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Conserved domains on  [gi|527036415|ref|WP_020883157|]
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MULTISPECIES: anaerobic glycerol-3-phosphate dehydrogenase subunit GlpC [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glycerol3P_GlpC super family cl31342
glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are ...
 3-395 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species. [Energy metabolism, Anaerobic]


The actual alignment was detected with superfamily member TIGR03379:

Pssm-ID: 132422 [Multi-domain]  Cd Length: 397  Bit Score: 767.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415    3 DTRFESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAR 82
Cdd:TIGR03379   1 DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKIGDIIARARNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   83 YSTQKP---SLRDAILSHTDLMGSVSTPFAPLVNAATSLKPVRKLLDATLKIDHHRSLPKYSHGTFRRWYTSVAAEQAQY 159
Cdd:TIGR03379  81 YQKKKPnikKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPKYSFGTFRRWYKKNATSQALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  160 TDQVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIVDKGIPVLA 239
Cdd:TIGR03379 161 ERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIANGFPDKAKKQAQFNVKQIEAMVDENGIPVIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  240 TSSTCTFTLRDEYPHLLDVDNTGLREHIELATRFLWRKLDSGQTLPLRELPLKVVYHTPCHMEKMGWSLYTLELLRLIPG 319
Cdd:TIGR03379 241 TSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFMEGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036415  320 LELTVLDSRCCGIAGTYGFKRENYETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSKRCEHPITLLAKAL 395
Cdd:TIGR03379 321 LEVVVLDSQCCGIAGTYGFKSENYETSQAIGKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMAL 396
 
Name Accession Description Interval E-value
glycerol3P_GlpC TIGR03379
glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are ...
 3-395 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species. [Energy metabolism, Anaerobic]


Pssm-ID: 132422 [Multi-domain]  Cd Length: 397  Bit Score: 767.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415    3 DTRFESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAR 82
Cdd:TIGR03379   1 DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKIGDIIARARNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   83 YSTQKP---SLRDAILSHTDLMGSVSTPFAPLVNAATSLKPVRKLLDATLKIDHHRSLPKYSHGTFRRWYTSVAAEQAQY 159
Cdd:TIGR03379  81 YQKKKPnikKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPKYSFGTFRRWYKKNATSQALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  160 TDQVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIVDKGIPVLA 239
Cdd:TIGR03379 161 ERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIANGFPDKAKKQAQFNVKQIEAMVDENGIPVIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  240 TSSTCTFTLRDEYPHLLDVDNTGLREHIELATRFLWRKLDSGQTLPLRELPLKVVYHTPCHMEKMGWSLYTLELLRLIPG 319
Cdd:TIGR03379 241 TSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFMEGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036415  320 LELTVLDSRCCGIAGTYGFKRENYETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSKRCEHPITLLAKAL 395
Cdd:TIGR03379 321 LEVVVLDSQCCGIAGTYGFKSENYETSQAIGKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMAL 396
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
1-396 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 742.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   1 MNDTRFESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRAR 80
Cdd:PRK11168   1 MSDTSFDSCIKCTVCTTACPVARVNPLYPGPKQAGPDGERLRLKDGALYDESLKYCSNCKRCEVACPSGVKIGDIIQRAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  81 ARYSTQK-PSLRDAILSHTDLMGSVSTPFAPLVNAATSLKPVRKLLDATLKIDHHRSLPKYSHGTFRRWYTSVAAEQAQY 159
Cdd:PRK11168  81 AKYVTERgPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLLEKTLGIDHRRPLPKYAFGTFRRWYRKQAAQQAQY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 160 TDQVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVqLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIvDKGIPVLA 239
Cdd:PRK11168 161 KKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEV-LLPKEKCCGLPLIANGFLDKARKQAEFNVESLREAI-EKGIPVIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 240 TSSTCTFTLRDEYPHLLDVDNTGLREHIELATRFLWRKLDSGQTLPLRELPLKVVYHTPCHMEKMGWSLYTLELLRLIPG 319
Cdd:PRK11168 239 TSSSCTLTLRDEYPELLGVDNAGVRDHIEDATEFLRRLLDQGKLLPLKPLPLKVAYHTPCHLEKQGWGLYTLELLRLIPG 318

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036415 320 LELTVLDSRCCGIAGTYGFKRENYETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSKRCEHPITLLAKALG 396
Cdd:PRK11168 319 LEVVVLDSQCCGIAGTYGFKKEKYETSQAIGAPLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALG 395
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 6-396 2.94e-95

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 291.21  E-value: 2.94e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   6 FESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYD------EALKYCINCKRCEVACPSDVKIGDIIQRA 79
Cdd:COG0247   77 LDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDlseevyEVLDLCLTCKACETACPSGVDIADLIAEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  80 RARYSTQkpslrdailshtdlmgsvstpfaplvnaatslkpvrklldatlkidHHRSLPKYSHGTFRRWYTSVAAEQAQy 159
Cdd:COG0247  157 RAQLVER----------------------------------------------GGRPLRDRLLRTFPDRVPAADKEGAE- 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 160 tdqVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVtslrEAIVDKGIP-VL 238
Cdd:COG0247  190 ---VLLFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNI----EALERLGVKaIV 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 239 ATSSTCTFTLRDEYPHLLDVDntgLREHIELATRFLWRKLDSGQtLPLRELPLKVVYHTPCHMEK-MGWSLYTLELLRLI 317
Cdd:COG0247  263 TTCPSCGLTLKDEYPELLGDR---VAFEVLDISEFLAELILEGK-LKLKPLGEKVTYHDPCHLGRgGGVYDAPRELLKAI 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 318 PGLELTVL--DSRCCGIAGTYGFKREnyETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSK---RCEHPITLLA 392
Cdd:COG0247  339 PGVEVVEMpeDSGCCGGAGGYGFEEP--ELSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKEygiEVKHPVELLA 416


                 ....
gi 527036415 393 KALG 396
Cdd:COG0247  417 EALG 420
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 163-248 4.01e-16

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 72.73  E-value: 4.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  163 VAFFHGCYV-NYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIVDkgiPVLATS 241
Cdd:pfam02754   1 VAYFDGCHLgRALYPEPRKALKKVLGALGVEVVILEKQSCCGAGGGFSGKEDVAEALAKRNIDTAEETGAD---AIVTAC 77


                  ....*..
gi 527036415  242 STCTFTL 248
Cdd:pfam02754  78 PGCLLQL 84
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 9-91 9.48e-06

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


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 47.79  E-value: 9.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   9 CIKCTVCTTVCPVSgvnPRYPGPKQAGPDGERLRLKDgaLYDEalkyCINCKRCEVACPSDVKIGDIIQRA-RARYSTQK 87
Cdd:cd01916  367 CTDCGWCTRACPNS---LRIKEAMEAAKEGDFSGLAD--LFDQ----CVGCGRCEQECPKEIPIINMIEKAaRERIKEEK 437


                 ....
gi 527036415  88 PSLR 91
Cdd:cd01916  438 GKMR 441
 
Name Accession Description Interval E-value
glycerol3P_GlpC TIGR03379
glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are ...
 3-395 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, C subunit; Members of this protein family are the membrane-anchoring, non-catalytic C subunit, product of the glpC gene, of a three-subunit, FAD-dependent, anaerobic glycerol-3-phosphate dehydrogenase. GlpC lasks classical hydrophobic transmembrane helices; Cole, et al suggest interaction with the membrane may involve amphipathic helices. GlcC has conserved Cys-containing motifs suggestive of iron-sulfur binding. This complex is found mostly in Escherichia coli and closely related species. [Energy metabolism, Anaerobic]


Pssm-ID: 132422 [Multi-domain]  Cd Length: 397  Bit Score: 767.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415    3 DTRFESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRARAR 82
Cdd:TIGR03379   1 DTSFESCIKCTVCTVYCPVAKANPLYPGPKQAGPDGERLRLKSAELYDEALKYCTNCKRCEVACPSDVKIGDIIARARNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   83 YSTQKP---SLRDAILSHTDLMGSVSTPFAPLVNAATSLKPVRKLLDATLKIDHHRSLPKYSHGTFRRWYTSVAAEQAQY 159
Cdd:TIGR03379  81 YQKKKPnikKLRDFVLSHTDLMGSISTPFAPIVNAITGLKPVKKLLDKTLGVSKHRTLPKYSFGTFRRWYKKNATSQALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  160 TDQVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIVDKGIPVLA 239
Cdd:TIGR03379 161 ERQVAYFHGCYVNYNHPQLGKDLVKVLNAMNIGVQLLEKEKCCGVPLIANGFPDKAKKQAQFNVKQIEAMVDENGIPVIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  240 TSSTCTFTLRDEYPHLLDVDNTGLREHIELATRFLWRKLDSGQTLPLRELPLKVVYHTPCHMEKMGWSLYTLELLRLIPG 319
Cdd:TIGR03379 241 TSSTCSFTLRDEYPHVLGVDNAKVRDHIELVTRFLYRLFMEGKTPPMKPLPLKVAYHTPCHMEKMGWAPYTLELLKMIPG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036415  320 LELTVLDSRCCGIAGTYGFKRENYETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSKRCEHPITLLAKAL 395
Cdd:TIGR03379 321 LEVVVLDSQCCGIAGTYGFKSENYETSQAIGKSLFDQIEQSGADYVITDCETCKWQIEMSTSLECIHPISLLAMAL 396
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
1-396 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 742.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   1 MNDTRFESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDVKIGDIIQRAR 80
Cdd:PRK11168   1 MSDTSFDSCIKCTVCTTACPVARVNPLYPGPKQAGPDGERLRLKDGALYDESLKYCSNCKRCEVACPSGVKIGDIIQRAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  81 ARYSTQK-PSLRDAILSHTDLMGSVSTPFAPLVNAATSLKPVRKLLDATLKIDHHRSLPKYSHGTFRRWYTSVAAEQAQY 159
Cdd:PRK11168  81 AKYVTERgPPLRDRILSHTDLMGSLATPFAPLVNAATGLKPVRWLLEKTLGIDHRRPLPKYAFGTFRRWYRKQAAQQAQY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 160 TDQVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVqLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIvDKGIPVLA 239
Cdd:PRK11168 161 KKQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEV-LLPKEKCCGLPLIANGFLDKARKQAEFNVESLREAI-EKGIPVIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 240 TSSTCTFTLRDEYPHLLDVDNTGLREHIELATRFLWRKLDSGQTLPLRELPLKVVYHTPCHMEKMGWSLYTLELLRLIPG 319
Cdd:PRK11168 239 TSSSCTLTLRDEYPELLGVDNAGVRDHIEDATEFLRRLLDQGKLLPLKPLPLKVAYHTPCHLEKQGWGLYTLELLRLIPG 318

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036415 320 LELTVLDSRCCGIAGTYGFKRENYETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSKRCEHPITLLAKALG 396
Cdd:PRK11168 319 LEVVVLDSQCCGIAGTYGFKKEKYETSQAIGAPLFRQIEESGADLVVTDCETCKWQIEMSTGLECEHPITLLAEALG 395
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 6-396 2.94e-95

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 291.21  E-value: 2.94e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   6 FESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDGERLRLKDGALYD------EALKYCINCKRCEVACPSDVKIGDIIQRA 79
Cdd:COG0247   77 LDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDlseevyEVLDLCLTCKACETACPSGVDIADLIAEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  80 RARYSTQkpslrdailshtdlmgsvstpfaplvnaatslkpvrklldatlkidHHRSLPKYSHGTFRRWYTSVAAEQAQy 159
Cdd:COG0247  157 RAQLVER----------------------------------------------GGRPLRDRLLRTFPDRVPAADKEGAE- 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 160 tdqVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVtslrEAIVDKGIP-VL 238
Cdd:COG0247  190 ---VLLFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNI----EALERLGVKaIV 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 239 ATSSTCTFTLRDEYPHLLDVDntgLREHIELATRFLWRKLDSGQtLPLRELPLKVVYHTPCHMEK-MGWSLYTLELLRLI 317
Cdd:COG0247  263 TTCPSCGLTLKDEYPELLGDR---VAFEVLDISEFLAELILEGK-LKLKPLGEKVTYHDPCHLGRgGGVYDAPRELLKAI 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 318 PGLELTVL--DSRCCGIAGTYGFKREnyETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSK---RCEHPITLLA 392
Cdd:COG0247  339 PGVEVVEMpeDSGCCGGAGGYGFEEP--ELSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKEygiEVKHPVELLA 416


                 ....
gi 527036415 393 KALG 396
Cdd:COG0247  417 EALG 420
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 8-395 4.23e-40

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 148.62  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   8 SCIKCTVCTTVCPVSGVNpRYPGP----KQA----GPDGERLRLKDGalYDEALKYCINCKRCEVACPSDVKI-GDIIQR 78
Cdd:PRK06259 134 GCIECLSCVSTCPARKVS-DYPGPtfmrQLArfafDPRDEGDREKEA--FDEGLYNCTTCGKCVEVCPKEIDIpGKAIEK 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  79 ARARYSTQKPSLRdailSHtdlmgsvstpfaplvnaatslKPVRKLLDATlkidhHRSLPKYSHGTFRRWYTSVAAEQAQ 158
Cdd:PRK06259 211 LRALAFKKGLGLP----AH---------------------LEVRENVLKT-----GRSVPKEKPSFLEEVSDIYPYGNEK 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 159 YTdqVAFFHGCYVNYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIVDKGIPVL 238
Cdd:PRK06259 261 LR--VAFFTGCLVDYRLQEVGKDAIRVLNAHGISVIIPKNQVCCGSPLIRTGQTDVAEELKKKNLEIFNKLDVDTVVTIC 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 239 AtssTCTFTLRDEYPH----LLDVdntglrehielaTRFLwrkLDSGqTLPLRELPLKVVYHTPCHMEK-MGWSLYTLEL 313
Cdd:PRK06259 339 A---GCGSTLKNDYKEkefnVMDI------------TEVL---VEVG-LEKYKPLDITVTYHDPCHLRRgQGIYEEPRKI 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 314 LRLIPGLELTVLD--SRCCGIAGtyGFKRENYETSQAIGAPLFRQIEESGADIVVTDCETCKWQIEMSTSK-----RCEH 386
Cdd:PRK06259 400 LRSIPGLEFVEMEipDQCCGAGG--GVRSGKPEIAEALGKRKAEMIRETGADYVITVCPFCEYHIRDSLKKysediPVMN 477


                 ....*....
gi 527036415 387 PITLLAKAL 395
Cdd:PRK06259 478 IVSLLDKVY 486
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 163-248 4.01e-16

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 72.73  E-value: 4.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  163 VAFFHGCYV-NYNHPQLGKDLLKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQAKSNVTSLREAIVDkgiPVLATS 241
Cdd:pfam02754   1 VAYFDGCHLgRALYPEPRKALKKVLGALGVEVVILEKQSCCGAGGGFSGKEDVAEALAKRNIDTAEETGAD---AIVTAC 77


                  ....*..
gi 527036415  242 STCTFTL 248
Cdd:pfam02754  78 PGCLLQL 84
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
 293-376 5.08e-16

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 72.73  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  293 VVYHTPCHMEKmGWSLYTLELLRLIPGLELTVL----DSRCCGIAGTYGFKREnyeTSQAIGAPLFRQIEESGADIVVTD 368
Cdd:pfam02754   1 VAYFDGCHLGR-ALYPEPRKALKKVLGALGVEVvileKQSCCGAGGGFSGKED---VAEALAKRNIDTAEETGADAIVTA 76


                  ....*...
gi 527036415  369 CETCKWQI 376
Cdd:pfam02754  77 CPGCLLQL 84
glcF PRK11274
glycolate oxidase subunit GlcF;
8-396 3.15e-10

glycolate oxidase subunit GlcF;


Pssm-ID: 236890 [Multi-domain]  Cd Length: 407  Bit Score: 61.43  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   8 SCIKCTVCTTVCPVsgvnprYP-------GP-------KQA---GPDGERLRLKdgalydeaLKYCINCKRCEVACPSDV 70
Cdd:PRK11274  24 KCVHCGFCTATCPT------YQllgdeldGPrgriyliKQVlegAEVTEKTQLH--------LDRCLTCRNCETTCPSGV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415  71 KIGDIIQRARARYSTQKP-SLRDAILSHTdLMGSVSTP--FAPLVNAATSLKPvrkLLDATLKidhhRSLPKyshgtfrr 147
Cdd:PRK11274  90 QYGRLLDIGRKVVEEKVPrPLGERLLRWG-LREVLPRPalFGPLMRLGQAVRP---LLPEALR----AKVPA-------- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 148 wyTSVAAE--QAQYTDQVAFFHGCyV------NYNHPQLgkdllKVLNAMGTGVQLLNKEKCCGVPLIANGFTDKARKQA 219
Cdd:PRK11274 154 --RQPAAPwpPPRHARRVLMLEGC-VqpamspNINAATA-----RVLDRLGISLVVAPEAGCCGAVRYHLNAQEGGLARM 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 220 KSN-------VTSLREAIVdkgipvlATSSTCTFTLRdEYPHLL--DVDNTGLREHIELATRFL---WRKLDSGQTLPLR 287
Cdd:PRK11274 226 RRNidawwpaIEAGAEAIV-------MTASGCGATVK-EYGHLLrdDPAYAEKAARVSALTRDLselLPAEPLELLALLG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415 288 ELPLKVVYHTPC---HMEKMGWSLYTLeLLRLipGLELT-VLDSR-CCGIAGTYGFKreNYETSQAIGAPLFRQIEESGA 362
Cdd:PRK11274 298 RPDRRVAFHPPCtlqHGQKLRGKVERL-LTRL--GFELTlVADSHlCCGSAGTYSLL--QPELSYQLRDNKLAALEAGKP 372

                        410       420       430
                 ....*....|....*....|....*....|....
gi 527036415 363 DIVVTDCETCKWQIEMSTSKRCEHPITLLAKALG 396
Cdd:PRK11274 373 EVIVTANIGCQTHLQSGTRTPVRHWIELVDEALA 406
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 9-70 4.17e-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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 55.39  E-value: 4.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036415    9 CIKCTVCTTVCPVS-GVNPRYPGPKQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDV 70
Cdd:pfam13183   2 CIRCGACLAACPVYlVTGGRFPGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 6-83 1.06e-09

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: 58.22  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   6 FESCIKCTVCTTVCPVSGVNPRYPGPK---QA---------GPDGERLRlkdgALYDEA-LKYCINCKRCEVACPSDVKI 72
Cdd:COG0479  141 LAECILCGACVAACPNVWANPDFLGPAalaQAyrfaldprdEETEERLE----ALEDEEgVWRCTTCGNCTEVCPKGIPP 216

                         90
                 ....*....|.
gi 527036415  73 GDIIQRARARY 83
Cdd:COG0479  217 TKAIAKLKREA 227
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
6-80 1.66e-09

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 54.14  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   6 FESCIKCTVCTTVCPVS---GVNPRypgpkqagpdgERLRL-----KDGALYDEALKYCINCKRCEVACPSDVKIGDIIQ 77
Cdd:COG1150    2 LKKCYQCGTCTASCPVAramDYNPR-----------KIIRLaqlglKEEVLKSDSIWLCVSCYTCTERCPRGIDIADVMD 70


                 ...
gi 527036415  78 RAR 80
Cdd:COG1150   71 ALR 73
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 6-80 7.29e-07

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 49.74  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415    6 FESCIKCTVCTTVCPVSGVNPRYPGP---KQAG-------PDGERLRLKdgALYDEALKY-CINCKRCEVACPSDVKIGD 74
Cdd:TIGR00384 137 LSGCILCGCCYSSCPAFWWNPEFLGPaalTAAYrflidsrDHATKDRLE--GLNDKNGVWrCTTCMNCSEVCPKGVNPAR 214


                  ....*.
gi 527036415   75 IIQRAR 80
Cdd:TIGR00384 215 AIEKLK 220
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 9-70 1.19e-06

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: 45.53  E-value: 1.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036415    9 CIKCTVCTTVCPVSGVNPRYPgpkQAGPDGERLRLKDGALYDEALKYCINCKRCEVACPSDV 70
Cdd:pfam13534   2 CIQCGCCVDECPRYLLNGDEP---KKLMRAAYLGDLEELQANKVANLCSECGLCEYACPMGL 60
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 9-91 9.48e-06

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


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 47.79  E-value: 9.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   9 CIKCTVCTTVCPVSgvnPRYPGPKQAGPDGERLRLKDgaLYDEalkyCINCKRCEVACPSDVKIGDIIQRA-RARYSTQK 87
Cdd:cd01916  367 CTDCGWCTRACPNS---LRIKEAMEAAKEGDFSGLAD--LFDQ----CVGCGRCEQECPKEIPIINMIEKAaRERIKEEK 437


                 ....
gi 527036415  88 PSLR 91
Cdd:cd01916  438 GKMR 441
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 9-70 4.71e-05

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: 40.59  E-value: 4.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527036415    9 CIKCTVCTTVCPVSGVNPRYPGPKQAGPDgerlrlkdgalYDEALKYCINCKRCEVACPSDV 70
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKT-----------VVIDPERCVGCGACVAVCPTGA 51
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 6-69 8.42e-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: 42.00  E-value: 8.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036415   6 FESCIKCTVCTTVCPVsgvnprypGPKQAGPDGERLRLKDG-ALYDEALkyCINCKRCEVACPSD 69
Cdd:cd10549   39 EDKCVFCGACVEVCPT--------GAIELTPEGKEYVPKEKeAEIDEEK--CIGCGLCVKVCPVD 93
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
7-70 9.93e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 43.51  E-value: 9.93e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036415   7 ESCIKCTVCTTVCPVsGVNPRypgpkqagpDGERLRLKdgalydealkyCINCKRCEVACPSDV 70
Cdd:COG0348  210 GDCIDCGLCVKVCPM-GIDIR---------KGEINQSE-----------CINCGRCIDACPKDA 252
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 7-87 1.20e-04

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: 43.97  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036415   7 ESCIKCTVCTTVCPVsGVNPrypgpkqagpdgerLRLKDGAL---YDEALKY----CINCKRCEVACPSDVKIGDIIQRA 79
Cdd:COG4656  364 QPCIRCGRCVDACPM-GLLP--------------QQLYWYARagdFDKAEEYnlmdCIECGCCSYVCPSKIPLVQYIRLA 428


                 ....*...
gi 527036415  80 RARYSTQK 87
Cdd:COG4656  429 KAEIRARR 436
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 6-69 4.34e-04

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: 38.88  E-value: 4.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036415   6 FESCIKCTVCTTVCPVSgvnprypgpkqagpdgeRLRLKDGALYDEALKYCINCKRCEVACPSD 69
Cdd:COG1144   29 EDKCIGCGLCWIVCPDG-----------------AIRVDDGKYYGIDYDYCKGCGICAEVCPVK 75
NapF COG1145
Ferredoxin [Energy production and conversion];
7-70 4.65e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.63  E-value: 4.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036415   7 ESCIKCTVCTTVCPVsgvnprypgpkQAgpdgerLRLKDG-ALYDEALKYCINCKRCEVACPSDV 70
Cdd:COG1145  182 EKCIGCGLCVKVCPT-----------GA------IRLKDGkPQIVVDPDKCIGCGACVKVCPVGA 229
psaC CHL00065
photosystem I subunit VII
 6-69 6.19e-04

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 38.20  E-value: 6.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036415   6 FESCIKCTVCTTVCP--VSGVNPrYPGPKqAGPDGERLRLKDgalydealkyCINCKRCEVACPSD 69
Cdd:CHL00065   8 YDTCIGCTQCVRACPtdVLEMIP-WDGCK-AKQIASAPRTED----------CVGCKRCESACPTD 61
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 7-70 8.90e-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: 38.92  E-value: 8.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036415   7 ESCIKCTVCTTVCPVsgvnprypgpkqagpdgERLRLKDGALYDEALKYCINCKRCEVACPSDV 70
Cdd:cd10549   78 EKCIGCGLCVKVCPV-----------------DAITLEDELEIVIDKEKCIGCGICAEVCPVNA 124
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 7-69 1.14e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.00  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036415   7 ESCIKCTVCTTVCPVsGVnprypgpKQAGPDGERlrlkdgALYDEAlKYCINCKRCEVACPSD 69
Cdd:COG1146    8 DKCIGCGACVEVCPV-DV-------LELDEEGKK------ALVINP-EECIGCGACELVCPVG 55
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 9-31 1.59e-03

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 39.78  E-value: 1.59e-03
                         10        20
                 ....*....|....*....|....
gi 527036415   9 CIKCTVCTTVCPVSGVNP-RYPGP 31
Cdd:PRK05950 143 CILCACCSTSCPSFWWNPdKFLGP 166
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 7-69 2.85e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 36.24  E-value: 2.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036415   7 ESCIKCTVCTTVCPVsgvnprypgpkQAgpdgerLRLKDGALYDEALKYCINCKRCEVACPSD 69
Cdd:COG1149   11 EKCIGCGLCVEVCPE-----------GA------IKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 7-69 4.14e-03

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 35.49  E-value: 4.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036415   7 ESCIKCTVCTTVCPVSGVNPRYPGPKQAgpdgerlrlkdgalYDEALKYCINCKRCEVACPSD 69
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDGEPGKV--------------YVIDPDKCIGCGLCVEVCPTG 50
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 6-69 4.53e-03

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 36.08  E-value: 4.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036415   6 FESCIKCTVCTTVCPVSgVNPRYPGpkqagpDGERLRLKDGALYDEAlkyCINCKRCEVACPSD 69
Cdd:PLN00071   8 YDTCIGCTQCVRACPTD-VLEMIPW------DGCKAKQIASAPRTED---CVGCKRCESACPTD 61
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 7-69 4.89e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.79  E-value: 4.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036415   7 ESCIKCTVCTTVCPVsgvnprypgpkqagpdgERLRLKDGALY-DEALkyCINCKRCEVACPSD 69
Cdd:COG4231   22 DKCTGCGACVKVCPA-----------------DAIEEGDGKAViDPDL--CIGCGSCVQVCPVD 66
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
56-84 6.56e-03

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


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 38.26  E-value: 6.56e-03
                         10        20
                 ....*....|....*....|....*....
gi 527036415  56 CINCKRCEVACPSDVKIGDIIQRARARYS 84
Cdd:COG1453  333 CIECGACEERCPQGLDIPELLKEAHELLG 361
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 7-67 6.57e-03

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 34.92  E-value: 6.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036415    7 ESCIKCTVCTTVCPVSGVNpryPGPKQAGPDGERLRLKDGAlydealkyCINCKRCEVACP 67
Cdd:pfam13237   7 DKCIGCGRCTAACPAGLTR---VGAIVERLEGEAVRIGVWK--------CIGCGACVEACP 56
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 7-70 9.81e-03

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: 35.84  E-value: 9.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036415   7 ESCIKCTVCTTVCPVSGVNPRYPGPKQAGPDgerlrlkdgalYDEALkyCINCKRCEVACPSDV 70
Cdd:cd10549    6 EKCIGCGICVKACPTDAIELGPNGAIARGPE-----------IDEDK--CVFCGACVEVCPTGA 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 7-78 9.82e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 34.64  E-value: 9.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036415   7 ESCIKCTVCTTVCPVsgvnprypgpkQAgpdgerLRLKDGALY-DEALkyCINCKRCEVACPSDVKIGDIIQR 78
Cdd:COG2221   15 EKCIGCGLCVAVCPT-----------GA------ISLDDGKLViDEEK--CIGCGACIRVCPTGAIKGEKPKK 68
 
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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