6 GO Terms
Identifier | Name | Description |
---|---|---|
GO:0016491 | oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
GO:0055114 | oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
GO:0009055 | electron carrier activity | Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. |
GO:0006099 | tricarboxylic acid cycle | A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. |
GO:0051536 | iron-sulfur cluster binding | Interacting selectively and non-covalently with an iron-sulfur cluster, a combination of iron and sulfur atoms. |
GO:0051537 | 2 iron, 2 sulfur cluster binding | Interacting selectively and non-covalently with a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. |
41 Blast
13 Domain Motifs
Analysis | Begin | End | Length | Domain Identifier | Cross Ref | Description | Inter Pro |
---|---|---|---|---|---|---|---|
SUPERFAMILY | 44 | 145 | 102 | SSF54292 | none | none | IPR001041 |
PANTHER | 21 | 270 | 250 | PTHR11921 | none | none | none |
Gene3D | 146 | 273 | 128 | G3DSA:1.10.1060.10 | none | none | none |
TIGRFAM | 49 | 270 | 222 | TIGR00384 | "KEGG:00020+1.3.5.1","KEGG:00190+1.3.5.1","KEGG:00650+1.3.5.1","KEGG:00720+1.3.5.1","MetaCyc:PWY-3781","MetaCyc:PWY-4302","MetaCyc:PWY-561","MetaCyc:PWY-5690","MetaCyc:PWY-6728","MetaCyc:PWY-6969","MetaCyc:PWY-7254","MetaCyc:PWY-7279" | dhsB: succinate dehydrogenase and fumarate reductase iron-sulfur protein | IPR004489 |
ProSiteProfiles | 58 | 136 | 79 | PS51085 | none | 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. | IPR001041 |
ProSitePatterns | 189 | 200 | 12 | PS00198 | none | 4Fe-4S ferredoxin-type iron-sulfur binding region signature. | IPR017900 |
ProSiteProfiles | 179 | 209 | 31 | PS51379 | none | 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. | IPR017896 |
ProSitePatterns | 97 | 105 | 9 | PS00197 | none | 2Fe-2S ferredoxin-type iron-sulfur binding region signature. | IPR006058 |
SUPERFAMILY | 146 | 272 | 127 | SSF46548 | none | none | IPR009051 |
Pfam | 188 | 261 | 74 | PF13534 | none | 4Fe-4S dicluster domain | none |
Gene3D | 38 | 145 | 108 | G3DSA:3.10.20.30 | none | none | IPR012675 |
Pfam | 46 | 151 | 106 | PF13085 | "KEGG:00020+1.3.5.1","KEGG:00190+1.3.5.1","KEGG:00650+1.3.5.1","KEGG:00720+1.3.5.1","MetaCyc:PWY-3781","MetaCyc:PWY-4302","MetaCyc:PWY-561","MetaCyc:PWY-5690","MetaCyc:PWY-6728","MetaCyc:PWY-6969","MetaCyc:PWY-7254","MetaCyc:PWY-7279" | 2Fe-2S iron-sulfur cluster binding domain | IPR025192 |
PANTHER | 21 | 270 | 250 | PTHR11921:SF8 | none | none | none |
17 Qtllist
Qtl Name | Chromosome Name | Linkage Group | Prox Marker | Dist Marker | Position QTL | Pos One | Pos Two | Test Type | Test Value | R 2 |
---|---|---|---|---|---|---|---|---|---|---|
Bourran1_2003_QTL2_peak_Bud_burst_A4 | Qrob_Chr02 | 2 | s_1B0H8U_259 | s_1CB1VL_554 | 17 | 0 | 87 | lod | 3,3 | 8,7 |
Bourran2_2004_QTL9_peak_Bud_burst_3P | Qrob_Chr02 | 2 | s_1C34E9_788 | v_12238_322 | 50 | 25 | 75 | lod | 4,4 | 10,1 |
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL2_d13Cf | Qrob_Chr02 | 2 | s_1AQA4Z_1644 | s_1AK5QX_947 | 53.67 | 14,01 | 79,68 | lod | 5.6594 | 0.03 |
Bourran1_2004_QTL2_peak_Bud_burst_3P | Qrob_Chr02 | 2 | s_1AW12F_382 | s_1A77MR_223 | 42 | 6 | 64 | lod | 3,6 | 9,6 |
Bourran2_2002_QTL7_peak_Bud_burst_3P | Qrob_Chr02 | 2 | s_1ANG6_1446 | v_11270_161 | 40 | 29 | 52 | lod | 8,1 | 16 |
Bourran2_2002_QTL9_peak_Bud_burst_A4 | Qrob_Chr02 | 2 | s_1BFNDA_375 | s_1A3VA1_2139 | 32,5 | 17 | 62 | lod | 3,1 | 4,2 |
Bourran2_2003_QTL8_peak_Bud_burst_3P | Qrob_Chr02 | 2 | s_1ANG6_1446 | v_11270_161 | 40 | 0 | 72 | lod | 4,4 | 9,9 |
Bourran2_2014_nP_A4 | Qrob_Chr11 | 11 | s_1B58GB_1413 | s_1A5BYY_1671 | 11,15 | 0 | 42,38 | lod | 1,8913 | 4,5 |
Bourran2_2015_nP_A4 | Qrob_Chr02 | 2 | s_1A0FUE_1868 | s_1A1UAI_500 | 20,64 | 20,47 | 21,36 | lod | 5.8 | 10.9 |
Bourran2_2015_nPriLBD_A4 | Qrob_Chr02 | 2 | s_1CP5DI_1183 | s_1A63ZX_1277 | 24,87 | 24,63 | 26,18 | lod | 3.8 | 7 |
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL6_d13Cf | Qrob_Chr02 | 2 | s_1AEP21_172 | v_6048_204 | 46.33 | 22,5 | 65,23 | lod | 4.972 | 0.03 |
Bourran2_2015_nEpis_A4 | Qrob_Chr09 | 9 | v_15847_485 | v_8329_369 | 34,94 | 34,88 | 37,45 | lod | 3.1 | 7 |
Bourran2_2015_nSecLBD_A4 | Qrob_Chr09 | 9 | v_15847_485 | v_8329_369 | 35,81 | 34,88 | 37,45 | lod | 4.4 | 10.4 |
Bourran1_2004_QTL3_peak_Bud_burst_A4 | Qrob_Chr02 | 2 | s_1B0H8U_259 | s_1CB1VL_554 | 17 | 0 | 46 | lod | 2,9 | 6,4 |
Bourran2_2015_nEpiBC_A4 | Qrob_Chr07 | 7 | s_1DP9TW_798 | v_8128_173 | 22,61 | 22,14 | 22,73 | lod | 3.1 | 8.5 |
Champenoux_2015_nP_A4 | Qrob_Chr02 | 2 | s_1BN4CB_644 | v_508_128 | 23,76 | 23,06 | 24,51 | lod | 2.8 | 6.2 |
Champenoux_2015_nPriLBD_A4 | Qrob_Chr02 | 2 | s_1CP5DI_1183 | s_1A63ZX_1277 | 25,35 | 24,63 | 26,18 | lod | 4.0 | 8.7 |