Protein : Qrob_P0437960.2 Q. robur
Protein Identifier  ? Qrob_P0437960.2 Organism . Name  Quercus robur
Score  94.4 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: 769  
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 3 768 + 766 Gaps:6 93.51 817 71.47 0.0 phopholipase d alpha putative (EC:3.1.4.4)
blastp_kegg lcl|pxb:103946698 2 768 + 767 Gaps:8 94.55 807 71.43 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|fve:101296068 4 768 + 765 Gaps:9 96.23 796 71.41 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|mdm:103456204 2 768 + 767 Gaps:8 94.20 810 71.56 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|pper:PRUPE_ppa001818mg 3 768 + 766 Gaps:12 99.61 761 71.37 0.0 hypothetical protein
blastp_kegg lcl|cmo:103488309 3 768 + 766 Gaps:7 93.98 814 70.98 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|csv:101207900 3 768 + 766 Gaps:7 94.44 810 70.85 0.0 phospholipase D alpha 2-like
blastp_kegg lcl|pmum:103319699 2 768 + 767 Gaps:12 94.17 806 71.67 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|pvu:PHAVU_005G177300g 7 768 + 762 Gaps:6 94.42 807 69.82 0.0 hypothetical protein
blastp_kegg lcl|gmx:100786410 7 768 + 762 Gaps:6 94.19 809 68.90 0.0 phospholipase D alpha 1-like
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 9 768 + 760 Gaps:8 94.06 808 70.13 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q41142|PLDA1_RICCO 7 768 + 762 Gaps:8 94.31 808 69.42 0.0 Phospholipase D alpha 1 OS Ricinus communis GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|O04865|PLDA1_VIGUN 7 768 + 762 Gaps:7 94.31 809 68.55 0.0 Phospholipase D alpha 1 OS Vigna unguiculata GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|P86387|PLDA1_CARPA 7 768 + 762 Gaps:8 94.31 808 69.29 0.0 Phospholipase D alpha 1 OS Carica papaya GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9SSQ9|PLDA2_ARATH 7 768 + 762 Gaps:7 94.20 810 67.37 0.0 Phospholipase D alpha 2 OS Arabidopsis thaliana GN PLDALPHA2 PE 2 SV 1
blastp_uniprot_sprot sp|Q70EW5|PLDA1_CYNCA 8 768 + 761 Gaps:8 94.18 808 68.07 0.0 Phospholipase D alpha 1 OS Cynara cardunculus GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q43007|PLDA1_ORYSJ 6 768 + 763 Gaps:7 93.84 812 67.98 0.0 Phospholipase D alpha 1 OS Oryza sativa subsp. japonica GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q38882|PLDA1_ARATH 7 768 + 762 Gaps:9 94.20 810 67.76 0.0 Phospholipase D alpha 1 OS Arabidopsis thaliana GN PLDALPHA1 PE 1 SV 2
blastp_uniprot_sprot sp|P55939|PLDA2_BRAOC 7 768 + 762 Gaps:8 94.09 812 67.93 0.0 Phospholipase D alpha 2 OS Brassica oleracea var. capitata GN PLD2 PE 1 SV 2
blastp_uniprot_sprot sp|O82549|PLDA1_BRAOC 7 768 + 762 Gaps:9 94.20 810 66.84 0.0 Phospholipase D alpha 1 OS Brassica oleracea var. capitata GN PLD1 PE 2 SV 1
rpsblast_cdd gnl|CDD|165912 7 768 + 762 Gaps:8 94.31 808 70.08 0.0 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|165993 6 768 + 763 Gaps:63 95.51 758 48.20 0.0 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|178585 2 768 + 767 Gaps:80 91.82 868 44.29 1e-180 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|197295 449 659 + 211 none 100.00 211 79.15 1e-109 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 449 659 + 211 Gaps:3 100.00 208 70.67 1e-103 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|197293 160 335 + 176 Gaps:3 99.44 178 66.67 8e-79 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|197296 449 655 + 207 Gaps:5 96.68 211 62.75 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|197237 159 335 + 177 Gaps:5 100.00 176 57.95 8e-72 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 159 337 + 179 Gaps:13 100.00 180 52.22 2e-59 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 453 650 + 198 Gaps:35 94.54 183 43.93 5e-42 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
PANTHER 167 438 272 PTHR18896:SF56 none none none
PIRSF 1 768 768 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
Pfam 686 759 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
PANTHER 610 767 158 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 7 146 140 PTHR18896:SF56 none none none
Gene3D 7 105 99 G3DSA:2.60.40.150 none none IPR000008
PANTHER 454 592 139 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
SUPERFAMILY 357 393 37 SSF56024 none none none
SUPERFAMILY 111 324 214 SSF56024 none none none
Pfam 6 68 63 PF00168 none C2 domain IPR000008
SMART 612 639 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 283 321 39 SM00155 none Phospholipase D. Active site motifs. IPR001736
SUPERFAMILY 6 107 102 SSF49562 none none 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
SUPERFAMILY 433 561 129 SSF56024 none none none
SUPERFAMILY 608 687 80 SSF56024 none none none
ProSiteProfiles 283 321 39 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Gene3D 457 560 104 G3DSA:3.30.870.10 none none none
Gene3D 605 655 51 G3DSA:3.30.870.10 none none none
Gene3D 161 388 228 G3DSA:3.30.870.10 none none none
ProSiteProfiles 612 639 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Pfam 613 639 27 PF00614 none Phospholipase D Active site motif IPR001736
Pfam 283 321 39 PF00614 none Phospholipase D Active site motif IPR001736
PANTHER 610 767 158 PTHR18896:SF56 none none none
PANTHER 454 592 139 PTHR18896:SF56 none none none

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