP 56
PRK06991 PRK06991
electron transport complex subunit RsxB;
373-557 1.27e-07

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 53.64  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 373 EEQSCIRCSACADACPADLL---PQQLYWFskgqqhdkatthnIAD-CIECGACAWVCPSN-IPLVQYFRqEKAEIAAIR 447
Cdd:PRK06991   83 DEQLCIGCTLCMQACPVDAIvgaPKQMHTV-------------LADlCTGCDLCVPPCPVDcIDMVPVTG-ERTGWDAWS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 448 QEekRAAEAKARFEARQARLEREKAARLERHKSAAvqpaakdkdaiAAALARVKEKQAQATQPIVIKAGERpdNSAIIAA 527
Cdd:PRK06991  149 QA--QADAARARHDARQARLRREREAAEARAAARA-----------AASAAAAAAEASAAAAPAADDAEAK--KRAIIAA 213

                         170       180       190
                  ....*....|....*....|....*....|
gi 1352185129 528 REARkaqARAKQAELqqtndAATVADPRKT 557
Cdd:PRK06991  214 ALER---ARKKKEEL-----AAQGAGPKNT 235
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 371-429 2.90e-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: 2.90e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1352185129 371 PQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:TIGR01971  39 PNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEINFGRCIFCGLCEEACPTD 97
PRK05352 PRK05352
Na(+)-translocating NADH-quinone reductase subunit A; Provisional
 59-438 3.22e-07

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


Pssm-ID: 235426 [Multi-domain]  Cd Length: 448  Bit Score: 53.26  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  59 VSVGDKVLRGQPL-----TRGrgkmlpVH--APTSGTVTAIAphstahpsaLAE----LSVIIDADGEDcwipRDGWADY 127
Cdd:PRK05352   46 VKEGDKVKKGQPLfedkkNPG------VKftSPASGTVVAIN---------RGErrvlQSVVIEVEGDE----QVTFEKY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 128 R-----TRSREELIERIHQfgvAGLGGA--GFPTgvklqgggDKIETL-------IINAAECEPyITADDRL-MQDCAAQ 192
Cdd:PRK05352  107 DakdlaSLSREQVKENLLE---SGLWTAlrTRPF--------SKVPAPdstpraiFVTAMDTNP-LAADPEViIAEQEEA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 193 VVEGIRILAHiLQPREILIGIEDNkpqaismLRAVLADSNDISLRVIPTKYPSGGA-KQLTYIL---TGKQVPHggrssd 268
Cdd:PRK05352  175 FQAGLTVLSR-LTDGKVHVCKAPG-------ASLPGENLKNVEVHTFSGPHPAGLVgTHIHFLDpvsAGKTVWT------ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 269 IGVlmQNVgtaYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLndAGFCPSADQMVIMGGPLMGFT--- 345
Cdd:PRK05352  241 IGY--QDV---IAIGKLFLTGELYTERVVALAGPAVKKPRLVRTRLGASLSELT--AGELKAGDNRVISGSVLTGRTakg 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 346 -----------------------LPWLdVPVVK---ITNCLL---------APSANELGepqEEQSCIRCSACADACPAD 390
Cdd:PRK05352  314 phaylgryhnqvsvlpegrerelFGWL-RPGFNkfsVTRTYLshlfkkklfNFTTNTNG---SERAMVPIGNYERVMPLD 389

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1352185129 391 LLPQQL--------YwfskgqqhDKATTHNIADCIE--CGACAWVCPSNIPLVQYFRQ 438
Cdd:PRK05352  390 ILPTQLlralivgdT--------DEAQALGALELDEedLALCTFVCPGKYEYGPILRD 439
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 377-429 4.08e-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: 4.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352185129 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 5.28e-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: 5.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1352185129 377 CIRCSACADACPADLLpqqlywfsKGQQHDKATTHNI--ADCIECGACAWVCPSN 429
Cdd:COG1143     4 CIGCGLCVRVCPVDAI--------TIEDGEPGKVYVIdpDKCIGCGLCVEVCPTG 50
NapF COG1145
Ferredoxin [Energy production and conversion];
324-429 8.16e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.88  E-value: 8.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 324 DAGFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQ-EEQSCIRCSACADACPADLLpqqlywfsKG 402
Cdd:COG1145   130 EVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAViDAEKCIGCGLCVKVCPTGAI--------RL 201

                          90       100
                  ....*....|....*....|....*..
gi 1352185129 403 QQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:COG1145   202 KDGKPQIVVDPDKCIGCGACVKVCPVG 228
SLBB pfam10531
SLBB domain;
296-344 1.26e-06

SLBB domain;


Pssm-ID: 463136 [Multi-domain]  Cd Length: 56  Bit Score: 46.12  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1352185129 296 VVTLTGEaIARPGNVWARLGTPVRHLLNDA-GFCPSADQMVI------MGGPLMGF 344
Cdd:pfam10531   1 VVTVTGE-VKRPGNYEVPIGTTLSDLIELAgGFTDDADLDINlrrlkrPGGPMMGI 55
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 377-455 1.28e-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: 46.26  E-value: 1.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352185129 377 CIRCSACADACPADLLpqqlywfskGQQHDKATTHNIADCIECGACAWVCPSNiplvqyfrqekaeiaAIRQEEKRAAE 455
Cdd:COG1149    13 CIGCGLCVEVCPEGAI---------KLDDGGAPVVDPDLCTGCGACVGVCPTG---------------AITLEEREAGK 67
NuoF COG1894
NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and ...
 109-353 2.84e-06

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: 50.40  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 109 IIDADGEDCWIPRDGWADYR----TRSREELIERIHQFGVAGLGGAGFPTGVK-----LQGGGDKieTLIINAAECEPYi 179
Cdd:COG1894    13 IIDPESLEDYIARGGYQALRkaltEMTPEEVIEEVKDSGLRGRGGAGFPTGLKwsfvpKAPGDPK--YLVCNADEGEPG- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 180 TADDR-LMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLAD----------------SNDISLRViptk 242
Cdd:COG1894    90 TFKDRsLLEGDPHQLIEGMIIAAYAIGATKGYIYIRGEYPLAIERLEKAIEEareagllgknilgsgfDFDIEVHR---- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 243 ypSGGAkqltYI----------LTGK------------------------------QVPH----GGRS-SDIGVlMQNVG 277
Cdd:COG1894   166 --GAGA----YIcgeetallesLEGKrgqprlkppfpavsglwgkptvvnnvetlaNVPHiirnGAEWfASIGT-EKSKG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 278 TayavkravidgepiteRVVTLTGeAIARPGNVWARLGTPVRHLLND-AGFCPSADQ--MVIMGGPLMGFtLP--WLDVP 352
Cdd:COG1894   239 T----------------KLFSLSG-HVKNPGLYEVPMGTTLRELIYDiGGGIRGGRKlkAVQPGGPSGGC-LPaeHLDTP 300


                  .
gi 1352185129 353 V 353
Cdd:COG1894   301 M 301
Fer4_9 pfam13187
4Fe-4S dicluster domain;
377-430 3.93e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 44.47  E-value: 3.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1352185129 377 CIRCSACADACPADLLpqqlywfskgQQHDKATTHNI----ADCIECGACAWVCPSNI 430
Cdd:pfam13187   2 CTGCGACVAACPAGAI----------VPDLVGQTIRGdiagLACIGCGACVDACPRGA 49
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 376-429 5.68e-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: 5.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 376 SCIRCSACADACPADLLPQQLYwFSKGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:cd10549    41 KCVFCGACVEVCPTGAIELTPE-GKEYVPKEKEAEIDEEKCIGCGLCVKVCPVD 93
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
377-429 6.24e-06

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 44.40  E-value: 6.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352185129 377 CIRCSACADACPADLLPQQLY-WFS-----------KGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGvLDArrcisyltiekKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 377-430 6.76e-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: 6.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 377 CIRCSACADACPADLLpqqlywfSKGQQHDKATTHNIADCIECGACAWVCPSNI 430
Cdd:TIGR00402  36 CTRCGECASACENNIL-------QLGQQGQPTVEFDNAECDFCGKCAEACPTNA 82
PRK11278 PRK11278
NADH-quinone oxidoreductase subunit NuoF;
113-205 7.60e-06

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 236891 [Multi-domain]  Cd Length: 448  Bit Score: 49.03  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 113 DGEDCWI----PRDGWADYR----TRSREELIERIHQFGVAGLGGAGFPTGVKL----QGGGDKIETLIINAAECEPYIT 180
Cdd:PRK11278   21 DKQPVWLdeyrSKNGYEGARkaltGMSPDEIVNQVKDAGLKGRGGAGFSTGLKWslmpKDESMNIRYLLCNADEMEPGTY 100

                          90       100
                  ....*....|....*....|....*
gi 1352185129 181 ADDRLMQDCAAQVVEGIRILAHILQ 205
Cdd:PRK11278  101 KDRLLMEQLPHLLVEGMLISAFALK 125
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
377-427 1.02e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.95  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352185129 377 CIRCSACADACPADLLpqqlywfskgQQHDKATTHNIADCIECGACAWVCP 427
Cdd:COG2768    13 CIGCGACVKVCPVGAI----------SIEDGKAVIDPEKCIGCGACIEVCP 53
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 376-470 2.30e-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: 47.38  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 376 SCIRCSACADACP---------------ADLLpQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSNIPLVQYFRQEK 440
Cdd:COG0247    79 ACVGCGFCRAMCPsykatgdekdsprgrINLL-REVLEGELPLDLSEEVYEVLDLCLTCKACETACPSGVDIADLIAEAR 157

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1352185129 441 AEIAA--IRQEEKRAAEAKARFEARQARLERE 470
Cdd:COG0247   158 AQLVErgGRPLRDRLLRTFPDRVPAADKEGAE 189
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 369-479 2.39e-05

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 45.41  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 369 GEPQEE-QSCIRCSACADACPADLLPQQLywfsKGQQHDKATTHNIADCIECGACAWVCPSN-IPLVQYFrqekaEIAAI 446
Cdd:PRK12387   31 GKPEYNpQQCIGCAACVNACPSNALTVET----DLATGELAWEFNLGRCIFCGRCEEVCPTAaIKLSQEF-----ELAVW 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352185129 447 RqeeKRAAEAKARFEARQ------------------ARLEREKAARLERHK 479
Cdd:PRK12387  102 K---KEDLLQQSEFALCNcrvcgrpfavqkeidyaiALLKHNGDSRAENHR 149
PRK13596 PRK13596
NADH-quinone oxidoreductase subunit NuoF;
117-199 3.03e-05

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 237441  Cd Length: 433  Bit Score: 47.27  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 117 CWiprDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKL----QGGGDKIETLIINAAECEPYITADDRLMQDCAAQ 192
Cdd:PRK13596   28 DW---DGTKAILDKGRDWIIEEMKASGLRGRGGAGFPTGLKWsfmpKESDGRPHYLVVNADESEPGTCKDRDILRHDPHK 104


                  ....*..
gi 1352185129 193 VVEGIRI 199
Cdd:PRK13596  105 LIEGCLI 111
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 377-430 3.22e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 43.92  E-value: 3.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1352185129 377 CIRCSACADACPADLLpqqlywfSKGQQHDKATTHNI--ADCIECGACAWVCPSNI 430
Cdd:cd10549     8 CIGCGICVKACPTDAI-------ELGPNGAIARGPEIdeDKCVFCGACVEVCPTGA 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 377-427 6.06e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.58  E-value: 6.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352185129 377 CIRCSACADACPADLLpqqlyWFSKGqqhdKATTHNiADCIECGACAWVCP 427
Cdd:COG2221    17 CIGCGLCVAVCPTGAI-----SLDDG----KLVIDE-EKCIGCGACIRVCP 57
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
373-430 2.68e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 43.51  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1352185129 373 EEQSCIRCSACADACPADLLPqqlywfSKGQQHDkatthniADCIECGACAWVCPSNI 430
Cdd:COG0348   208 DRGDCIDCGLCVKVCPMGIDI------RKGEINQ-------SECINCGRCIDACPKDA 252
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 369-436 3.85e-04

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 42.05  E-value: 3.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 369 GEPQ-EEQSCIRCSACADACPADLLPQQlywfSKGQQHDKATTHNIADCIECGACAWVCPSN-IPLVQYF 436
Cdd:PRK08222   31 GKPDlMPSQCIACGACTCACPANALTIQ----TDDQQNSRTWQLYLGRCIYCGRCEEVCPTRaIQLTNNF 96
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
370-477 4.19e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 41.41  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 370 EPQEEQSCIRCSACADACPADLLpqQLYWfSKGQQHDKATTH---NIADCIECGACAWVCPSN-IPLVQYFrqekaEIAa 445
Cdd:PRK05888   53 DPNGEERCIACKLCAAICPADAI--TIEA-AEREDGRRRTTRydiNFGRCIFCGFCEEACPTDaIVETPDF-----ELA- 123

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1352185129 446 irqEEKRAAEA--KARFEARQARLEREKAARLER 477
Cdd:PRK05888  124 ---TETREELIydKEKLLANGDRVEREIAPGKAA 154
PTZ00121 PTZ00121
MAEBL; Provisional
 434-652 5.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  434 QYFRQEKAEiAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQPiVI 513
Cdd:PTZ00121  1207 KAEEERKAE-EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE-LK 1284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  514 KAGERPDNSAIIAAREARKA-QARAKQAELQQTNDAATVADPRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVE 592
Cdd:PTZ00121  1285 KAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  593 AAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQVDPRK 652
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 363-449 7.70e-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: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 363 PSANELGEpqEEQSCIRCSACADACPADL-LPQQLYWFSKGQQHDKATTHNIadCIECGACAWVCPSNIPLVQYFrqEKA 441
Cdd:cd01916   355 PTDEEFQE--LAAKCTDCGWCTRACPNSLrIKEAMEAAKEGDFSGLADLFDQ--CVGCGRCEQECPKEIPIINMI--EKA 428


                  ....*...
gi 1352185129 442 EIAAIRQE 449
Cdd:cd01916   429 ARERIKEE 436
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 376-429 8.29e-04

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 38.77  E-value: 8.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 376 SCIRCSACADACPADLLPQQLYWFSKGQQhdKATTHNIADCIECGACAWVCPSN 429
Cdd:PLN00071   10 TCIGCTQCVRACPTDVLEMIPWDGCKAKQ--IASAPRTEDCVGCKRCESACPTD 61
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
373-446 8.71e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.54  E-value: 8.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352185129 373 EEQSCIRCSACADACPadllpqqlywFSKGQQHDKATTH-NIADCIECGACAWVCPSNIPLVQYFRQE--KAEIAAI 446
Cdd:COG1148   494 DPEKCTGCGRCVEVCP----------YGAISIDEKGVAEvNPALCKGCGTCAAACPSGAISLKGFTDDqiLAQIDAL 560
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 375-440 1.04e-03

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: 40.36  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 375 QSCIRCS--ACADACPADLLpqqlywfskgqQHDK--ATTHNIADCIECGACAWVCPSNIPlvQYFRQEK 440
Cdd:cd10562    68 RQCMHCTdaACVKVCPTGAL-----------YKTEngAVVVDEDKCIGCGYCVAACPFDVP--RYDETTN 124
PRK09898 PRK09898
ferredoxin-like protein;
373-428 1.14e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 40.97  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1352185129 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 1.18e-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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 377 CIRCSACADACP---ADLL---PQ---QLYWF---SKGQQHDK-----ATTHNIADCIECGACAWVCPSNIPLvqyfrqE 439
Cdd:COG0479   144 CILCGACVAACPnvwANPDflgPAalaQAYRFaldPRDEETEErlealEDEEGVWRCTTCGNCTEVCPKGIPP------T 217

                          90
                  ....*....|
gi 1352185129 440 KAeIAAIRQE 449
Cdd:COG0479   218 KA-IAKLKRE 226
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 374-427 1.28e-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: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 374 EQSCIRCSACADACPADllpqQLYWfskgqqhdKATTHNIADCIECGACAWVCP 427
Cdd:cd16370    82 KEKCIGCGNCVKACIVG----AIFW--------DEETNKPIICIHCGYCARYCP 123
PTZ00121 PTZ00121
MAEBL; Provisional
 440-684 1.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  440 KAEIAAIRQEEKRAAEAKARFEARQA----RLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAqatqpiVIKA 515
Cdd:PTZ00121  1201 KAEAARKAEEERKAEEARKAEDAKKAeavkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA------AIKA 1274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  516 GERPDNSAIIAAREARKAQARAKQAELQQTNDAATVADPRKTAVEAAIARakarklEQQQANAEPEQQVDPRKAAVEAAI 595
Cdd:PTZ00121  1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA------EEAKKKADAAKKKAEEAKKAAEAA 1348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  596 ARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKREQQPANAE 675
Cdd:PTZ00121  1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE 1428


                   ....*....
gi 1352185129  676 PEEQVDPRK 684
Cdd:PTZ00121  1429 EKKKADEAK 1437
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 377-429 1.57e-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: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352185129 377 CIRCSACADACPADLLpqqlywfskgQQHDKATTHniADCIECGACAWVCPSN 429
Cdd:cd16372    79 CVGCLMCVGFCPEGAM----------FKHEDYPEP--FKCIACGICVKACPTG 119
psaC CHL00065
photosystem I subunit VII
 376-429 1.93e-03

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 37.82  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 376 SCIRCSACADACPADLLPQQLYWFSKGQQhdKATTHNIADCIECGACAWVCPSN 429
Cdd:CHL00065   10 TCIGCTQCVRACPTDVLEMIPWDGCKAKQ--IASAPRTEDCVGCKRCESACPTD 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-652 2.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 437 RQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQpaakdKDAIAAALARVKEKQAQATQpivikag 516
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----LEELEEELAELEEELEELEE------- 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 517 erpDNSAIIAAREARKAQARAKQAELQQTNDAATVADPRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAAIA 596
Cdd:COG1196   338 ---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1352185129 597 RAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQVDPRK 652
Cdd:COG1196   415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
ndhI CHL00014
NADH dehydrogenase subunit I
 373-429 2.36e-03

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 39.36  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1352185129 373 EEQSCIRCSACADACPADlLPQQLYWFSKGQQHDKATTHNI--ADCIECGACAWVCPSN 429
Cdd:CHL00014   57 EFDKCIACEVCVRVCPID-LPVVDWKLETDIRKKRLLNYSIdfGVCIFCGNCVEYCPTN 114
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 377-429 2.61e-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: 37.34  E-value: 2.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352185129 377 CIRCSACADACPADLLpqqlywfskGQQHDKATTHNIADCIECGACAWVCPSN 429
Cdd:COG1144    32 CIGCGLCWIVCPDGAI---------RVDDGKYYGIDYDYCKGCGICAEVCPVK 75
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 376-431 2.97e-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: 2.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352185129 376 SCIRCS--ACADACPAdllPQQLYWFSKGQ---QHDKatthniadCIECGACAWVCPSNIP 431
Cdd:cd10558    69 GCMHCAdpGCLKACPS---PGAIVQYANGIvdfQSDK--------CIGCGYCIKGCPFDIP 118
PTZ00121 PTZ00121
MAEBL; Provisional
 438-681 3.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  438 QEKAEIAAIRQEEKRAAEaKARFEARQARLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQpiVIKAGE 517
Cdd:PTZ00121  1456 AKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE--AKKAEE 1532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  518 RPDNSAIIAAREARKAQARAKQAELQQTNDAATVADPRKT----------------AVEAAIARAKARKLEQQQANAEPE 581
Cdd:PTZ00121  1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAeedknmalrkaeeakkAEEARIEEVMKLYEEEKKMKAEEA 1612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  582 QQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQvdpRKAAVEAAIARAKARKLEQQQANAEPEQqvdpRKAAVEAAIAR 661
Cdd:PTZ00121  1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKAEEENKIKAAEEAKKAEEDK----KKAEEAKKAEE 1685

                          250       260
                   ....*....|....*....|
gi 1352185129  662 AKARKREQQPANAEPEEQVD 681
Cdd:PTZ00121  1686 DEKKAAEALKKEAEEAKKAE 1705
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 437-479 4.11e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.48  E-value: 4.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1352185129 437 RQEKAEIAAIRQEEKRAAEAKARFEARQARLEREK------AARLERHK 479
Cdd:pfam05672  89 EQREQEEQERLQKQKEEAEAKAREEAERQRQEREKimqqeeQERLERKK 137
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 436-689 4.32e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 436 FRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQpaakdKDAIAAALARVKEKQAQATQPIVIKA 515
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-----LEELEEELEEAEEELEEAEAELAEAE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 516 GERPDNSAIIAAREARKAQARAKQAELQQTNDAATVADPRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAAI 595
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 596 ARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQVDPRKAAVEAAIARAKARKREQQPANAE 675
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524

                         250
                  ....*....|....
gi 1352185129 676 PEEQVDPRKAAVEA 689
Cdd:COG1196   525 AVAVLIGVEAAYEA 538
PTZ00304 PTZ00304
NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional
 121-196 4.63e-03

NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional


Pssm-ID: 185547 [Multi-domain]  Cd Length: 461  Bit Score: 40.15  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 121 RDGWadYRTRS-----REELIERIHQFGVAGLGGAGFPTGVKLQ-----GGGDKIETLIINAAECEPYITADDRLMQDCA 190
Cdd:PTZ00304   46 RGDW--YRTKDillkgHDWIIDEIKKSGLRGRGGAGFPSGLKWSfmpkvKPDGRPSYLVVNADESEPGTCKDREIMRHDP 123


                  ....*.
gi 1352185129 191 AQVVEG 196
Cdd:PTZ00304  124 HKLVEG 129
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 375-430 5.08e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 37.99  E-value: 5.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352185129 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 5.30e-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: 5.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352185129 376 SCIRCS--ACADACPADLlpqqlywFSKgqQHDKATTHNIADCIECGACAWVCP 427
Cdd:cd16371    53 SCNHCEnpACVKVCPTGA-------ITK--REDGIVVVDQDKCIGCGYCVWACP 97
PTZ00121 PTZ00121
MAEBL; Provisional
 444-652 6.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  444 AAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQpiviKAGERPDNSA 523
Cdd:PTZ00121  1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK----KKAEEAKKAA 1345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  524 IIAAREARKAQARAKQAELQQTNDAATVADPRKTAVEAAIARAKARKLEQQQANAEPEQQV--DPRKAAVEAAIARAKAR 601
Cdd:PTZ00121  1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKK 1425

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1352185129  602 KLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEQQVDPRK 652
Cdd:PTZ00121  1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
374-451 6.21e-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: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 374 EQSCIRCSACADACPADLLpqqlywfskGQQHDKATTHNiADCIECGACAWVCPSNiplvqyFRQEKAEI----AAIRQE 449
Cdd:COG4624    90 KEKCKNCYPCVRACPVKAI---------KVDDGKAEIDE-EKCISCGQCVAVCPFG------AITEKSDIekvkKALKDP 153


                  ..
gi 1352185129 450 EK 451
Cdd:COG4624   154 EK 155
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 375-429 6.52e-03

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 39.11  E-value: 6.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1352185129 375 QSCIRCSACADACPAdllPQQLYWFSKGQQHDKATTHniADCIECGACAWVCPSN 429
Cdd:PRK09477  208 QKCTRCMDCFHVCPE---PQVLRPPLKGKQSPSQVTS--GDCITCGRCIDVCSED 257
PTZ00121 PTZ00121
MAEBL; Provisional
 438-588 8.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129  438 QEKAEIAAIRQEE--KRAAEAKARFEARQARLEREKAARLERHKSAAVQPAAKDKDAIAAalARVKEKQAQATQPIVIKA 515
Cdd:PTZ00121  1363 EEKAEAAEKKKEEakKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEKKKADEAKKKA 1440

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352185129  516 GE-RPDNSAIIAAREARKAQARAKQAELQQTNDAAtvadpRKTAVEAAIARAKARKLEQQQANAEPEQQVDPRK 588
Cdd:PTZ00121  1441 EEaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA-----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 358-429 9.64e-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: 36.93  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185129 358 NCLLAPSANELGEPQEEQSCIR---------------CSACADACPADLL---PQQLYWFSKgqqhdkatthniADCIEC 419
Cdd:cd16372    15 QCEEACSKTFFKEEDREKSCIRiteteggyainvcnqCGECIDVCPTGAItrdANGVVMINK------------KLCVGC 82

                          90
                  ....*....|
gi 1352185129 420 GACAWVCPSN 429
Cdd:cd16372    83 LMCVGFCPEG 92
napH_ TIGR02163
ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, ...
 372-430 9.66e-03

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


Pssm-ID: 274004 [Multi-domain]  Cd Length: 255  Bit Score: 38.49  E-value: 9.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1352185129 372 QEEQSCIRCSACADACPAdllPQQLYWFSKGQQHDKATThniADCIECGACAWVCPSNI 430
Cdd:TIGR02163 198 SDREKCTNCMDCFNVCPE---PQVLRMPLKKGGSTLVLS---GDCTLCGRCIDVCHEDV 250
 
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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