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Conserved domains on  [gi|805029041|emb|CRC60911|]
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fumarate reductase [Mycobacterium tuberculosis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12385 super family cl32759
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-233 1.14e-127

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


The actual alignment was detected with superfamily member PRK12385:

Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 361.33  E-value: 1.14e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   1 MMDRIVMEVSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFL 80
Cdd:PRK12385   3 EMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  81 ADYlPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPvEDGEYRQTPAELDAFKQFSMCINCMLCYSACP 160
Cdd:PRK12385  83 RDY-TGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTP-DDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 805029041 161 VYALDPDFLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYKLTAA 233
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESA 233
 
Name Accession Description Interval E-value
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-233 1.14e-127

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 361.33  E-value: 1.14e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   1 MMDRIVMEVSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFL 80
Cdd:PRK12385   3 EMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  81 ADYlPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPvEDGEYRQTPAELDAFKQFSMCINCMLCYSACP 160
Cdd:PRK12385  83 RDY-TGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTP-DDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 805029041 161 VYALDPDFLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYKLTAA 233
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESA 233
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 4-229 6.48e-115

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: 328.24  E-value: 6.48e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   4 RIVMEVSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADy 83
Cdd:COG0479    2 TVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  84 LPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPveDGEYRQTPAELDAFKQFSMCINCMLCYSACPVYA 163
Cdd:COG0479   81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP--DNERLQSPEDREKADDLAECILCGACVAACPNVW 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 805029041 164 LDPDFLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:COG0479  159 ANPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLK 224
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 9-229 2.29e-103

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: 298.96  E-value: 2.29e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041    9 VSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPGPV 88
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   89 RVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPvEDGEYRQTPAELDAFKQFSMCINCMLCYSACPVYALDPDF 168
Cdd:TIGR00384  81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPE-PEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEF 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 805029041  169 LGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:TIGR00384 160 LGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 8-111 1.16e-43

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 143.15  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041    8 EVSRYRPEI-ESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPG 86
Cdd:pfam13085   3 RVFRYDPRVdRDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQ 82

                          90       100
                  ....*....|....*....|....*
gi 805029041   87 PVRVEPMRNFPVIRDLVVDISDFMA 111
Cdd:pfam13085  83 DITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-233 1.14e-127

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 361.33  E-value: 1.14e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   1 MMDRIVMEVSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFL 80
Cdd:PRK12385   3 EMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  81 ADYlPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPvEDGEYRQTPAELDAFKQFSMCINCMLCYSACP 160
Cdd:PRK12385  83 RDY-TGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTP-DDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 805029041 161 VYALDPDFLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYKLTAA 233
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESA 233
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 4-229 6.48e-115

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: 328.24  E-value: 6.48e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   4 RIVMEVSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADy 83
Cdd:COG0479    2 TVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  84 LPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPveDGEYRQTPAELDAFKQFSMCINCMLCYSACPVYA 163
Cdd:COG0479   81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP--DNERLQSPEDREKADDLAECILCGACVAACPNVW 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 805029041 164 LDPDFLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:COG0479  159 ANPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLK 224
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 9-229 2.29e-103

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: 298.96  E-value: 2.29e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041    9 VSRYRPEIESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPGPV 88
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   89 RVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPvEDGEYRQTPAELDAFKQFSMCINCMLCYSACPVYALDPDF 168
Cdd:TIGR00384  81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPE-PEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEF 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 805029041  169 LGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:TIGR00384 160 LGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 8-236 9.15e-93

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 272.44  E-value: 9.15e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   8 EVSRYRPEIESAPTFQAYEVPLTREW-AVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPG 86
Cdd:PRK05950   3 KIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLKKG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  87 PVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPveDGEYRQTPAELDAFKQFSMCINCMLCYSACPVYALDP 166
Cdd:PRK05950  83 KIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPP--ARERLQSPEDREKLDGLYECILCACCSTSCPSFWWNP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 805029041 167 D-FLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQRYKLTAATHA 236
Cdd:PRK05950 161 DkFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERR 231
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
2-229 4.20e-82

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 246.97  E-value: 4.20e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   2 MDRIVMEVSRYRPEieSAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLA 81
Cdd:PRK12576   6 EKEVIFKVKRYDPE--KGSWWQEYKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  82 DYLP---GPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPVEDGEYRQTPAELDAFKQFSMCINCMLCYSA 158
Cdd:PRK12576  84 DVAKkynSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 805029041 159 CPVYALDPDFLGPAAIALGQRYNLDSRDQGAADRRDVLaaADGAWACTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:PRK12576 164 CPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAIKKTR 232
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 9-229 9.01e-58

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 184.99  E-value: 9.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   9 VSRYRPEIESAPTFQAYEVPLTR-EWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPGP 87
Cdd:PLN00129  48 IYRWNPDNPGKPHLQSYKVDLNDcGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGP 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  88 VRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPVEDGEYRQTPAE---LDAFKQfsmCINCMLCYSACPVYAL 164
Cdd:PLN00129 128 TTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDrakLDGMYE---CILCACCSTSCPSYWW 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 805029041 165 DPD-FLGPAAIALGQRYNLDSRDQGAADRrdvLAAADGAWA---CTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:PLN00129 205 NPEkFLGPAALLHAYRWISDSRDEYTKER---LEALDDEFKlyrCHTIRNCSNACPKGLNPAKAIAKIK 270
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-225 1.26e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 178.23  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   1 MMDRIVMEVSRYRPEIESAPTFQAYEV-PLTREWAVLDGLTYIKdHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATF 79
Cdd:PRK12575   1 MADTRILHIYRYDPDDDAAPRMQRYEIaPRAEDRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  80 LADyLPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPveDGEYRQTPAELDAFKQFSMCINCMLCYSAC 159
Cdd:PRK12575  80 MQA-LPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPP--ERERLQTPQEREQLDGLYECILCACCSTAC 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 805029041 160 PVYALDPD-FLGPAAIALGQRYNLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAI 225
Cdd:PRK12575 157 PSYWWNPDkFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAI 223
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
4-229 2.36e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 180.28  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   4 RIVMEVSRYRPEieSAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADY 83
Cdd:PRK12577   2 EVLFKILRQKQN--SAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  84 L----------PGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWlVRHDEPPVEDGEYRQTPAELDAFKQFSMCINCM 153
Cdd:PRK12577  80 LarlsdsnsgaIPEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPY-VSTAARQVPEREFLQTPEERSKLDQTGNCILCG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 805029041 154 LCYSACPVYALDPDFLGPAAIALGQRYNLDSRDQGAADRRDVL-AAADGAWACTLVGECSTACPKGVDPAGAIQRYK 229
Cdd:PRK12577 159 ACYSECNAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 2-227 3.09e-52

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 176.35  E-value: 3.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   2 MDRIVMEVSRYRPEIEsAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLA 81
Cdd:PRK06259   1 MKMITITVKRFDPEKD-EPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  82 DylpgPVRVEPMRnFPVIRDLVVDISDFMAKLPSVKPWLVRHDEPPvedgeyrQTPAELDAFKQFSMCINCMLCYSACPV 161
Cdd:PRK06259  80 D----GMIIEPLD-FPVIKDLIVDREPYYKKLKSLRNYLQRKNEKI-------TYPEDIEDIKKLRGCIECLSCVSTCPA 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 805029041 162 YALDpDFLGPAAIALGQRYNLDSRDQGaadRRDVLAAADGAWACTLVGECSTACPKGVD-PAGAIQR 227
Cdd:PRK06259 148 RKVS-DYPGPTFMRQLARFAFDPRDEG---DREKEAFDEGLYNCTTCGKCVEVCPKEIDiPGKAIEK 210
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 8-111 1.16e-43

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 143.15  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041    8 EVSRYRPEI-ESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPG 86
Cdd:pfam13085   3 RVFRYDPRVdRDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQ 82

                          90       100
                  ....*....|....*....|....*
gi 805029041   87 PVRVEPMRNFPVIRDLVVDISDFMA 111
Cdd:pfam13085  83 DITLEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 1-217 1.06e-40

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 139.70  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   1 MMDRIVMEVSRYRPEI-ESAPTFQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATF 79
Cdd:PRK13552   1 MGRTLTFNIFRYNPQDpGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  80 LADYLPGPVRVEPMRNFPVIRDLVVDISDFMAKLPS-VKPWLVRHDEPPVEDGEYRQTPAELDAFKQFSMCINCMLCYSA 158
Cdd:PRK13552  81 TSDYPDGVITLMPLPVFKLIGDLSVNTGKWFREMSErVESWIHTDKEFDIHRLEERMEPEEADEIYELDRCIECGCCVAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 805029041 159 CPVYALDPDFLGPAAIALGQRYNLDSRDQ-GAADRRDVLAAADGAWAC-TLVGeCSTACPK 217
Cdd:PRK13552 161 CGTKQMREDFVGAVGLNRIARFELDPRDErTDEDFYELIGNDDGVFGCmSLLG-CEDNCPK 220
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 22-219 1.27e-34

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 124.43  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  22 FQAYEVPLTREWAVLDGLTYIKDHLDGTLSFRWSCRMGICGSSGMTINGDPKLACATFLADYLPG-PVRVEPMRNFPVIR 100
Cdd:PRK12386  19 LQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTFDEDeTVTVTPMRTFPVIR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041 101 DLVVDIS---DFMAKLPSVKPwlvrhdEPPVEDGEYRQTPAELDAFKQFSMCINCMLCYSACPV----YALDPDFLGPaa 173
Cdd:PRK12386  99 DLVTDVSfnyEKAREIPSFTP------PKDLQPGEYRMQQVDVERSQEFRKCIECFLCQNVCHVvrdhEENKPAFAGP-- 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 805029041 174 ialgqRY-----NLDSRDQGAADRRDVLAAADGAWACTLVGECSTACPKGV 219
Cdd:PRK12386 171 -----RFlmriaELEMHPLDTADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 1-242 2.35e-29

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 110.46  E-value: 2.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041   1 MMDRIVMEVSRYRPEiESAPTFQAYEVPLTREWAVLDGLTYIKDH---LDG--TLSFRW--SCRMGICGSSGMTINGDPK 73
Cdd:PRK08640   2 SEKTVRLIIKRQDGP-DSKPYWEEFEIPYRPNMNVISALMEIRRNpvnAKGekTTPVVWdmNCLEEVCGACSMVINGKPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  74 LACaTFLADYLPGPVRVEPMRNFPVIRDLVVDISDFMAKLPSVKPWLvrhdepPVeDGEY------RQTPAELDAFKQFS 147
Cdd:PRK08640  81 QAC-TALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWI------PI-DGTYdlgpgpRMPEEKRQWAYELS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041 148 MCINCMLCYSACPVYALDPDFLGPAAIALGQRYNLD-SRDQGAADRRDVLAAADGAWACTLVGECSTACPKGVDPAGAIQ 226
Cdd:PRK08640 153 KCMTCGCCLEACPNVNEKSDFIGPAAISQVRLFNAHpTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIA 232

                        250
                 ....*....|....*.
gi 805029041 227 RYKLTAATHALKKLLF 242
Cdd:PRK08640 233 AMNRETTKQSFKSFFG 248
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 22-227 4.34e-14

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 69.48  E-value: 4.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  22 FQAYEVP-LTREWAVLDGLtyikDHLDGTL--------SFRWSCRMGICGSSGMTINGDP------KLACATFLADYLPG 86
Cdd:PRK07570  19 FETYEVDdISPDMSFLEML----DVLNEQLiekgeepvAFDHDCREGICGMCGLVINGRPhgpdrgTTTCQLHMRSFKDG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041  87 -PVRVEPMRN--FPVIRDLVVDISDF-----MAKLPSVkpwlvrhDEPPVEDGEYRQTPAElDAFKQFSM--CINCMLCY 156
Cdd:PRK07570  95 dTITIEPWRAaaFPVIKDLVVDRSALdriiqAGGYVSV-------NTGGAPDANAIPVPKE-DADRAFDAaaCIGCGACV 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 805029041 157 SACPVYA--LdpdFLGpAAIAlgqryNLDSRDQGAADR----RDVLAAAD--GAWACTLVGECSTACPKGVdPAGAIQR 227
Cdd:PRK07570 167 AACPNGSamL---FTG-AKVS-----HLALLPQGQPERarrvRAMVAQMDeeGFGNCTNTGECEAVCPKGI-SLENIAR 235
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 148-219 1.05e-09

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 53.08  E-value: 1.05e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 805029041  148 MCINCMLCYSACPVYaldpdflgpaaIALGQRYNLDSRDQGAADRRDVLA---AADGAWACTLVGECSTACPKGV 219
Cdd:pfam13183   1 RCIRCGACLAACPVY-----------LVTGGRFPGDPRGGAAALLGRLEAlegLAEGLWLCTLCGACTEVCPVGI 64
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 135-222 6.61e-08

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 52.39  E-value: 6.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041 135 QTPAELDAFKQFSMCINCMLCYSACPVYALDPDF-LGPAAIALGQRYNLDSRDQGAADRRDvlaaADGAWACTLVGECST 213
Cdd:COG0247   66 KTLPWKELLDALDACVGCGFCRAMCPSYKATGDEkDSPRGRINLLREVLEGELPLDLSEEV----YEVLDLCLTCKACET 141


                 ....*....
gi 805029041 214 ACPKGVDPA 222
Cdd:COG0247  142 ACPSGVDIA 150
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
146-226 6.47e-06

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 42.96  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041 146 FSMCINCMLCYSACPVyALDPDFLgPA----AIALGqrynldsrdqgaadRRDVLAAADGAWACTLVGECSTACPKGVDP 221
Cdd:COG1150    2 LKKCYQCGTCTASCPV-ARAMDYN-PRkiirLAQLG--------------LKEEVLKSDSIWLCVSCYTCTERCPRGIDI 65


                 ....*
gi 805029041 222 AGAIQ 226
Cdd:COG1150   66 ADVMD 70
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 149-220 1.15e-05

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: 42.06  E-value: 1.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 805029041  149 CINCMLCYSACPVYALDPDFlgPAAIAlgQRYNLDSRDQgaadrrdvLAAADGAWACTLVGECSTACPKGVD 220
Cdd:pfam13534   2 CIQCGCCVDECPRYLLNGDE--PKKLM--RAAYLGDLEE--------LQANKVANLCSECGLCEYACPMGLD 61
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 149-219 4.12e-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: 40.20  E-value: 4.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 805029041  149 CINCMLCYSACPVYALDPDFLGPAAIAlgQRYNLDSRDqgaadrrdvlaaadgawaCTLVGECSTACPKGV 219
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGT--KTVVIDPER------------------CVGCGACVAVCPTGA 51
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
149-227 1.24e-04

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 42.55  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805029041 149 CINCMLCYSACPVYALDPDFLGPAAIAL-GQRYnldsRDQGAADRRDVLAaadgawACTLVGECSTACPKGVDPAGAIQR 227
Cdd:PRK11168   9 CIKCTVCTTACPVARVNPLYPGPKQAGPdGERL----RLKDGALYDESLK------YCSNCKRCEVACPSGVKIGDIIQR 78
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 149-216 1.83e-04

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: 38.39  E-value: 1.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 805029041  149 CINCMLCYSACPVYAldpdflgpaaialgqrynldSRDQGAADRRDVLAAADGAWACTLVGECSTACP 216
Cdd:pfam13237   9 CIGCGRCTAACPAGL--------------------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
 
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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