Protein : Qrob_P0437970.2 Q. robur
Protein Identifier  ? Qrob_P0437970.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=4) PTHR18896//PTHR18896:SF56 - PHOSPHOLIPASE D // SUBFAMILY NOT NAMED Code Enzyme  EC:3.1.4.4
Gene Prediction Quality  validated Protein length 

Sequence

Length: 768  
Kegg Orthology  K01115
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0 Synonyms

6 GO Terms

Identifier Name Description
GO:0005515 protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
GO:0016020 membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
GO:0003824 catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0005509 calcium ion binding Interacting selectively and non-covalently with calcium ions (Ca2+).
GO:0004630 phospholipase D activity Catalysis of the reaction: a phosphatidylcholine + H2O = choline + a phosphatidate.
GO:0046470 phosphatidylcholine metabolic process The chemical reactions and pathways involving phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. They are important constituents of cell membranes.

31 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|rcu:RCOM_0924040 3 767 + 765 Gaps:5 93.51 817 69.90 0.0 phopholipase d alpha putative (EC:3.1.4.4)
blastp_kegg lcl|pxb:103946698 2 767 + 766 Gaps:7 94.55 807 69.72 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|pper:PRUPE_ppa001818mg 3 767 + 765 Gaps:11 99.61 761 70.18 0.0 hypothetical protein
blastp_kegg lcl|mdm:103456204 2 767 + 766 Gaps:7 94.20 810 69.59 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|pmum:103319699 2 767 + 766 Gaps:11 94.17 806 70.22 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|csv:101207900 3 767 + 765 Gaps:6 94.44 810 69.15 0.0 phospholipase D alpha 2-like
blastp_kegg lcl|cmo:103488309 3 767 + 765 Gaps:6 93.98 814 69.15 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|fve:101296068 4 767 + 764 Gaps:8 96.23 796 69.06 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|gmx:100786410 7 767 + 761 Gaps:5 94.19 809 67.45 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|pvu:PHAVU_005G177300g 7 767 + 761 Gaps:5 94.42 807 67.98 0.0 hypothetical protein
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 9 767 + 759 Gaps:5 94.06 808 68.68 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q41142|PLDA1_RICCO 7 767 + 761 Gaps:5 94.31 808 68.11 0.0 Phospholipase D alpha 1 OS Ricinus communis GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q43007|PLDA1_ORYSJ 6 767 + 762 Gaps:4 93.84 812 67.06 0.0 Phospholipase D alpha 1 OS Oryza sativa subsp. japonica GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|O04865|PLDA1_VIGUN 7 767 + 761 Gaps:6 94.31 809 66.84 0.0 Phospholipase D alpha 1 OS Vigna unguiculata GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|P86387|PLDA1_CARPA 7 767 + 761 Gaps:5 94.31 808 67.85 0.0 Phospholipase D alpha 1 OS Carica papaya GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q38882|PLDA1_ARATH 7 767 + 761 Gaps:6 94.20 810 66.45 0.0 Phospholipase D alpha 1 OS Arabidopsis thaliana GN PLDALPHA1 PE 1 SV 2
blastp_uniprot_sprot sp|P55939|PLDA2_BRAOC 7 767 + 761 Gaps:7 94.09 812 67.02 0.0 Phospholipase D alpha 2 OS Brassica oleracea var. capitata GN PLD2 PE 1 SV 2
blastp_uniprot_sprot sp|Q9SSQ9|PLDA2_ARATH 7 767 + 761 Gaps:6 94.20 810 65.66 0.0 Phospholipase D alpha 2 OS Arabidopsis thaliana GN PLDALPHA2 PE 2 SV 1
blastp_uniprot_sprot sp|Q70EW5|PLDA1_CYNCA 8 767 + 760 Gaps:5 94.18 808 66.36 0.0 Phospholipase D alpha 1 OS Cynara cardunculus GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|O82549|PLDA1_BRAOC 7 767 + 761 Gaps:6 94.20 810 65.53 0.0 Phospholipase D alpha 1 OS Brassica oleracea var. capitata GN PLD1 PE 2 SV 1
rpsblast_cdd gnl|CDD|165912 7 767 + 761 Gaps:5 94.31 808 68.50 0.0 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|165993 6 767 + 762 Gaps:62 95.51 758 47.79 0.0 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|178585 2 767 + 766 Gaps:71 91.82 868 44.67 0.0 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|197295 449 658 + 210 Gaps:1 100.00 211 77.73 1e-106 cd09199 PLDc_pPLDalpha_2 Catalytic domain repeat 2 of plant alpha-type phospholipase D. Catalytic domain repeat 2 of plant alpha-type phospholipase D (PLDalpha EC 3.1.4.4). Plant PLDalpha is a phosphatidylinositol 4 5-bisphosphate (PIP2)-independent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require millimolar calcium for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes the monomer of plant PLDalpha consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDalpha may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group.
rpsblast_cdd gnl|CDD|197240 449 658 + 210 Gaps:4 100.00 208 69.71 1e-101 cd09142 PLDc_pPLD_like_2 Catalytic domain repeat 2 of plant phospholipase D and similar proteins. Catalytic domain repeat 2 of plant phospholipase D (PLD EC 3.1.4.4) and similar proteins. Plant PLDs have broad substrate specificity and can hydrolyze the terminal phosphodiester bond of several common membrane phospholipids such as phosphatidylcholine (PC) phosphatidylethanolamine (PE) phosphatidylglycerol (PG) and phosphatidylserine (PS) with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols by which various phospholipids can be synthesized. Most plant PLDs possess a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require calcium for activity which is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes the monomer of plant PLDs consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDs may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group. This subfamily includes two types of plant PLDs alpha-type and beta-type PLDs which are derived from different gene products and distinctly regulated. The zeta-type PLD from Arabidopsis is not included in this subfamily.
rpsblast_cdd gnl|CDD|197296 449 654 + 206 Gaps:6 96.68 211 63.24 2e-77 cd09200 PLDc_pPLDbeta_2 Catalytic domain repeat 2 of plant beta-type phospholipase D. Catalytic domain repeat 2 of plant beta-type phospholipase D (PLDbeta EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes the monomer of plant PLDbeta consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group.
rpsblast_cdd gnl|CDD|197293 160 335 + 176 Gaps:1 99.44 178 65.54 3e-76 cd09197 PLDc_pPLDalpha_1 Catalytic domain repeat 1 of plant alpha-type phospholipase D. Catalytic domain repeat 1 of plant alpha-type phospholipase D (PLDalpha EC 3.1.4.4). Plant PLDalpha is a phosphatidylinositol 4 5-bisphosphate (PIP2)-independent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require millimolar calcium for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes the monomer of plant PLDalpha consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDalpha may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group.
rpsblast_cdd gnl|CDD|197237 160 335 + 176 Gaps:5 99.43 176 55.43 4e-69 cd09139 PLDc_pPLD_like_1 Catalytic domain repeat 1 of plant phospholipase D and similar proteins. Catalytic domain repeat 1 of plant phospholipase D (PLD EC 3.1.4.4) and similar proteins. Plant PLDs have broad substrate specificity and can hydrolyze the terminal phosphodiester bond of several common membrane phospholipids such as phosphatidylcholine (PC) phosphatidylethanolamine (PE) phosphatidylglycerol (PG) and phosphatidylserine (PS) with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols by which various phospholipids can be synthesized. Most plant PLDs possess a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require calcium for activity which is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes the monomer of plant PLDs consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDs may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group. This subfamily includes two types of plant PLDs alpha-type and beta-type PLDs which are derived from different gene products and distinctly regulated. The zeta-type PLD from Arabidopsis is not included in this subfamily.
rpsblast_cdd gnl|CDD|197294 160 337 + 178 Gaps:7 99.44 180 51.40 9e-61 cd09198 PLDc_pPLDbeta_1 Catalytic domain repeat 1 of plant beta-type phospholipase D. Catalytic domain repeat 1 of plant beta-type phospholipase D (PLDbeta EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes the monomer of plant PLDbeta consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group.
rpsblast_cdd gnl|CDD|197239 451 649 + 199 Gaps:34 95.63 183 42.29 2e-41 cd09141 PLDc_vPLD1_2_yPLD_like_2 Catalytic domain repeat 2 of vertebrate phospholipases PLD1 and PLD2 yeast PLDs and similar proteins. Catalytic domain repeat 2 of vertebrate phospholipases D (PLD1 and PLD2) yeast phospholipase D (PLD SPO14/PLD1) and other similar eukaryotic proteins. These PLD enzymes play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols by which various phospholipids can be synthesized. The vertebrate PLD1 and PLD2 are membrane associated phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent enzymes that selectively hydrolyze phosphatidylcholine (PC). Protein cofactors and calcium may be required for their activation. Yeast SPO14/PLD1 is a calcium-independent PLD which needs PIP2 for its activity. Instead of the regulatory calcium-dependent phospholipid-binding C2 domain in plants most mammalian and yeast PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at the N-terminus which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. The PX and PH domains are also present in zeta-type PLD from Arabidopsis which is more closely related to vertebrate PLDs than to other plant PLD types. In addition this subfamily also includes some related proteins which have either PX-like or PH domains in their N-termini. Like other members of the PLD superfamily the monomer of mammalian and yeast PLDs consists of two catalytic domains each containing one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from the two domains form a single active site. These PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group.

26 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SMART 2 84 83 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
PANTHER 7 146 140 PTHR18896 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039";signature_desc=PHOSPHOLIPASE D none IPR015679
PANTHER 167 438 272 PTHR18896 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039";signature_desc=PHOSPHOLIPASE D none IPR015679
PANTHER 609 766 158 PTHR18896:SF56 none none none
PANTHER 454 591 138 PTHR18896:SF56 none none none
PANTHER 7 146 140 PTHR18896:SF56 none none none
PANTHER 167 438 272 PTHR18896:SF56 none none none
SUPERFAMILY 111 324 214 SSF56024 none none none
SUPERFAMILY 357 390 34 SSF56024 none none none
SUPERFAMILY 6 107 102 SSF49562 none none IPR000008
Gene3D 604 654 51 G3DSA:3.30.870.10 none none none
Gene3D 458 560 103 G3DSA:3.30.870.10 none none none
Gene3D 169 389 221 G3DSA:3.30.870.10 none none none
Pfam 612 638 27 PF00614 none Phospholipase D Active site motif IPR001736
Pfam 283 321 39 PF00614 none Phospholipase D Active site motif IPR001736
SUPERFAMILY 435 561 127 SSF56024 none none none
SUPERFAMILY 607 679 73 SSF56024 none none none
PIRSF 1 767 767 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
Pfam 685 758 74 PF12357 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" Phospholipase D C terminal IPR024632
Pfam 6 68 63 PF00168 none C2 domain IPR000008
SMART 611 638 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 283 321 39 SM00155 none Phospholipase D. Active site motifs. IPR001736
PANTHER 609 766 158 PTHR18896 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039";signature_desc=PHOSPHOLIPASE D none IPR015679
PANTHER 454 591 138 PTHR18896 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039";signature_desc=PHOSPHOLIPASE D none IPR015679
Gene3D 7 106 100 G3DSA:2.60.40.150 none none IPR000008
ProSiteProfiles 611 638 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736

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