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Conserved domains on  [gi|2104022124|ref|WP_224451645|]
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electron transport complex subunit RsxC [Hafnia paralvei]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-550 0e+00

electron transport complex protein RnfC; Provisional


:

Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 896.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124   7 ALKKDKLWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAGR-NLPVHAST 85
Cdd:PRK05035    1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRmSLPVHAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  86 SGVISAISPQVTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLEGGYGKV 165
Cdd:PRK05035   81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 166 ETLIINAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGHDDIKLRVIPTKYPS 245
Cdd:PRK05035  161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 246 GGAKQLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLLQAG 325
Cdd:PRK05035  241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 326 EFEAQNRtPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEAEEEQACIRCSQCADACPAGLLPQQLYWFSRGKE 405
Cdd:PRK05035  321 GFKPDAD-QRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 406 HEKARQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIKSADQEAARAAQAKERFEARQARLAREKAARELRHKQSAVN 485
Cdd:PRK05035  400 HDKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEA 479

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 486 VSESDQSAVQAAVARVKQRQEQASGISSIHPfnNEQEDNS-IRAAREARKALARERKQEIASDTTA 550
Cdd:PRK05035  480 RAAKDKDAVAAALARVKAKKAAATQPIVIKA--GARPDNSaVIAAREARKAQARARQAEKQAAAAA 543
 
Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-550 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 896.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124   7 ALKKDKLWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAGR-NLPVHAST 85
Cdd:PRK05035    1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRmSLPVHAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  86 SGVISAISPQVTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLEGGYGKV 165
Cdd:PRK05035   81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 166 ETLIINAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGHDDIKLRVIPTKYPS 245
Cdd:PRK05035  161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 246 GGAKQLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLLQAG 325
Cdd:PRK05035  241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 326 EFEAQNRtPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEAEEEQACIRCSQCADACPAGLLPQQLYWFSRGKE 405
Cdd:PRK05035  321 GFKPDAD-QRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 406 HEKARQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIKSADQEAARAAQAKERFEARQARLAREKAARELRHKQSAVN 485
Cdd:PRK05035  400 HDKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEA 479

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 486 VSESDQSAVQAAVARVKQRQEQASGISSIHPfnNEQEDNS-IRAAREARKALARERKQEIASDTTA 550
Cdd:PRK05035  480 RAAKDKDAVAAALARVKAKKAAATQPIVIKA--GARPDNSaVIAAREARKAQARARQAEKQAAAAA 543
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 12-463 0e+00

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


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 722.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  12 KLWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAG-RNLPVHASTSGVIS 90
Cdd:COG4656     2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGfVSAPVHAPVSGTVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  91 AISPqvTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLEGGYG-KVETLI 169
Cdd:COG4656    82 AIEP--APHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDkKIDTLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 170 INAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGHDDIKLRVIPTKYPSGGAK 249
Cdd:COG4656   160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDDIEVVVLPTKYPQGGEK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 250 QLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLL-QAGEFE 328
Cdd:COG4656   240 QLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLeQAGGFK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 329 AQNrtPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEaEEEQACIRCSQCADACPAGLLPQQLYWFSRGKEHEK 408
Cdd:COG4656   320 EEP--GKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVPP-PEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDK 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 409 ARQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIKSADQEAARAAQAKERFEA 463
Cdd:COG4656   397 AEEYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARERFEA 451
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 13-445 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: 615.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  13 LWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAG-RNLPVHASTSGVISA 91
Cdd:TIGR01945   1 LFTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGfVSAPIHAPTSGTVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  92 ISPQVTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLE-GGYGKVETLII 170
Cdd:TIGR01945  81 IEERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNpPPEKKIETLII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 171 NAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGhDDIKLRVIPTKYPSGGAKQ 250
Cdd:TIGR01945 161 NGAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGG-YNIKVRVLPTKYPQGGEKQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 251 LTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLL-QAGEFEa 329
Cdd:TIGR01945 240 LIYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILaFCGGFR- 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 330 qNRTPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEaEEEQACIRCSQCADACPAGLLPQQLYWFSRGKEHEKA 409
Cdd:TIGR01945 319 -EKPERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPE-SPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEA 396

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2104022124 410 RQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIK 445
Cdd:TIGR01945 397 EEHNLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLR 432
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
152-283 3.92e-50

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 171.93  E-value: 3.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 152 FPTGNKLEGGYG-KVETLIINAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKG 230
Cdd:pfam01512  14 FPTHVKLSPPPKkKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEKPEAIAALEKAIAE 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2104022124 231 ----HDDIKLRVIPTKYPSGGAKQLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIK 283
Cdd:pfam01512  94 araaGFDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 359-429 1.07e-05

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: 45.40  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 359 NCILAPSKNEFDEAEEEQACIR---------------CSQCADACPAGLL---PQQLYWFSRGK---------------- 404
Cdd:cd16372    15 QCEEACSKTFFKEEDREKSCIRiteteggyainvcnqCGECIDVCPTGAItrdANGVVMINKKLcvgclmcvgfcpegam 94

                          90       100
                  ....*....|....*....|....*.
gi 2104022124 405 -EHEKARQHhlFDCIECGACAYVCPS 429
Cdd:cd16372    95 fKHEDYPEP--FKCIACGICVKACPT 118
 
Name Accession Description Interval E-value
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 7-550 0e+00

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 896.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124   7 ALKKDKLWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAGR-NLPVHAST 85
Cdd:PRK05035    1 QIRKGKLWDFPGGIHPPEMKTQSNGTPIRQAPLPQRLVIPLKQHIGAEGELCVKVGDRVLKGQPLTQGDGRmSLPVHAPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  86 SGVISAISPQVTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLEGGYGKV 165
Cdd:PRK05035   81 SGTVVAIEPHPTAHPSGLAELCVVIEPDGEDRWIERQPWADYRQLSPEELIERIRQAGIAGLGGAGFPTAVKLQPGGDKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 166 ETLIINAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGHDDIKLRVIPTKYPS 245
Cdd:PRK05035  161 ETLIINGAECEPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDIRVRVIPTKYPS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 246 GGAKQLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLLQAG 325
Cdd:PRK05035  241 GGEKQLIQILTGKEVPSGGRPADIGVLMQNVGTAYAIKRAVIDGEPLIERVVTLTGEAVARPGNVWARLGTPVRHLLNQA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 326 EFEAQNRtPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEAEEEQACIRCSQCADACPAGLLPQQLYWFSRGKE 405
Cdd:PRK05035  321 GFKPDAD-QRVIMGGPMMGFTLPSLDVPVVKTTNCLLAPSATELPPPPPEQPCIRCGACADACPASLLPQQLYWFAKAEE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 406 HEKARQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIKSADQEAARAAQAKERFEARQARLAREKAARELRHKQSAVN 485
Cdd:PRK05035  400 HDKAQEYNLFDCIECGACAYVCPSNIPLVQYYRQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEA 479

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 486 VSESDQSAVQAAVARVKQRQEQASGISSIHPfnNEQEDNS-IRAAREARKALARERKQEIASDTTA 550
Cdd:PRK05035  480 RAAKDKDAVAAALARVKAKKAAATQPIVIKA--GARPDNSaVIAAREARKAQARARQAEKQAAAAA 543
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 12-463 0e+00

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


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 722.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  12 KLWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAG-RNLPVHASTSGVIS 90
Cdd:COG4656     2 KLWTFKGGIHPPENKELSADKPIERLPLPEKLVIPLQQHIGAPAEPLVKVGDKVLKGQLIAEADGfVSAPVHAPVSGTVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  91 AISPqvTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLEGGYG-KVETLI 169
Cdd:COG4656    82 AIEP--APHPSGLKVLCIVIEPDGEDEWIELEPLADYEDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDkKIDTLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 170 INAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGHDDIKLRVIPTKYPSGGAK 249
Cdd:COG4656   160 INGAECEPYLTCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDDIEVVVLPTKYPQGGEK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 250 QLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLL-QAGEFE 328
Cdd:COG4656   240 QLIKALTGREVPSGGLPADVGVVVQNVGTAYAIYRAVRDGKPLIERVVTVTGDAVKEPGNLLVRIGTPVSDLLeQAGGFK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 329 AQNrtPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEaEEEQACIRCSQCADACPAGLLPQQLYWFSRGKEHEK 408
Cdd:COG4656   320 EEP--GKLIMGGPMMGFALPSLDVPVTKGTNGILALTKEEVPP-PEEQPCIRCGRCVDACPMGLLPQQLYWYARAGDFDK 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 409 ARQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIKSADQEAARAAQAKERFEA 463
Cdd:COG4656   397 AEEYNLMDCIECGCCSYVCPSKIPLVQYIRLAKAEIRARRREKQKAEEARERFEA 451
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 13-445 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: 615.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  13 LWDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAG-RNLPVHASTSGVISA 91
Cdd:TIGR01945   1 LFTFKGGIHPPENKELSNDKPIEQLPLPQELIVPLSQHIGAPAEPIVKVGDKVLKGQKIAKADGfVSAPIHAPTSGTVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  92 ISPQVTAHPSGLSEPCVTLIPDNQDRWGELHPVANFQAESPLTLTHLIHQAGIAGLGGAGFPTGNKLE-GGYGKVETLII 170
Cdd:TIGR01945  81 IEERVSPHASGLPVPAIVIEPDGEDEWIELEPIPDFENLSPEEILEKIRAAGIVGLGGATFPTHVKLNpPPEKKIETLII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 171 NAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKGhDDIKLRVIPTKYPSGGAKQ 250
Cdd:TIGR01945 161 NGAECEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKALGG-YNIKVRVLPTKYPQGGEKQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 251 LTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLL-QAGEFEa 329
Cdd:TIGR01945 240 LIYALTGREVPSGGLPADIGVVVQNVGTAFAIYEAVVNGKPLIERVVTVTGDAIRRPKNLWVLIGTPVSDILaFCGGFR- 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 330 qNRTPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFDEaEEEQACIRCSQCADACPAGLLPQQLYWFSRGKEHEKA 409
Cdd:TIGR01945 319 -EKPERLIMGGPMMGLALPSLDVPVTKGTSGILALDKEETPE-SPEKPCIRCGKCVQVCPMNLLPQQLNWLALADEFDEA 396

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2104022124 410 RQHHLFDCIECGACAYVCPSSIPLVQYYRQEKAEIK 445
Cdd:TIGR01945 397 EEHNLMDCIECGCCSYVCPSNIPLVQYIRQAKAKLR 432
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
152-283 3.92e-50

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 171.93  E-value: 3.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 152 FPTGNKLEGGYG-KVETLIINAAECEPYITADDRLMREHADEIILGCEILGHILTPKRTLIGIEDNKPEAIAALKKALKG 230
Cdd:pfam01512  14 FPTHVKLSPPPKkKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIGIRDEKPEAIAALEKAIAE 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2104022124 231 ----HDDIKLRVIPTKYPSGGAKQLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIK 283
Cdd:pfam01512  94 araaGFDIEVHRGAGAYPCGEEKALIYSLTGRGVPRGKPPADVGVVVNNVETLAAVP 150
RnfC_N pfam13375
RnfC Barrel sandwich hybrid domain; This domain is part of the barrel sandwich hybrid ...
 14-115 1.34e-36

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: 132.68  E-value: 1.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124  14 WDFKGGIHPPEMKHPSSHVPLRHVSLPPMLIIPLQQHIGQEGELLVKVGQHVMKGQPLTRGAG-RNLPVHASTSGVISAI 92
Cdd:pfam13375   1 WTFKGGIHPPENKELSKDKPIEKLPLPKELVIPLSQHIGAPAEPIVKVGDRVLKGQKIAEADGfVSAPVHASVSGTVKAI 80

                          90       100
                  ....*....|....*....|...
gi 2104022124  93 SPQVTAHPSGLsePCVTLIPDNQ 115
Cdd:pfam13375  81 EPRPVPHGSGV--NCIVIENDGE 101
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 378-431 1.70e-10

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: 56.77  E-value: 1.70e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 378 CIRCSQCADACPAGLLPQQLYWFSRGKEHEkarQHHLFDCIECGACAYVCPSSI 431
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTV---VIDPERCVGCGACVAVCPTGA 51
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 374-428 1.75e-10

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 56.88  E-value: 1.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 374 EEQACIRCSQCADACPAGLLPQQLYwfsRGKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:pfam13237   5 DPDKCIGCGRCTAACPAGLTRVGAI---VERLEGEAVRIGVWKCIGCGACVEACP 56
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 375-428 5.99e-10

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 55.49  E-value: 5.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 375 EQACIRCSQCADACPAGLlpqqlywFSRGKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:COG1146     7 TDKCIGCGACVEVCPVDV-------LELDEEGKKALVINPEECIGCGACELVCP 53
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 377-432 7.71e-10

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


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 55.16  E-value: 7.71e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 377 ACIRCSQCADACPAGLL----PQQL----YWFSRGKEHEKARqhhLFDCIECGACAYVCPSSIP 432
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLngdePKKLmraaYLGDLEELQANKV---ANLCSECGLCEYACPMGLD 61
NapF COG1145
Ferredoxin [Energy production and conversion];
211-428 1.39e-09

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 59.35  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 211 IGIEDNKPEAIAALKKALKGHDDIKLRVIPTKYPSGGAKQLTKILTGMEVPFGKHSASIGVLMQNIGTVYAIKRAIINGE 290
Cdd:COG1145    21 VVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIVRVGIAAADLNLKAVALVL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 291 PLIERVVTLTGELMKKpgnvwARLGTPVKHLLQAGEFEAQNRTPMVIMGGPLMGFTLAHLSVPIVKISNCILAPSKNEFD 370
Cdd:COG1145   101 LLALAVAGAAKRLIIS-----AVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2104022124 371 EAE-EEQACIRCSQCADACPAGLLpqqlywfsRGKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:COG1145   176 KAViDAEKCIGCGLCVKVCPTGAI--------RLKDGKPQIVVDPDKCIGCGACVKVCP 226
PRK06991 PRK06991
electron transport complex subunit RsxB;
374-550 8.94e-09

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 57.11  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 374 EEQACIRCSQCADACP----AGllpqqlywfsrgkeheKARQHH--LFD-CIECGACAYVCP-SSIPLVQYYRQEKAEik 445
Cdd:PRK06991   83 DEQLCIGCTLCMQACPvdaiVG----------------APKQMHtvLADlCTGCDLCVPPCPvDCIDMVPVTGERTGW-- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 446 sADQEAARAAQAKERFEARQARLAREKAARELR--------------HKQSAVNVSESD-----QSAVQAAVARVKQRQE 506
Cdd:PRK06991  145 -DAWSQAQADAARARHDARQARLRREREAAEARaaaraaasaaaaaaEASAAAAPAADDaeakkRAIIAAALERARKKKE 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2104022124 507 QASGiSSIHPFNNEQEDNSIRAAREARKALARERKQEIASDTTA 550
Cdd:PRK06991  224 ELAA-QGAGPKNTEGVSAAVQAQIDAAEARRKRLAEQRDAPDDA 266
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 377-431 4.03e-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: 4.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 377 ACIRCSQCADACPAGLLPQQLYWFSRGKEHEKARQ---------HHLFDCIECGACAYVCPSSI 431
Cdd:pfam13183   1 RCIRCGACLAACPVYLVTGGRFPGDPRGGAAALLGrlealeglaEGLWLCTLCGACTEVCPVGI 64
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 374-429 5.01e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 50.11  E-value: 5.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 374 EEQACIRCSQCADACPAGLLpqqlywfsrGKEHEKARQHHLFDCIECGACAYVCPS 429
Cdd:COG1149     9 DEEKCIGCGLCVEVCPEGAI---------KLDDGGAPVVDPDLCTGCGACVGVCPT 55
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 375-428 5.94e-08

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 50.13  E-value: 5.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 375 EQACIRCSQCADACPAGLLPQqlywfsRGKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITI------EDGEPGKVYVIDPDKCIGCGLCVEVCP 48
Fer4_9 pfam13187
4Fe-4S dicluster domain;
377-428 3.35e-07

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 47.55  E-value: 3.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2104022124 377 ACIRCSQCADACPAGLlpqqlywFSRGKEHEKARQHHLFD-CIECGACAYVCP 428
Cdd:pfam13187   1 KCTGCGACVAACPAGA-------IVPDLVGQTIRGDIAGLaCIGCGACVDACP 46
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 375-430 4.00e-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: 4.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 375 EQACIRCSQCADACPAGLLpqqlywfsrgKEHEKARQHHLFDCIECGACAYVCPSS 430
Cdd:COG4231    21 EDKCTGCGACVKVCPADAI----------EEGDGKAVIDPDLCIGCGSCVQVCPVD 66
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 364-433 4.28e-07

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: 51.29  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 364 PSKNEFDEAEEEQACIRCSQCADAC-----------PAGLLpqQLYWF---SRGKEHEK-----ARQHHLFDCIECGACA 424
Cdd:COG0479   130 QSPEDREKADDLAECILCGACVAACpnvwanpdflgPAALA--QAYRFaldPRDEETEErlealEDEEGVWRCTTCGNCT 207


                  ....*....
gi 2104022124 425 YVCPSSIPL 433
Cdd:COG0479   208 EVCPKGIPP 216
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
378-428 5.06e-07

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 47.48  E-value: 5.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2104022124 378 CIRCSQCADACPAGLLPQQLY-------WFSRGKEHEKA-----RQHHLFDCIECGACAYVCP 428
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGvldarrcISYLTIEKKGLipdelRCLLGNRCYGCDICQDVCP 63
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
375-428 1.85e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.88  E-value: 1.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 375 EQACIRCSQCADACPAGLLpqqlywfsrgKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:COG2768    10 EEKCIGCGACVKVCPVGAI----------SIEDGKAVIDPEKCIGCGACIEVCP 53
SLBB pfam10531
SLBB domain;
296-345 2.09e-06

SLBB domain;


Pssm-ID: 463136 [Multi-domain]  Cd Length: 56  Bit Score: 45.35  E-value: 2.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 296 VVTLTGElMKKPGNVWARLGTPVKHLL-QAGEF-----EAQNRTPMVIMGGPLMGF 345
Cdd:pfam10531   1 VVTVTGE-VKRPGNYEVPIGTTLSDLIeLAGGFtddadLDINLRRLKRPGGPMMGI 55
PRK05352 PRK05352
Na(+)-translocating NADH-quinone reductase subunit A; Provisional
 279-439 2.59e-06

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


Pssm-ID: 235426 [Multi-domain]  Cd Length: 448  Bit Score: 50.56  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 279 VYAIKRAIINGEPLIERVVTLTGELMKKPGNVWARLGTPVKHLLQAGEFEAQNRtpmVIMGGPLMGFTLA---------H 349
Cdd:PRK05352  246 VIAIGKLFLTGELYTERVVALAGPAVKKPRLVRTRLGASLSELTAGELKAGDNR---VISGSVLTGRTAKgphaylgryH 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 350 LSVPIV-----------------KISN------CILAPSKNEFDEAE--EEQACIRCSQCADACPAGLLPQQLYwfsRG- 403
Cdd:PRK05352  323 NQVSVLpegrerelfgwlrpgfnKFSVtrtylsHLFKKKLFNFTTNTngSERAMVPIGNYERVMPLDILPTQLL---RAl 399

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2104022124 404 --KEHEKARQHHLFDCIE--CGACAYVCPSSIPLVQYYRQ 439
Cdd:PRK05352  400 ivGDTDEAQALGALELDEedLALCTFVCPGKYEYGPILRD 439
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 375-428 3.16e-06

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: 45.81  E-value: 3.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 375 EQACIRCSQCADACPAGLLpqqlywfsrGKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:COG1144    29 EDKCIGCGLCWIVCPDGAI---------RVDDGKYYGIDYDYCKGCGICAEVCP 73
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 359-429 1.07e-05

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: 45.40  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 359 NCILAPSKNEFDEAEEEQACIR---------------CSQCADACPAGLL---PQQLYWFSRGK---------------- 404
Cdd:cd16372    15 QCEEACSKTFFKEEDREKSCIRiteteggyainvcnqCGECIDVCPTGAItrdANGVVMINKKLcvgclmcvgfcpegam 94

                          90       100
                  ....*....|....*....|....*.
gi 2104022124 405 -EHEKARQHhlFDCIECGACAYVCPS 429
Cdd:cd16372    95 fKHEDYPEP--FKCIACGICVKACPT 118
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 375-447 1.14e-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: 45.47  E-value: 1.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2104022124 375 EQACIRCSQCADACPAGLLpqqlywfSRGKEHEKARqHHLFD---CIECGACAYVCP-SSIPLVQYYRQEKAEIKSA 447
Cdd:cd10549     5 PEKCIGCGICVKACPTDAI-------ELGPNGAIAR-GPEIDedkCVFCGACVEVCPtGAIELTPEGKEYVPKEKEA 73
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 361-490 1.22e-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: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 361 ILAPSKNEFDEAEEeqACIRCSQCADACPA-GLLPQQLYwfS-RGK--------------EHEKARQHHLFDCIECGACA 424
Cdd:COG0247    65 LKTLPWKELLDALD--ACVGCGFCRAMCPSyKATGDEKD--SpRGRinllrevlegelplDLSEEVYEVLDLCLTCKACE 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 425 YVCPSSIPLvqyyrqekAEIKsadqeaaraAQAKERFEARQARLAREKAARELRHKQSAVNVSESD 490
Cdd:COG0247   141 TACPSGVDI--------ADLI---------AEARAQLVERGGRPLRDRLLRTFPDRVPAADKEGAE 189
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 377-428 1.30e-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: 45.08  E-value: 1.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 377 ACIRCSQCADACPAGLLPQQLYWFSRGKEHEKArqhhLFD---CIECGACAYVCP 428
Cdd:cd10549    41 KCVFCGACVEVCPTGAIELTPEGKEYVPKEKEA----EIDeekCIGCGLCVKVCP 91
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 370-429 1.96e-05

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 45.32  E-value: 1.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 370 DEAEEEQACIRCSQCADACPAGLLpqQLYWFSRGKehEKARQHHL-FD---CI-ECGACAYVCPS 429
Cdd:cd16373     8 DEEEFLALCIRCGLCVEACPTGVI--QPAGLEDGL--EGGRTPYLdPRegpCDlCCDACVEVCPT 68
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 375-428 2.60e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 42.73  E-value: 2.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2104022124 375 EQACIRCSQCADACPAGLLpqqlyWFSRGK---EHEKarqhhlfdCIECGACAYVCP 428
Cdd:COG2221    14 EEKCIGCGLCVAVCPTGAI-----SLDDGKlviDEEK--------CIGCGACIRVCP 57
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 370-429 3.15e-05

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: 44.16  E-value: 3.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2104022124 370 DEAEEEQACIRCSQCADACPAGLL-------PQqlYWFSRGkehekarqhhlfDCIECGACAYVCPS 429
Cdd:cd10564     7 DEALFLDLCTRCGDCVEACPEGIIvrgdggfPE--LDFSRG------------ECTFCGACAEACPE 59
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 373-428 4.01e-05

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: 43.56  E-value: 4.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 373 EEEQACIRCSQCADACPAGLLPQQLYWFSRGKEHEKARQHHLFDCIECGACAYVCP 428
Cdd:TIGR01971  40 NGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEINFGRCIFCGLCEEACP 95
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
374-429 5.74e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 45.44  E-value: 5.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 374 EEQACIRCSQCADACPAGLLPQQLYWFSrgkehekarqhhlFDCIECGACAYVCPS 429
Cdd:COG0348   208 DRGDCIDCGLCVKVCPMGIDIRKGEINQ-------------SECINCGRCIDACPK 250
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 433-547 1.63e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 433 LVQYYRQEKAEIKSADQEAARAAQAKERFEA---------RQARLAREKAARELRHKQSAVNVSESDQSAVQAAVARVKQ 503
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAelaeleaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2104022124 504 RQEQASgissihpfNNEQEDNSIRAAREARKALARERKQEIASD 547
Cdd:COG1196   310 RRRELE--------ERLEELEEELAELEEELEELEEELEELEEE 345
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 378-431 2.10e-04

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


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 41.09  E-value: 2.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 378 CIRCSQCADACPAGLLpqqlywfSRGKEHEKARQHHLFDCIECGACAYVCPSSI 431
Cdd:TIGR00402  36 CTRCGECASACENNIL-------QLGQQGQPTVEFDNAECDFCGKCAEACPTNA 82
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 378-428 2.97e-04

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: 41.23  E-value: 2.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 378 CIRCSQCADACPAGLLPqqlywFSRGKEH----EKarqhhlfdCIECGACAYVCP 428
Cdd:cd10549    80 CIGCGLCVKVCPVDAIT-----LEDELEIvidkEK--------CIGCGICAEVCP 121
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
375-428 5.65e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 43.09  E-value: 5.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 375 EQACIRCSQCADACPAGLLpqqlywfsrGKEHEKARQHHLfDCIECGACAYVCP 428
Cdd:COG4624    90 KEKCKNCYPCVRACPVKAI---------KVDDGKAEIDEE-KCISCGQCVAVCP 133
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 366-429 5.87e-04

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 41.28  E-value: 5.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 366 KNEFDEAEeeqaCIRCSQCADACPAGLLPQQlywfsrGKEHEKARQHHLF--DCIECGACAYVCPS 429
Cdd:PRK08222   32 KPDLMPSQ----CIACGACTCACPANALTIQ------TDDQQNSRTWQLYlgRCIYCGRCEEVCPT 87
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
368-428 6.18e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 41.02  E-value: 6.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2104022124 368 EFDEAEEEQaCIRCSQCADACPAGLLpqQLYWfsrGKEHEKARQHHLFD-----CIECGACAYVCP 428
Cdd:PRK05888   51 RRDPNGEER-CIACKLCAAICPADAI--TIEA---AEREDGRRRTTRYDinfgrCIFCGFCEEACP 110
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
438-540 6.64e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.94  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 438 RQEKAEIKSADQEAARA-AQAKERFEARQARLAREKAARE-----LRHKQSAVNVSESDQsAVQAAVARVKQRQEQasgi 511
Cdd:COG2268   231 EREIETARIAEAEAELAkKKAEERREAETARAEAEAAYEIaeanaEREVQRQLEIAERER-EIELQEKEAEREEAE---- 305

                          90       100
                  ....*....|....*....|....*....
gi 2104022124 512 ssihpfnnEQEDNSIRAAREARKALARER 540
Cdd:COG2268   306 --------LEADVRKPAEAEKQAAEAEAE 326
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
378-432 1.99e-03

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 40.96  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2104022124 378 CIRCSQCAdACPAGL-LPQ--QLY-WFSRGKEHEKARQH--------HLFDCIECGACAYVCPSSIP 432
Cdd:COG1453   283 CTGCGYCM-PCPQGInIPEvfRLYnLARAYGMREYAKERynalgpgaKASACIECGACEERCPQGLD 348
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 359-433 2.23e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 40.20  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 359 NCILAPsKNEFDEAEEEQACIRCSQCADACPAG--------------LLPQqlywfsrGKEHEKARQHHLFDCIE----- 419
Cdd:PRK07570  141 NAIPVP-KEDADRAFDAAACIGCGACVAACPNGsamlftgakvshlaLLPQ-------GQPERARRVRAMVAQMDeegfg 212

                          90
                  ....*....|....*...
gi 2104022124 420 -C---GACAYVCPSSIPL 433
Cdd:PRK07570  213 nCtntGECEAVCPKGISL 230
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
362-450 2.26e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.38  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 362 LAPSKNEFDEaeeeQACIRCSQCADACPAGLLpqqlywfsrgkeHEKARQHHLFD---CIECGACAYVCPSSIPLVQYYR 438
Cdd:COG1148   486 VEPSVAEVDP----EKCTGCGRCVEVCPYGAI------------SIDEKGVAEVNpalCKGCGTCAAACPSGAISLKGFT 549

                          90
                  ....*....|....
gi 2104022124 439 QE--KAEIKSADQE 450
Cdd:COG1148   550 DDqiLAQIDALLVP 563
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 376-509 2.53e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 39.63  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 376 QACIRCSQCADACPAGLLPQQLywfsRGKEHEKARQHHLFDCIECGACAYVCPS-SIPLVQYYrqEKAEIKSAD--QEA- 451
Cdd:PRK12387   38 QQCIGCAACVNACPSNALTVET----DLATGELAWEFNLGRCIFCGRCEEVCPTaAIKLSQEF--ELAVWKKEDllQQSe 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2104022124 452 ---ARAAQAKERFEARQ------ARLAREKAARELRHKQSAVNVSE--SDQSAVQAAVARVKQRQEQAS 509
Cdd:PRK12387  112 falCNCRVCGRPFAVQKeidyaiALLKHNGDSRAENHRESFETCPEckRQKCLVPSDRIELTRHMKEAI 180
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 375-428 3.59e-03

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 38.02  E-value: 3.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 375 EQACIRCSQCADACPAGllpqQLYWfsrGKEHEKArqhhlFDCIECGACAYVCP 428
Cdd:cd16370    82 KEKCIGCGNCVKACIVG----AIFW---DEETNKP-----IICIHCGYCARYCP 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-545 4.22e-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: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 437 YRQEKAEIKSADQEA-------ARAAQAKERFEARQARLAREKAARELRHKQSAVNVSESDQSAVQAAVARVKQRQEQAs 509
Cdd:COG1196   215 YRELKEELKELEAELlllklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL- 293

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2104022124 510 gISSIhpfnnEQEDNSIRAAREARKALARERKQEIA 545
Cdd:COG1196   294 -LAEL-----ARLEQDIARLEERRRELEERLEELEE 323
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 378-437 4.26e-03

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 36.85  E-value: 4.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 378 CIRCSQCADACPAGLLpQQLYWfSRGKEHEKARQHHLFDCIECGACAYVCPSSIPLVQYY 437
Cdd:PLN00071   11 CIGCTQCVRACPTDVL-EMIPW-DGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVY 68
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 375-432 4.99e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 38.39  E-value: 4.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2104022124 375 EQACI------RCSQCADACP-AGLLPQQLYWFSRGKEHEKArqhhlfdCIECGACAYVCPSSIP 432
Cdd:cd16373    90 KDRCLawqggtDCGVCVEACPtEAIAIVLEDDVLRPVVDEDK-------CVGCGLCEYVCPVEPP 147
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 347-434 5.90e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 39.60  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 347 LAHLSVPIVKISNCILAPskNEFDEAEEEQACIRCSQCADACPA--------GLLPQQLYWFSRGKEHEKARQ-----HH 413
Cdd:PRK06259  106 LKSLRNYLQRKNEKITYP--EDIEDIKKLRGCIECLSCVSTCPArkvsdypgPTFMRQLARFAFDPRDEGDREkeafdEG 183

                          90       100
                  ....*....|....*....|.
gi 2104022124 414 LFDCIECGACAYVCPSSIPLV 434
Cdd:PRK06259  184 LYNCTTCGKCVEVCPKEIDIP 204
psaC CHL00065
photosystem I subunit VII
 378-437 6.06e-03

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 36.28  E-value: 6.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104022124 378 CIRCSQCADACPAGLLpQQLYWfsrgkEHEKARQ----HHLFDCIECGACAYVCPSSIPLVQYY 437
Cdd:CHL00065   11 CIGCTQCVRACPTDVL-EMIPW-----DGCKAKQiasaPRTEDCVGCKRCESACPTDFLSVRVY 68
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 369-430 9.13e-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: 37.22  E-value: 9.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104022124 369 FDEAEeeqaCIRCSQCADACPAGLLPQQLywfsrgkehEKARQHHL---FDC-----IECGACAYVCPSS 430
Cdd:cd10564    42 FSRGE----CTFCGACAEACPEGALDPAR---------EAPWPLRAeigDSClalqgVECRSCQDACPTQ 98
 
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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