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Conserved domains on  [gi|119615235|gb|EAW94829|]
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succinate dehydrogenase complex, subunit B, iron sulfur (Ip), isoform CRA_b [Homo sapiens]

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
 1-214 1.24e-155

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: 432.29  E-value: 1.24e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:PLN00129  61 LQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYR 160
Cdd:PLN00129 141 DLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 214
Cdd:PLN00129 221 WISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-214 1.24e-155

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 432.29  E-value: 1.24e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:PLN00129  61 LQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYR 160
Cdd:PLN00129 141 DLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 214
Cdd:PLN00129 221 WISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-214 5.93e-112

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: 319.77  E-value: 5.93e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtNLNKVSKIYPLPHMYVIK 80
Cdd:COG0479   20 FQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-DLKDTITIEPLRNFPVIK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDkYLGPAVLMQAYR 160
Cdd:COG0479   98 DLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVWANPD-FLGPAALAQAYR 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 214
Cdd:COG0479  175 FALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 1-210 4.18e-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: 297.03  E-value: 4.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235    1 MQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:TIGR00384  14 LQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPVMKIEPLPNLPVIK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDkYLGPAVLMQAYR 160
Cdd:TIGR00384  93 DLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE-FLGPAALTAAYR 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 119615235  161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 210
Cdd:TIGR00384 171 FLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 1-91 6.08e-41

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: 135.44  E-value: 6.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235    1 MQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:pfam13085  18 YQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQDITLEPLPGFPVIR 96

                          90
                  ....*....|.
gi 119615235   81 DLVPDLSNFYA 91
Cdd:pfam13085  97 DLVVDRSAFFE 107
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 15-52 5.59e-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: 35.06  E-value: 5.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 119615235  15 VLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 52
Cdd:cd00207   20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-214 1.24e-155

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 432.29  E-value: 1.24e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:PLN00129  61 LQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYR 160
Cdd:PLN00129 141 DLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 214
Cdd:PLN00129 221 WISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 1-215 4.57e-150

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 416.12  E-value: 4.57e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:PRK05950  17 MQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLKKGKIVIRPLPGLPVIK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDesQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYR 160
Cdd:PRK05950  97 DLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWNPDKFLGPAALLQAYR 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMAT 215
Cdd:PRK05950 175 FIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLE 229
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-214 5.93e-112

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: 319.77  E-value: 5.93e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtNLNKVSKIYPLPHMYVIK 80
Cdd:COG0479   20 FQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-DLKDTITIEPLRNFPVIK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDkYLGPAVLMQAYR 160
Cdd:COG0479   98 DLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVWANPD-FLGPAALAQAYR 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 214
Cdd:COG0479  175 FALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 1-210 4.18e-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: 297.03  E-value: 4.18e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235    1 MQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:TIGR00384  14 LQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPVMKIEPLPNLPVIK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   81 DLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDkYLGPAVLMQAYR 160
Cdd:TIGR00384  93 DLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE-FLGPAALTAAYR 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 119615235  161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 210
Cdd:TIGR00384 171 FLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-214 2.28e-96

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 280.69  E-value: 2.28e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKCGPMVLDALIKIKNEvDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTnLNKVSKIYPLPHMYVIK 80
Cdd:PRK12575  22 MQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA-LPREIVLRPLPGLPVVR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKkkDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYR 160
Cdd:PRK12575 100 DLIVDMTDFFNQYHSIRPYLI--NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNPDKFVGPAGLLQAYR 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 214
Cdd:PRK12575 178 FIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
2-219 6.31e-60

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 189.57  E-value: 6.31e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   2 QTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLAC-TRRID--TNLNKVSKIYPLPHMYV 78
Cdd:PRK12576  25 QEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACkTLVLDvaKKYNSVITIEPMDYFKV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  79 IKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNgDKYLGPAVLMQA 158
Cdd:PRK12576 104 VKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACPVVAID-PEFLGPAAHAKG 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119615235 159 YRWMIDSRDDFTEERLAKLQDpfSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEK 219
Cdd:PRK12576 183 YRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRSFTRVYKPK 241
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
2-222 1.79e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 179.51  E-value: 1.79e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   2 QTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSK----------IY 71
Cdd:PRK12577  19 QTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSELARLSDsnsgaipeitIA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  72 PLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkkdeSQEGKQ----QYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGD 147
Cdd:PRK12577  98 PLGNMPVIKDLVVDMSSFWQNLEAVDPYV-----STAARQvperEFLQTPEERSKLDQTGNCILCGACYSECNAREVNPE 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119615235 148 kYLGPAVLMQAYRWMIDSRDDFTEERLAKL-QDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKKAS 222
Cdd:PRK12577 173 -FVGPHALAKAQRMVADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQEILARKDAQDS 247
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 1-91 6.08e-41

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: 135.44  E-value: 6.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235    1 MQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:pfam13085  18 YQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQDITLEPLPGFPVIR 96

                          90
                  ....*....|.
gi 119615235   81 DLVPDLSNFYA 91
Cdd:pfam13085  97 DLVVDRSAFFE 107
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-210 4.19e-40

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 137.52  E-value: 4.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVsKIYPLPHMYVIK 80
Cdd:PRK12385  24 SQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTGGM-KVEALANFPIER 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDESQEgKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNgDKYLGPAVLMQAYR 160
Cdd:PRK12385 102 DLVVDMTHFIESLEAIKPYIIGNDRTPD-DGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLN-PEFIGPAAITLAHR 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119615235 161 WMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 210
Cdd:PRK12385 180 YNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 1-220 3.19e-36

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 132.82  E-value: 3.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLnkvsKIYPLpHMYVIK 80
Cdd:PRK06259  20 FESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM----IIEPL-DFPVIK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQYKSIEPYLKKKDEsqegKQQYLQSIEEREKLDGlyeCILCACCSTSCPSYwwNGDKYLGPAVLMQAYR 160
Cdd:PRK06259  94 DLIVDREPYYKKLKSLRNYLQRKNE----KITYPEDIEDIKKLRG---CIECLSCVSTCPAR--KVSDYPGPTFMRQLAR 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119615235 161 WMIDSRDDFTEERLAKLQdpfSLYRCHTIMNCTRTCPKGLN-PGKAIAEIKKMmaTYKEKK 220
Cdd:PRK06259 165 FAFDPRDEGDREKEAFDE---GLYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL--AFKKGL 220
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 1-215 3.59e-31

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 114.28  E-value: 3.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIK 80
Cdd:PRK13552  23 MVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSDYPDGVITLMPLPVFKLIG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  81 DLVPDLSNFYAQ-YKSIEPYLKKKDESQEGKqqylqsIEER---EKLDGLYE---CILCACCSTSCPSYWWNGDkYLGPA 153
Cdd:PRK13552 102 DLSVNTGKWFREmSERVESWIHTDKEFDIHR------LEERmepEEADEIYEldrCIECGCCVAACGTKQMRED-FVGAV 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119615235 154 VLMQAYRWMIDSRDDFTEERLAKL---QDpfSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMAT 215
Cdd:PRK13552 175 GLNRIARFELDPRDERTDEDFYELignDD--GVFGCMSLLGCEDNCPKDLPLQQQIAYLRRKMAA 237
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 1-200 4.28e-20

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 85.52  E-value: 4.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235   1 MQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT-NLNKVSKIYPLPHMYVI 79
Cdd:PRK12386  19 LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTfDEDETVTVTPMRTFPVI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  80 KDLVPDLSNFYAQYKSIEPYLKKKDEsQEGKQQYLQsiEEREKLDGLYECILCACCSTSC---PSYWWNGDKYLGPAVLM 156
Cdd:PRK12386  98 RDLVTDVSFNYEKAREIPSFTPPKDL-QPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvvRDHEENKPAFAGPRFLM 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119615235 157 QAYRWMIDSRDdfTEERLAKLQDPFSLYRCHTIMNCTRTCPKGL 200
Cdd:PRK12386 175 RIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 15-209 2.25e-15

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 72.33  E-value: 2.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  15 VLDALIKI-KNEVD------STLTFRRSCREGICGSCAMNINGGNTLACTRRIDtNLNKVSKIYPLPHMYVIKDLVPDLS 87
Cdd:PRK08640  35 VISALMEIrRNPVNakgektTPVVWDMNCLEEVCGACSMVINGKPRQACTALID-QLEQPIRLEPMSTFPVVRDLQVDRS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235  88 NFYAQYKSIEPYL--KKKDESQEGKQQylqSIEEREKLDGLYECILCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDS 165
Cdd:PRK08640 114 RMFDNLKRVKAWIpiDGTYDLGPGPRM---PEEKRQWAYELSKCMTCGCCLEACPNVNEKSD-FIGPAAISQVRLFNAHP 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 119615235 166 RDDFT-EERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEI 209
Cdd:PRK08640 190 TGEMHkEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAAM 234
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 128-201 1.94e-08

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


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 49.38  E-value: 1.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119615235  128 ECILCACCSTSCPSYWWNGDKylgPAVLMQAYRWmidsrddfteERLAKLQDPFSLYRCHTIMNCTRTCPKGLN 201
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 114-215 1.27e-06

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 48.15  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235 114 LQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIdsRDDFTEERLAKLQDpfSLYRCHTIMNCT 193
Cdd:COG0247   65 LKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVL--EGELPLDLSEEVYE--VLDLCLTCKACE 140

                         90       100
                 ....*....|....*....|..
gi 119615235 194 RTCPKGLNPGKAIAEIKKMMAT 215
Cdd:COG0247  141 TACPSGVDIADLIAEARAQLVE 162
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 129-200 1.01e-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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 41.91  E-value: 1.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119615235  129 CILCACCSTSCPSYwwngdkylgpavLMQAYRWMIDSRD---DFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGL 200
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
125-214 3.19e-05

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 41.04  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119615235 125 GLYECILCACCSTSCPSYWWNGdkyLGPAVLMQAYRWmiDSRDDFteerlakLQDPfSLYRCHTIMNCTRTCPKGLNPGK 204
Cdd:COG1150    1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL--GLKEEV-------LKSD-SIWLCVSCYTCTERCPRGIDIAD 67

                         90
                 ....*....|
gi 119615235 205 AIAEIKKMMA 214
Cdd:COG1150   68 VMDALRNLAI 77
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 36-89 1.12e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 42.13  E-value: 1.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119615235  36 CREGICGSCAMNING------GNTLACTRRI----DTNLNKV----SKIYPlphmyVIKDLVPDLSNF 89
Cdd:PRK07570  58 CREGICGMCGLVINGrphgpdRGTTTCQLHMrsfkDGDTITIepwrAAAFP-----VIKDLVVDRSAL 120
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 15-52 5.59e-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: 35.06  E-value: 5.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 119615235  15 VLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 52
Cdd:cd00207   20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 129-197 9.98e-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: 33.38  E-value: 9.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119615235  129 CILCACCSTSCPSYWWNGDKYlgpavlmqayrwmidsrddftEERLAKLQDPFSLYRCHTIMNCTRTCP 197
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAI---------------------VERLEGEAVRIGVWKCIGCGACVEACP 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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