Protein : Qrob_P0176520.2 Q. robur
Protein Identifier  ? Qrob_P0176520.2 Organism . Name  Quercus robur
Score  78.6 Score Type  egn
Protein Description  (M=1) K02260 - cytochrome c oxidase subunit XVII assembly protein Gene Prediction Quality  validated
Protein length 

Sequence

Length: 105  
Kegg Orthology  K02260
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0005507 copper ion binding Interacting selectively and non-covalently with copper (Cu) ions.
GO:0005758 mitochondrial intermembrane space The region between the inner and outer lipid bilayers of the mitochondrial envelope.
GO:0006825 copper ion transport The directed movement of copper (Cu) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
GO:0016531 copper chaperone activity Assists in the delivery of copper ions to target proteins or compartments.

24 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_031514 26 104 + 79 Gaps:1 100.00 78 76.92 7e-35 Cytochrome C oxidase copper chaperone isoform 1
blastp_kegg lcl|pmum:103326208 26 104 + 79 Gaps:2 100.00 81 75.31 3e-34 cytochrome c oxidase copper chaperone 1
blastp_kegg lcl|pper:PRUPE_ppa021425mg 26 104 + 79 Gaps:2 100.00 81 75.31 4e-34 hypothetical protein
blastp_kegg lcl|pxb:103947617 26 104 + 79 Gaps:1 100.00 80 77.50 7e-34 cytochrome c oxidase copper chaperone 2
blastp_kegg lcl|rcu:RCOM_0507800 26 104 + 79 Gaps:1 100.00 80 73.75 8e-34 Cytochrome c oxidase copper chaperone putative
blastp_kegg lcl|sly:101267272 26 104 + 79 none 100.00 79 70.89 9e-34 cytochrome c oxidase copper chaperone-like
blastp_kegg lcl|pxb:103933133 26 104 + 79 Gaps:1 100.00 80 76.25 3e-33 cytochrome c oxidase copper chaperone 2-like
blastp_kegg lcl|csv:101205238 26 104 + 79 Gaps:1 100.00 80 73.75 3e-33 cytochrome c oxidase copper chaperone-like
blastp_kegg lcl|sot:102597281 26 104 + 79 none 100.00 79 69.62 4e-33 cytochrome c oxidase copper chaperone 1-like
blastp_kegg lcl|mdm:103448680 26 104 + 79 Gaps:1 100.00 80 76.25 8e-33 cytochrome c oxidase copper chaperone 2
blastp_pdb 2rnb_A 55 104 + 50 Gaps:2 77.61 67 53.85 3e-13 mol:protein length:67 Cytochrome c oxidase copper chaperone
blastp_pdb 2rn9_A 55 104 + 50 Gaps:2 77.61 67 53.85 3e-13 mol:protein length:67 Cytochrome c oxidase copper chaperone
blastp_pdb 2l0y_B 55 104 + 50 Gaps:2 77.61 67 48.08 2e-11 mol:protein length:67 COX17 cytochrome c oxidase assembly homolog (
blastp_pdb 2lgq_A 55 104 + 50 Gaps:2 77.61 67 50.00 3e-11 mol:protein length:67 Cytochrome c oxidase copper chaperone
blastp_uniprot_sprot sp|Q9LJQ9|CX171_ARATH 44 104 + 61 none 82.43 74 72.13 2e-26 Cytochrome c oxidase copper chaperone 1 OS Arabidopsis thaliana GN COX17-1 PE 2 SV 1
blastp_uniprot_sprot sp|Q94FT1|CX172_ARATH 45 104 + 60 none 83.33 72 70.00 2e-23 Cytochrome c oxidase copper chaperone 2 OS Arabidopsis thaliana GN COX17-2 PE 3 SV 1
blastp_uniprot_sprot sp|Q54ID0|COX17_DICDI 52 104 + 53 none 88.33 60 62.26 7e-17 Cytochrome c oxidase copper chaperone OS Dictyostelium discoideum GN cox17 PE 3 SV 1
blastp_uniprot_sprot sp|P81045|COX17_PIG 49 104 + 56 Gaps:2 93.55 62 50.00 1e-13 Cytochrome c oxidase copper chaperone OS Sus scrofa GN COX17 PE 1 SV 1
blastp_uniprot_sprot sp|Q6J3Q7|COX17_CANFA 49 104 + 56 Gaps:3 93.65 63 50.85 1e-12 Cytochrome c oxidase copper chaperone OS Canis familiaris GN COX17 PE 3 SV 3
blastp_uniprot_sprot sp|Q14061|COX17_HUMAN 55 104 + 50 Gaps:2 82.54 63 53.85 1e-12 Cytochrome c oxidase copper chaperone OS Homo sapiens GN COX17 PE 1 SV 2
blastp_uniprot_sprot sp|P56394|COX17_MOUSE 62 104 + 43 none 68.25 63 58.14 6e-12 Cytochrome c oxidase copper chaperone OS Mus musculus GN Cox17 PE 3 SV 2
blastp_uniprot_sprot sp|Q9P7Z7|COX17_SCHPO 60 104 + 45 Gaps:2 67.14 70 46.81 4e-08 Cytochrome c oxidase copper chaperone OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN cox17 PE 3 SV 1
rpsblast_cdd gnl|CDD|203162 56 104 + 49 Gaps:1 100.00 48 62.50 2e-17 pfam05051 COX17 Cytochrome C oxidase copper chaperone (COX17). Cox17 is essential for the assembly of functional cytochrome c oxidase (CCO) and for delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast. The structure of Cox17 shows the protein to have an unstructured N-terminal region followed by two helices and several unstructured C-terminal residues. The Cu(I) binding site has been modelled as two-coordinate with ligation by conserved residues Cys23 and Cys26.
rpsblast_kog gnl|CDD|38706 49 104 + 56 none 77.78 72 53.57 4e-16 KOG3496 KOG3496 KOG3496 Cytochrome c oxidase assembly protein/Cu2+ chaperone COX17 [Posttranslational modification protein turnover chaperones].

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 50 104 55 SSF47072 none none IPR009069
Phobius 1 3 3 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
ProDom 58 104 47 PD014904 none COPPER CHAPERONE C OXIDASE CYTOCHROME COX17 CHAPERONE METAL-BINDING MITOCHONDRION ASSEMBLY IPR007745
Gene3D 68 98 31 G3DSA:1.10.810.10 none none IPR009069
Phobius 1 20 20 SIGNAL_PEPTIDE none Signal peptide region none
PANTHER 35 104 70 PTHR16719 none none IPR007745
Phobius 16 20 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Pfam 57 104 48 PF05051 none Cytochrome C oxidase copper chaperone (COX17) IPR007745
Phobius 21 104 84 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 4 15 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none

0 Localization

15 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2014_aSeqBC_A4 Qrob_Chr08 8 v_15999_278 v_AP13YL15_395 32,52 4,22 57,22 lod 2,7561 6,7
Bourran2_2014_nFork*_A4 Qrob_Chr08 8 PIE175 s_1CD7GJ_1398 31,22 5,24 57,24 lod 2,6724 6,8
Bourran2_2014_nLBD*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,25 0 35,55 lod 2,5951 6
Bourran2_2014_nP*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,19 0 31,97 lod 2,8472 6
Bourran2_2014_nPriLBD_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,36 0 30,43 lod 2,5806 5,1
Bourran2_2014_nPriLBD_A4 Qrob_Chr08 8 PIE175 v_9164_159 31,85 15,39 48,29 lod 2,8308 6,8
Bourran2_2015_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Champenoux_2015_nSeqBC_A4 Qrob_Chr08 8 v_AD7YD13_501 s_1A7IED_780 43,44 43,42 43,99 lod 3.7 8.9
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL3_d13Cf Qrob_Chr08 8 v_5216_549 v_11625_20 37.08 12,26 54,9 lod 6.5888 0.04
Bourran2_2014_nEpis*_3P Qrob_Chr08 8 s_1DA4QW_688 s_1DNI7D_820 17,96 0 37,75 lod 2,9745 7,5
Bourran2_2014_nPriBD_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 5,54 0,4 20,6 lod 2,6345 5,9

0 Targeting