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Conserved domains on  [gi|1735202923|gb|KAA0044721|]
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succinate dehydrogenase (ubiquinone) iron-sulfur subunit 3 [Cucumis melo var. makuwa]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 11476389)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-284 2.77e-175

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


:

Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 484.68  E-value: 2.77e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923   1 MLKGWFRHAYNKVSKKRFGVLEEHPMAkqHAEEAMEAHGEIKSNLrfnnqKEFKIYRWNPQYPNhKPFLHSFFLDLSKCG 80
Cdd:PLN00129    1 MAAGLLRRLAGAKAGLLAPAAAASAAA--SAETKASSKGSKPSNL-----KEFQIYRWNPDNPG-KPHLQSYKVDLNDCG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  81 PMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADTSKPTIITPLPHMYVIKDLVVDLTNFYQQ 160
Cdd:PLN00129   73 PMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 161 YKSIEPWLKTRRSAE-GGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWNPEEFLGPAALLHAYRWISDSRDEFKEE 239
Cdd:PLN00129  153 YKSIEPWLKTKKPPEdGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKE 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1735202923 240 RLQAIaEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAMHLIS 284
Cdd:PLN00129  233 RLEAL-DDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-284 2.77e-175

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 484.68  E-value: 2.77e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923   1 MLKGWFRHAYNKVSKKRFGVLEEHPMAkqHAEEAMEAHGEIKSNLrfnnqKEFKIYRWNPQYPNhKPFLHSFFLDLSKCG 80
Cdd:PLN00129    1 MAAGLLRRLAGAKAGLLAPAAAASAAA--SAETKASSKGSKPSNL-----KEFQIYRWNPDNPG-KPHLQSYKVDLNDCG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  81 PMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADTSKPTIITPLPHMYVIKDLVVDLTNFYQQ 160
Cdd:PLN00129   73 PMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 161 YKSIEPWLKTRRSAE-GGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWNPEEFLGPAALLHAYRWISDSRDEFKEE 239
Cdd:PLN00129  153 YKSIEPWLKTKKPPEdGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKE 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1735202923 240 RLQAIaEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAMHLIS 284
Cdd:PLN00129  233 RLEAL-DDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 53-280 3.66e-105

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: 305.13  E-value: 3.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  53 FKIYRWNPQYPNhKPFLHSFFLDLSkCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDaDT 132
Cdd:COG0479     5 LKIWRQDPETDS-KPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-DL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 133 SKPTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTRRSAEgGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWN 212
Cdd:COG0479    82 KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP-DNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735202923 213 PeEFLGPAALLHAYRWISDSRDEFKEERLQAIaEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAM 280
Cdd:COG0479   161 P-DFLGPAALAQAYRFALDPRDEETEERLEAL-EDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKRE 226
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 55-278 1.10e-98

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: 288.56  E-value: 1.10e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  55 IYRWNPQYPNhKPFLHSFFLDlSKCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADTSK 134
Cdd:TIGR00384   1 VLRFNPDVDE-KPHLQSYEVP-ADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 135 PTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTRRSAEGGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWNPe 214
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP- 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735202923 215 EFLGPAALLHAYRWISDSRDEFKEERLQaIAEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMK 278
Cdd:TIGR00384 158 EFLGPAALTAAYRFLIDSRDHATKDRLE-GLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 53-159 7.57e-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: 142.38  E-value: 7.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  53 FKIYRWNPQYPNHKPFLHSFFLDLsKCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADT 132
Cdd:pfam13085   2 LRVFRYDPRVDRDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 1735202923 133 SKPTIITPLPHMYVIKDLVVDLTNFYQ 159
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-284 2.77e-175

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 484.68  E-value: 2.77e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923   1 MLKGWFRHAYNKVSKKRFGVLEEHPMAkqHAEEAMEAHGEIKSNLrfnnqKEFKIYRWNPQYPNhKPFLHSFFLDLSKCG 80
Cdd:PLN00129    1 MAAGLLRRLAGAKAGLLAPAAAASAAA--SAETKASSKGSKPSNL-----KEFQIYRWNPDNPG-KPHLQSYKVDLNDCG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  81 PMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADTSKPTIITPLPHMYVIKDLVVDLTNFYQQ 160
Cdd:PLN00129   73 PMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 161 YKSIEPWLKTRRSAE-GGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWNPEEFLGPAALLHAYRWISDSRDEFKEE 239
Cdd:PLN00129  153 YKSIEPWLKTKKPPEdGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKE 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1735202923 240 RLQAIaEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAMHLIS 284
Cdd:PLN00129  233 RLEAL-DDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 52-280 9.75e-137

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 385.30  E-value: 9.75e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  52 EFKIYRWNPQYPNhKPFLHSFFLDLSKCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDAD 131
Cdd:PRK05950    1 TFKIYRYNPDVDA-NPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 132 TSKPTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTrRSAEGGREFRQTPAERKKLDGLYECILCACCSTSCPPYWW 211
Cdd:PRK05950   80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLIN-DTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWW 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735202923 212 NPEEFLGPAALLHAYRWISDSRDEFKEERLqAIAEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAM 280
Cdd:PRK05950  159 NPDKFLGPAALLQAYRFIADSRDEATGERL-DILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRM 226
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 53-280 3.66e-105

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: 305.13  E-value: 3.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  53 FKIYRWNPQYPNhKPFLHSFFLDLSkCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDaDT 132
Cdd:COG0479     5 LKIWRQDPETDS-KPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-DL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 133 SKPTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTRRSAEgGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWN 212
Cdd:COG0479    82 KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP-DNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735202923 213 PeEFLGPAALLHAYRWISDSRDEFKEERLQAIaEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAM 280
Cdd:COG0479   161 P-DFLGPAALAQAYRFALDPRDEETEERLEAL-EDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKRE 226
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 55-278 1.10e-98

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: 288.56  E-value: 1.10e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  55 IYRWNPQYPNhKPFLHSFFLDlSKCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADTSK 134
Cdd:TIGR00384   1 VLRFNPDVDE-KPHLQSYEVP-ADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 135 PTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTRRSAEGGREFRQTPAERKKLDGLYECILCACCSTSCPPYWWNPe 214
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP- 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735202923 215 EFLGPAALLHAYRWISDSRDEFKEERLQaIAEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMK 278
Cdd:TIGR00384 158 EFLGPAALTAAYRFLIDSRDHATKDRLE-GLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
48-286 1.76e-91

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 271.06  E-value: 1.76e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  48 NNQKEFKIYRWNPQyPNHKPFLHSFFLDLSKCGPMVLDALQMIKAEkDSSLSYRRSCREGICGSCAMNIDGANTVACLKP 127
Cdd:PRK12575    2 ADTRILHIYRYDPD-DDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 128 IDAdTSKPTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLkTRRSAEGGREFRQTPAERKKLDGLYECILCACCSTSCP 207
Cdd:PRK12575   80 MQA-LPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYL-INDTVPPERERLQTPQEREQLDGLYECILCACCSTACP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735202923 208 PYWWNPEEFLGPAALLHAYRWISDSRDEFKEERLQAIaEDETKLYRCRTVKNCTATCPKSLDPSSAIHHMKAMhLISRS 286
Cdd:PRK12575  158 SYWWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDL-EDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTM-LARRA 234
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
50-278 1.29e-60

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 195.30  E-value: 1.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  50 QKEFKIYRwnpQYPNHKPFLHSFFLDLSKcGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPID 129
Cdd:PRK12577    2 EVLFKILR---QKQNSAPYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 130 ADTSK---------PTI-ITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKT--RRSAEggREFRQTPAERKKLDGLYECI 197
Cdd:PRK12577   78 SELARlsdsnsgaiPEItIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTaaRQVPE--REFLQTPEERSKLDQTGNCI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 198 LCACCSTSCPPYWWNPeEFLGPAALLHAYRWISDSRDEFKEERLQAIAEDETKLYRCRTVKNCTATCPKSLDPSSAIHHM 277
Cdd:PRK12577  156 LCGACYSECNAREVNP-EFVGPHALAKAQRMVADSRDTATEQRLELYNQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKI 234


                  .
gi 1735202923 278 K 278
Cdd:PRK12577  235 K 235
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
53-279 6.63e-56

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 181.49  E-value: 6.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  53 FKIYRWNPQypnHKPFLHSFFLDLSKcGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPID--A 130
Cdd:PRK12576   11 FKVKRYDPE---KGSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVLdvA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 131 DTSKPTI-ITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTRRSAEGGR-EFRQTPAERKKLDGLYECILCACCSTSCPP 208
Cdd:PRK12576   87 KKYNSVItIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKaEHRLKPEDQKELWKFAQCIWCGLCVSACPV 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735202923 209 YWWNPeEFLGPAALLHAYRWISDSRDEFKEERLqAIAEDetKLYRCRTVKNCTATCPKSLDPSSAIHHMKA 279
Cdd:PRK12576  167 VAIDP-EFLGPAAHAKGYRFLADPRDTITEERM-KILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
52-279 6.60e-50

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 164.87  E-value: 6.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  52 EFKIYRWNPQYPNhKPFLHSFFL----DLSkcgpmVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVAClKP 127
Cdd:PRK12385    8 KIEVLRYNPEVDT-EPHSQTYEVpydeTTS-----LLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLAC-KT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 128 IDADTSKPTIITPLPHMYVIKDLVVDLTNFYQQYKSIEPW-LKTRRSAEGGrEFRQTPAERKKLDGLYECILCACCSTSC 206
Cdd:PRK12385   81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYiIGNDRTPDDG-PNKQTPAQMAKYHQFSGCINCGLCYAAC 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735202923 207 PPYWWNPeEFLGPAALLHAYRWISDSRDEFKEERLQAIAEDEtKLYRCRTVKNCTATCPKSLDPSSAIHHMKA 279
Cdd:PRK12385  160 PQFGLNP-EFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQN-GVWSCTFVGYCSEVCPKHVDPAAAIQQGKV 230
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 53-159 7.57e-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: 142.38  E-value: 7.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  53 FKIYRWNPQYPNHKPFLHSFFLDLsKCGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADT 132
Cdd:pfam13085   2 LRVFRYDPRVDRDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 1735202923 133 SKPTIITPLPHMYVIKDLVVDLTNFYQ 159
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 52-268 3.27e-35

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 126.60  E-value: 3.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  52 EFKIYRWNPQYPNHKPFLHSFFLDLSKcGPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVAClKPIDAD 131
Cdd:PRK13552    6 TFNIFRYNPQDPGSKPHMVTYQLEETP-GMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLAC-RTLTSD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 132 TSKPTI-ITPLPHMYVIKDLVVDLTNFYQQ-YKSIEPWLKTRRSAEGGR-EFRQTPAERKKLDGLYECILCACCSTSCPP 208
Cdd:PRK13552   84 YPDGVItLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRlEERMEPEEADEIYELDRCIECGCCVAACGT 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 209 YWWNPeEFLGPAALLHAYRWISDSRDEFKEERLQAIAEDETKLYRCRTVKNCTATCPKSL 268
Cdd:PRK13552  164 KQMRE-DFVGAVGLNRIARFELDPRDERTDEDFYELIGNDDGVFGCMSLLGCEDNCPKDL 222
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 83-280 2.78e-34

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 129.74  E-value: 2.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  83 VLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDADtskpTIITPLpHMYVIKDLVVDLTNFYQQYK 162
Cdd:PRK06259   33 VLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDG----MIIEPL-DFPVIKDLIVDREPYYKKLK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 163 SIEPWLktrrsaEGGREFRQTPAERKKLDGLYECILCACCSTSCPPYwwNPEEFLGPAALLHAYRWISDSRDEFKEERlQ 242
Cdd:PRK06259  108 SLRNYL------QRKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--KVSDYPGPTFMRQLARFAFDPRDEGDREK-E 178

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1735202923 243 AIAEDetkLYRCRTVKNCTATCPKSLD-PSSAIHHMKAM 280
Cdd:PRK06259  179 AFDEG---LYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL 214
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 63-277 1.11e-20

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 88.51  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  63 PNHKPFLHSFFLDLSKcGPMVLDALQMI-------KAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDaDTSKP 135
Cdd:PRK08640   16 PDSKPYWEEFEIPYRP-NMNVISALMEIrrnpvnaKGEKTTPVVWDMNCLEEVCGACSMVINGKPRQACTALID-QLEQP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 136 TIITPLPHMYVIKDLVVDLTNFYQQYKSIEPWLKTRRSAEGGREFRQTPAERKKLDGLYECILCACCSTSCPPYwwNPE- 214
Cdd:PRK08640   94 IRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGTYDLGPGPRMPEEKRQWAYELSKCMTCGCCLEACPNV--NEKs 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1735202923 215 EFLGPAAllhayrwISDSR--------DEFKEERLQAIAEDeTKLYRCRTVKNCTATCPKSLDPSSAIHHM 277
Cdd:PRK08640  172 DFIGPAA-------ISQVRlfnahptgEMHKEERLRALMGD-GGIADCGNAQNCVRVCPKGIPLTTSIAAM 234
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 80-265 1.93e-17

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 79.74  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923  80 GPMVLDALQMIKAEKDSSLSYRRSCREGICGSCAMNIDGANTVACLKPIDA-DTSKPTIITPLPHMYVIKDLVVDLTNFY 158
Cdd:PRK12386   29 GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTfDEDETVTVTPMRTFPVIRDLVTDVSFNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 159 QQYKSIEPWLKTRRSAEGgrEFRQTPAERKKLDGLYECILCACCSTSC---PPYWWNPEEFLGP------AAL-LHAYrw 228
Cdd:PRK12386  109 EKAREIPSFTPPKDLQPG--EYRMQQVDVERSQEFRKCIECFLCQNVChvvRDHEENKPAFAGPrflmriAELeMHPL-- 184

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1735202923 229 isDSRDEFKEerlqaiAEDETKLYRCRTVKNCTATCP 265
Cdd:PRK12386  185 --DTADRRAE------AQEEHGLGYCNITKCCTEVCP 213
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 196-268 3.17e-06

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: 43.84  E-value: 3.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735202923 196 CILCACCSTSCPPYwwnpeeflgpaaLLHAYRWISDSRD--EFKEERLQAIAEDETKLYRCRTVKNCTATCPKSL 268
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 104-153 1.11e-05

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 45.59  E-value: 1.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1735202923 104 CREGICGSCAMNIDG------ANTVAC------LKPIDADTSKPTIITPLPhmyVIKDLVVD 153
Cdd:PRK07570   58 CREGICGMCGLVINGrphgpdRGTTTCqlhmrsFKDGDTITIEPWRAAAFP---VIKDLVVD 116
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 195-269 2.39e-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: 41.29  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1735202923 195 ECILCACCSTSCPPYWWNPEEflgPAALlhAYRWISDSRDEfkeerlqaiAEDETKLYRCRTVKNCTATCPKSLD 269
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKL--MRAAYLGDLEE---------LQANKVANLCSECGLCEYACPMGLD 61
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 182-281 1.22e-03

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 40.06  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735202923 182 QTPAERKKLDGLYECILCACCSTSCPPYWWNPEEFLGPAALLHAYRwisdsrdEFKEERLQAIAEDETK--LYRCRTVKN 259
Cdd:COG0247    66 KTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLR-------EVLEGELPLDLSEEVYevLDLCLTCKA 138

                          90       100
                  ....*....|....*....|..
gi 1735202923 260 CTATCPKSLDPSSAIHHMKAMH 281
Cdd:COG0247   139 CETACPSGVDIADLIAEARAQL 160
 
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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