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Conserved domains on  [gi|149024454|gb|EDL80951|]
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succinate dehydrogenase complex, subunit B, iron sulfur (Ip) (predicted), isoform CRA_a [Rattus norvegicus]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 1001168)

quinone-dependent succinate dehydrogenase iron-sulfur subunit is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q)

CATH:  1.10.1060.10|3.10.20.30
EC:  1.3.5.1
Gene Ontology:  GO:0046872|GO:0009055|GO:0051536|GO:0008177|GO:0048039

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00129 super family cl33415
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-182 3.01e-96

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


The actual alignment was detected with superfamily member PLN00129:

Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 280.14  E-value: 3.01e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   1 MAAVVgvsLKRGFSATALGRVGLQFQACREAQ-----TAAAAAPRIKTFAIYRWDPDKaGDKPRMQTYKVDLNKCGPMVL 75
Cdd:PLN00129   1 MAAGL---LRRLAGAKAGLLAPAAAASAAASAetkasSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  76 DALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSI 155
Cdd:PLN00129  77 DVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSI 156

                        170       180
                 ....*....|....*....|....*..
gi 149024454 156 EPYLKKKDESQEGKQQYLQSIEDREKL 182
Cdd:PLN00129 157 EPWLKTKKPPEDGQKEHLQSKEDRAKL 183
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-182 3.01e-96

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 280.14  E-value: 3.01e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   1 MAAVVgvsLKRGFSATALGRVGLQFQACREAQ-----TAAAAAPRIKTFAIYRWDPDKaGDKPRMQTYKVDLNKCGPMVL 75
Cdd:PLN00129   1 MAAGL---LRRLAGAKAGLLAPAAAASAAASAetkasSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  76 DALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSI 155
Cdd:PLN00129  77 DVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSI 156

                        170       180
                 ....*....|....*....|....*..
gi 149024454 156 EPYLKKKDESQEGKQQYLQSIEDREKL 182
Cdd:PLN00129 157 EPWLKTKKPPEDGQKEHLQSKEDRAKL 183
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 43-182 1.96e-63

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: 195.35  E-value: 1.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  43 TFAIYRWDPDKaGDKPRMQTYKVDLNkCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtD 122
Cdd:COG0479    4 TLKIWRQDPET-DSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454 123 LGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEDREKL 182
Cdd:COG0479   81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKA 138
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 46-182 1.54e-57

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: 179.93  E-value: 1.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   46 IYRWDPDkAGDKPRMQTYKVDLNKCgPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGK 125
Cdd:TIGR00384   1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 149024454  126 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEDREKL 182
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKL 134
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 43-150 1.32e-51

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: 160.87  E-value: 1.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   43 TFAIYRWDPDKAGDKPRMQTYKVDlNKCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 149024454  123 LGKVSKIYPLPHMYVIKDLVPDLSNFYA 150
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 74-111 1.49e-03

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 36.22  E-value: 1.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 149024454  74 VLDALIKIKneidstLTFRRSCREGICGSCAMNINGGN 111
Cdd:cd00207   20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-182 3.01e-96

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 280.14  E-value: 3.01e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   1 MAAVVgvsLKRGFSATALGRVGLQFQACREAQ-----TAAAAAPRIKTFAIYRWDPDKaGDKPRMQTYKVDLNKCGPMVL 75
Cdd:PLN00129   1 MAAGL---LRRLAGAKAGLLAPAAAASAAASAetkasSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  76 DALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSI 155
Cdd:PLN00129  77 DVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSI 156

                        170       180
                 ....*....|....*....|....*..
gi 149024454 156 EPYLKKKDESQEGKQQYLQSIEDREKL 182
Cdd:PLN00129 157 EPWLKTKKPPEDGQKEHLQSKEDRAKL 183
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 43-182 1.20e-83

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 246.63  E-value: 1.20e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  43 TFAIYRWDPDKaGDKPRMQTYKVDLNKCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:PRK05950   1 TFKIYRYNPDV-DANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454 123 LGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDesQEGKQQYLQSIEDREKL 182
Cdd:PRK05950  80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKL 137
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 43-182 1.96e-63

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: 195.35  E-value: 1.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  43 TFAIYRWDPDKaGDKPRMQTYKVDLNkCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtD 122
Cdd:COG0479    4 TLKIWRQDPET-DSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454 123 LGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEDREKL 182
Cdd:COG0479   81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKA 138
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 46-182 1.54e-57

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: 179.93  E-value: 1.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   46 IYRWDPDkAGDKPRMQTYKVDLNKCgPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGK 125
Cdd:TIGR00384   1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 149024454  126 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEDREKL 182
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKL 134
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 43-150 1.32e-51

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: 160.87  E-value: 1.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454   43 TFAIYRWDPDKAGDKPRMQTYKVDlNKCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 149024454  123 LGKVSKIYPLPHMYVIKDLVPDLSNFYA 150
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
42-182 2.28e-39

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 133.93  E-value: 2.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  42 KTFAIYRWDPDKaGDKPRMQTYKVDLNKCGPMVLDALIKIKNEiDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT 121
Cdd:PRK12575   5 RILHIYRYDPDD-DAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149024454 122 dLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkKDESQEGKQQYLQSIEDREKL 182
Cdd:PRK12575  83 -LPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYL--INDTVPPERERLQTPQEREQL 140
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
43-182 4.64e-35

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 124.09  E-value: 4.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  43 TFAIYRWDPDKagdKPRMQTYKVDLNKcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLAC-TRRID- 120
Cdd:PRK12576  10 IFKVKRYDPEK---GSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACkTLVLDv 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149024454 121 -TDLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKL 182
Cdd:PRK12576  86 aKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKEL 148
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
43-182 3.26e-34

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 122.88  E-value: 3.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  43 TFAIYRWDPDKAgdkPRMQTYKVDLNKcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:PRK12577   4 LFKILRQKQNSA---PYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149024454 123 LGKVSK----------IYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkkdeSQEGKQ----QYLQSIEDREKL 182
Cdd:PRK12577  80 LARLSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYV-----STAARQvperEFLQTPEERSKL 148
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 40-164 4.84e-25

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 96.94  E-value: 4.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  40 RIKTFAIYRWDPDKAGDKPRMQTYKVDlNKCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACtRRI 119
Cdd:PRK13552   3 RTLTFNIFRYNPQDPGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLAC-RTL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149024454 120 DTDLGK-VSKIYPLPHMYVIKDLVPDLSNFYAQ-YKSIEPYLKKKDE 164
Cdd:PRK13552  81 TSDYPDgVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKE 127
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 46-182 2.47e-24

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 98.54  E-value: 2.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  46 IYRWDPDKagDKPRMQTYKVDLNKcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLgk 125
Cdd:PRK06259   8 VKRFDPEK--DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM-- 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149024454 126 vsKIYPLpHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsqegKQQYLQSIEDREKL 182
Cdd:PRK06259  83 --IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNE----KITYPEDIEDIKKL 132
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
40-181 5.31e-24

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 94.38  E-value: 5.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  40 RIKTFAIYRWDPDKaGDKPRMQTYKVDLNKcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRI 119
Cdd:PRK12385   5 KNLKIEVLRYNPEV-DTEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149024454 120 DTDLGKVsKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEgKQQYLQSIEDREK 181
Cdd:PRK12385  83 RDYTGGM-KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPD-DGPNKQTPAQMAK 142
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 43-163 3.10e-15

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 71.27  E-value: 3.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  43 TFAIYRWDpDKAGDkprMQTYKVDLNKcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT- 121
Cdd:PRK12386   6 KFRVWRGD-ASGGE---LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTf 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149024454 122 DLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKD 163
Cdd:PRK12386  81 DEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKD 122
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 49-148 8.24e-07

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 47.52  E-value: 8.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  49 WDPDKAGDKPRMQTYKVD--------------LNkcgpmvlDALIKIKNEIdstLTFRRSCREGICGSCAMNING----- 109
Cdd:PRK07570   8 WRQKGPDDKGKFETYEVDdispdmsflemldvLN-------EQLIEKGEEP---VAFDHDCREGICGMCGLVINGrphgp 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 149024454 110 -GNTLACTRRI----DTDLGKV----SKIYPlphmyVIKDLVPDLSNF 148
Cdd:PRK07570  78 dRGTTTCQLHMrsfkDGDTITIepwrAAAFP-----VIKDLVVDRSAL 120
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 39-146 1.15e-06

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 47.29  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149024454  39 PRIKTFAIYRWD-PDKagdKPRMQTYKVDLNKcGPMVLDALIKI-KNEID------STLTFRRSCREGICGSCAMNINGG 110
Cdd:PRK08640   3 EKTVRLIIKRQDgPDS---KPYWEEFEIPYRP-NMNVISALMEIrRNPVNakgektTPVVWDMNCLEEVCGACSMVINGK 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 149024454 111 NTLACTRRIDTdLGKVSKIYPLPHMYVIKDLVPDLS 146
Cdd:PRK08640  79 PRQACTALIDQ-LEQPIRLEPMSTFPVVRDLQVDRS 113
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 74-111 1.49e-03

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 36.22  E-value: 1.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 149024454  74 VLDALIKIKneidstLTFRRSCREGICGSCAMNINGGN 111
Cdd:cd00207   20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
 
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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