Protein : Qrob_P0338650.2 Q. robur
Protein Identifier  ? Qrob_P0338650.2 Organism . Name  Quercus robur
Protein Description  (M=1) PTHR10681//PTHR10681:SF91 - THIOREDOXIN PEROXIDASE // SUBFAMILY NOT NAMED (PTHR10681:SF91) Alias (in v1)  Qrob_P0006260.1
Gene Prediction Quality  manual_v1 Protein length 

Sequence

Length: 249  
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0 Synonyms

3 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:0016209 antioxidant activity Inhibition of the reactions brought about by dioxygen (O2) or peroxides. Usually the antioxidant is effective because it can itself be more easily oxidized than the substance protected. The term is often applied to components that can trap free radicals, thereby breaking the chain reaction that normally leads to extensive biological damage.

22 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100253998 8 246 + 239 Gaps:11 91.94 248 82.02 7e-131 uncharacterized LOC100253998
blastp_kegg lcl|pmum:103336375 44 248 + 205 none 82.00 250 85.37 1e-129 uncharacterized LOC103336375
blastp_kegg lcl|cit:102623534 1 246 + 246 Gaps:11 99.20 251 74.70 2e-128 uncharacterized LOC102623534
blastp_kegg lcl|tcc:TCM_035468 24 244 + 221 Gaps:7 72.19 302 83.49 2e-127 V(D)J recombination-activating protein 2 isoform 1
blastp_kegg lcl|sot:102589252 44 244 + 201 none 78.52 256 86.07 3e-126 uncharacterized LOC102589252
blastp_kegg lcl|mdm:103402175 1 244 + 244 Gaps:21 100.00 247 76.52 1e-125 uncharacterized LOC103402175
blastp_kegg lcl|sly:101266329 44 244 + 201 none 79.13 254 84.58 5e-124 uncharacterized LOC101266329
blastp_kegg lcl|gmx:100780633 27 245 + 219 Gaps:3 85.71 252 80.56 1e-123 uncharacterized LOC100780633
blastp_kegg lcl|rcu:RCOM_0137700 2 244 + 243 Gaps:24 97.41 270 68.82 3e-123 hypothetical protein
blastp_kegg lcl|gmx:100806693 30 244 + 215 Gaps:3 86.18 246 83.02 8e-123 uncharacterized LOC100806693
blastp_pdb 2ywi_B 66 244 + 179 Gaps:4 89.29 196 50.86 2e-62 mol:protein length:196 Hypothetical conserved protein
blastp_pdb 2ywi_A 66 244 + 179 Gaps:4 89.29 196 50.86 2e-62 mol:protein length:196 Hypothetical conserved protein
blastp_pdb 3u5r_H 58 242 + 185 Gaps:5 82.57 218 48.33 2e-53 mol:protein length:218 uncharacterized protein
blastp_pdb 3u5r_G 58 242 + 185 Gaps:5 82.57 218 48.33 2e-53 mol:protein length:218 uncharacterized protein
blastp_pdb 3u5r_F 58 242 + 185 Gaps:5 82.57 218 48.33 2e-53 mol:protein length:218 uncharacterized protein
blastp_pdb 3u5r_E 58 242 + 185 Gaps:5 82.57 218 48.33 2e-53 mol:protein length:218 uncharacterized protein
blastp_pdb 2ywo_A 60 244 + 185 Gaps:10 95.21 188 41.90 2e-33 mol:protein length:188 Probable thiol-disulfide isomerase/thioredoxi
blastp_pdb 2cvb_A 60 244 + 185 Gaps:10 95.21 188 41.90 2e-33 mol:protein length:188 probable thiol-disulfide isomerase/thioredoxi
rpsblast_cdd gnl|CDD|48518 67 242 + 176 Gaps:5 100.00 171 53.80 2e-65 cd02969 PRX_like1 Peroxiredoxin (PRX)-like 1 family hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs which aligns to the second cysteine in the CXXC motif of TRX. In addition these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide peroxynitrate and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin glutathione trypanothione and AhpF..
rpsblast_cdd gnl|CDD|201319 71 188 + 118 Gaps:15 92.74 124 25.22 5e-13 pfam00578 AhpC-TSA AhpC/TSA family. This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).
rpsblast_cdd gnl|CDD|203972 71 188 + 118 Gaps:13 82.39 142 27.35 3e-10 pfam08534 Redoxin Redoxin. This family of redoxins includes peroxiredoxin thioredoxin and glutaredoxin proteins.
rpsblast_cdd gnl|CDD|48515 72 188 + 117 Gaps:8 93.97 116 28.44 5e-09 cd02966 TlpA_like_family TlpA-like family composed of TlpA ResA DsbE and similar proteins. TlpA ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert approximately 25 residues in length which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3 while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases..

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 50 248 199 PTHR10681 none none none
ProSiteProfiles 64 224 161 PS51352 none Thioredoxin domain profile. IPR012336
Pfam 70 187 118 PF00578 "KEGG:00480+1.11.1.15" AhpC/TSA family IPR000866
PANTHER 50 248 199 PTHR10681:SF91 none none none
SUPERFAMILY 61 246 186 SSF52833 none none IPR012336
Gene3D 68 194 127 G3DSA:3.40.30.10 none none IPR012336

0 Localization

19 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_2003_QTL1_peak_Bud_burst_3P Qrob_Chr02 2 s_1AR8KI_1183 s_1B0QB1_473 22 6 41 lod 4,2 11,5
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_nEpis_A4 Qrob_Chr02 2 s_1BAGIZ_823 s_1BN4CB_644 23,06 23,06 23,06 lod 4.9 11
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

0 Targeting