Protein : Qrob_P0380050.2 Q. robur
Protein Identifier  ? Qrob_P0380050.2 Organism . Name  Quercus robur
Score  99.0 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: 781  
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|pop:POPTR_0001s19360g 6 780 + 775 Gaps:2 96.16 808 86.62 0.0 POPTRDRAFT_829577 phospholipase D family protein
blastp_kegg lcl|rcu:RCOM_0899520 4 780 + 777 Gaps:2 96.41 808 86.78 0.0 phopholipase d alpha putative (EC:3.1.4.4)
blastp_kegg lcl|pop:POPTR_0003s02730g 6 780 + 775 Gaps:2 96.16 808 86.36 0.0 phospholipase D family protein
blastp_kegg lcl|gmx:100786410 8 780 + 773 Gaps:2 95.80 809 87.23 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|gmx:100794849 8 780 + 773 Gaps:2 95.80 809 86.71 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|cam:101501626 5 780 + 776 Gaps:17 96.22 793 87.55 0.0 phospholipase D alpha 1-like
blastp_kegg lcl|tcc:TCM_027158 4 780 + 777 Gaps:2 96.29 809 85.11 0.0 Phospholipase D alpha 2 isoform 1
blastp_kegg lcl|pvu:PHAVU_010G155000g 8 780 + 773 Gaps:3 95.92 809 85.70 0.0 hypothetical protein
blastp_kegg lcl|pvu:PHAVU_005G177300g 6 780 + 775 Gaps:2 96.28 807 85.71 0.0 hypothetical protein
blastp_kegg lcl|vvi:100232987 4 780 + 777 Gaps:3 96.42 809 84.62 0.0 PLD phospholipase D alpha
blastp_uniprot_sprot sp|Q41142|PLDA1_RICCO 4 780 + 777 Gaps:2 96.41 808 86.52 0.0 Phospholipase D alpha 1 OS Ricinus communis GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|O04865|PLDA1_VIGUN 8 780 + 773 Gaps:3 95.92 809 85.05 0.0 Phospholipase D alpha 1 OS Vigna unguiculata GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|P86387|PLDA1_CARPA 6 780 + 775 Gaps:2 96.16 808 84.04 0.0 Phospholipase D alpha 1 OS Carica papaya GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 6 780 + 775 Gaps:2 96.16 808 83.53 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q38882|PLDA1_ARATH 6 780 + 775 Gaps:3 96.05 810 82.01 0.0 Phospholipase D alpha 1 OS Arabidopsis thaliana GN PLDALPHA1 PE 1 SV 2
blastp_uniprot_sprot sp|Q9SSQ9|PLDA2_ARATH 6 780 + 775 Gaps:3 96.05 810 81.75 0.0 Phospholipase D alpha 2 OS Arabidopsis thaliana GN PLDALPHA2 PE 2 SV 1
blastp_uniprot_sprot sp|O82549|PLDA1_BRAOC 6 780 + 775 Gaps:3 96.05 810 81.36 0.0 Phospholipase D alpha 1 OS Brassica oleracea var. capitata GN PLD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q43007|PLDA1_ORYSJ 4 780 + 777 Gaps:1 95.81 812 80.59 0.0 Phospholipase D alpha 1 OS Oryza sativa subsp. japonica GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|P55939|PLDA2_BRAOC 6 780 + 775 Gaps:4 95.94 812 79.97 0.0 Phospholipase D alpha 2 OS Brassica oleracea var. capitata GN PLD2 PE 1 SV 2
blastp_uniprot_sprot sp|Q70EW5|PLDA1_CYNCA 6 780 + 775 Gaps:2 96.16 808 77.73 0.0 Phospholipase D alpha 1 OS Cynara cardunculus GN PLD1 PE 1 SV 2
rpsblast_cdd gnl|CDD|165912 6 780 + 775 Gaps:2 96.16 808 87.13 0.0 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|165993 24 780 + 757 Gaps:57 94.99 758 46.53 0.0 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|178585 24 780 + 757 Gaps:72 90.90 868 45.75 0.0 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|197295 464 673 + 210 Gaps:1 100.00 211 88.15 1e-119 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 464 673 + 210 Gaps:4 100.00 208 71.15 1e-104 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 173 350 + 178 none 100.00 178 84.27 1e-101 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 173 350 + 178 Gaps:4 100.00 176 64.20 1e-81 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|197296 464 676 + 213 Gaps:6 100.00 211 60.66 2e-78 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|197294 173 352 + 180 Gaps:6 100.00 180 56.67 1e-63 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 468 664 + 197 Gaps:34 94.54 183 42.20 6e-43 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.

28 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 181 453 273 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 469 606 138 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
PANTHER 624 779 156 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 4 160 157 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
SMART 9 98 90 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
Pfam 627 653 27 PF00614 none Phospholipase D Active site motif IPR001736
Pfam 298 336 39 PF00614 none Phospholipase D Active site motif IPR001736
PIRSF 4 780 777 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
Gene3D 472 584 113 G3DSA:3.30.870.10 none none none
Gene3D 373 407 35 G3DSA:3.30.870.10 none none none
Gene3D 619 667 49 G3DSA:3.30.870.10 none none none
Gene3D 178 341 164 G3DSA:3.30.870.10 none none none
SMART 626 653 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 298 336 39 SM00155 none Phospholipase D. Active site motifs. IPR001736
SUPERFAMILY 372 416 45 SSF56024 none none none
SUPERFAMILY 124 343 220 SSF56024 none none none
ProSiteProfiles 298 336 39 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Pfam 697 771 75 PF12357 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" Phospholipase D C terminal IPR024632
Gene3D 18 120 103 G3DSA:2.60.40.150 none none IPR000008
SUPERFAMILY 18 122 105 SSF49562 none none IPR000008
Pfam 19 82 64 PF00168 none C2 domain IPR000008
PANTHER 469 606 138 PTHR18896:SF56 none none none
PANTHER 624 779 156 PTHR18896:SF56 none none none
PANTHER 4 160 157 PTHR18896:SF56 none none none
SUPERFAMILY 452 576 125 SSF56024 none none none
SUPERFAMILY 622 709 88 SSF56024 none none none
PANTHER 181 453 273 PTHR18896:SF56 none none none
ProSiteProfiles 626 653 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736

0 Localization

13 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_nPriLBD_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,36 0 30,43 lod 2,5806 5,1
Bourran2_2014_nEpis*_A4 Qrob_Chr07 7 v_12400_446 s_1BPEBU_1211 6,93 0 15,13 lod 4,7411 11
Bourran2_2014_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2014_nP_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 7,9 0,09 30,09 lod 2,3636 5
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_nEpiBC_A4 Qrob_Chr07 7 s_1DP9TW_798 v_8128_173 22,61 22,14 22,73 lod 3.1 8.5
Bourran2_2014_nEpiBC_A4 Qrob_Chr07 7 s_2FI9D9_500 s_1AXDMJ_325 12,26 0 34,9 lod 2,2306 6,1
Bourran2_2014_nPriBD_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 5,54 0,4 20,6 lod 2,6345 5,9
Bourran2_2002_QTL10_peak_Bud_burst_3P Qrob_Chr07 7 s_1CAWP_311 s_1BEZ9M_461 7,5 0 21,5 lod 3,7 6,3
Bourran2_2014_nPriBD*_A4 Qrob_Chr07 7 s_1A7UI0_596 s_1A3H6S_352 8,02 0 20,53 lod 4,1062 10,8
Bourran2_2014_nPriLBD*_A4 Qrob_Chr07 7 s_1C6BY7_802 s_1BPEBU_1211 7,15 0 16,34 lod 3,9419 10,2

0 Targeting