Protein : Qrob_P0483580.2 Q. robur
Protein Identifier  ? Qrob_P0483580.2 Organism . Name  Quercus robur
Score  100.0 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: 754  
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|cit:102619040 1 753 + 753 Gaps:17 98.70 772 74.67 0.0 phospholipase D epsilon-like
blastp_kegg lcl|cic:CICLE_v10024940mg 1 753 + 753 Gaps:17 98.70 772 74.67 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_029016 1 753 + 753 Gaps:16 100.00 765 73.46 0.0 Phospholipase D alpha 4
blastp_kegg lcl|fve:101298884 1 753 + 753 Gaps:18 100.00 767 74.19 0.0 phospholipase D epsilon-like
blastp_kegg lcl|rcu:RCOM_0312720 1 753 + 753 Gaps:13 100.00 762 72.70 0.0 phospholipase d putative (EC:3.1.4.4)
blastp_kegg lcl|pmum:103327720 1 753 + 753 Gaps:17 100.00 766 73.89 0.0 phospholipase D epsilon
blastp_kegg lcl|vvi:100256679 1 753 + 753 Gaps:15 100.00 752 73.40 0.0 phospholipase D epsilon-like
blastp_kegg lcl|pop:POPTR_0003s02990g 1 753 + 753 Gaps:10 100.00 759 72.07 0.0 Phospholipase D epsilon family protein
blastp_kegg lcl|mtr:MTR_2g100250 6 753 + 748 Gaps:12 99.74 756 72.81 0.0 Phospholipase D epsilon
blastp_kegg lcl|cmo:103490014 1 753 + 753 Gaps:10 99.74 761 70.36 0.0 phospholipase D epsilon
blastp_uniprot_sprot sp|Q9C888|PLDE1_ARATH 1 753 + 753 Gaps:35 99.74 762 62.24 0.0 Phospholipase D epsilon OS Arabidopsis thaliana GN PLDEPSILON PE 3 SV 1
blastp_uniprot_sprot sp|Q43007|PLDA1_ORYSJ 7 753 + 747 Gaps:73 99.51 812 43.19 0.0 Phospholipase D alpha 1 OS Oryza sativa subsp. japonica GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q43270|PLDA1_MAIZE 7 753 + 747 Gaps:77 99.51 812 43.32 0.0 Phospholipase D alpha 1 OS Zea mays GN PLD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q70EW5|PLDA1_CYNCA 7 753 + 747 Gaps:75 99.50 808 42.16 0.0 Phospholipase D alpha 1 OS Cynara cardunculus GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 7 753 + 747 Gaps:73 99.50 808 41.54 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q38882|PLDA1_ARATH 7 753 + 747 Gaps:73 99.51 810 41.44 0.0 Phospholipase D alpha 1 OS Arabidopsis thaliana GN PLDALPHA1 PE 1 SV 2
blastp_uniprot_sprot sp|P55939|PLDA2_BRAOC 7 753 + 747 Gaps:73 99.51 812 40.97 0.0 Phospholipase D alpha 2 OS Brassica oleracea var. capitata GN PLD2 PE 1 SV 2
blastp_uniprot_sprot sp|O82549|PLDA1_BRAOC 7 753 + 747 Gaps:75 99.51 810 41.19 0.0 Phospholipase D alpha 1 OS Brassica oleracea var. capitata GN PLD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9SSQ9|PLDA2_ARATH 39 753 + 715 Gaps:59 93.83 810 42.24 0.0 Phospholipase D alpha 2 OS Arabidopsis thaliana GN PLDALPHA2 PE 2 SV 1
blastp_uniprot_sprot sp|Q41142|PLDA1_RICCO 39 753 + 715 Gaps:60 93.94 808 42.69 0.0 Phospholipase D alpha 1 OS Ricinus communis GN PLD1 PE 1 SV 1
rpsblast_cdd gnl|CDD|165993 1 753 + 753 Gaps:9 100.00 758 74.41 0.0 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|165912 39 753 + 715 Gaps:60 93.94 808 43.35 1e-179 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|178585 39 753 + 715 Gaps:120 90.90 868 38.02 1e-137 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|197240 447 643 + 197 Gaps:9 99.04 208 59.22 2e-89 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|197295 447 640 + 194 Gaps:12 97.63 211 52.91 4e-67 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|197296 447 640 + 194 Gaps:9 96.21 211 55.17 3e-66 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 186 346 + 161 Gaps:11 95.45 176 55.36 3e-66 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|197293 186 347 + 162 Gaps:13 96.07 178 50.29 1e-47 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|197294 186 349 + 164 Gaps:13 96.11 180 41.62 3e-42 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 451 636 + 186 Gaps:37 94.54 183 37.57 6e-40 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.

22 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 7 125 119 SSF49562 none none IPR000008
SMART 297 334 38 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 598 625 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
Pfam 601 624 24 PF00614 none Phospholipase D Active site motif IPR001736
SUPERFAMILY 594 670 77 SSF56024 none none none
SUPERFAMILY 427 548 122 SSF56024 none none none
Gene3D 156 339 184 G3DSA:3.30.870.10 none none none
Gene3D 453 545 93 G3DSA:3.30.870.10 none none none
Gene3D 591 636 46 G3DSA:3.30.870.10 none none none
Gene3D 372 402 31 G3DSA:3.30.870.10 none none none
PANTHER 596 752 157 PTHR18896:SF56 none none none
PANTHER 188 578 391 PTHR18896:SF56 none none none
PANTHER 1 171 171 PTHR18896:SF56 none none none
ProSiteProfiles 598 625 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Gene3D 39 131 93 G3DSA:2.60.40.150 none none IPR000008
PIRSF 2 753 752 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
PANTHER 596 752 157 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
PANTHER 1 171 171 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 188 578 391 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
Pfam 670 744 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
SUPERFAMILY 144 341 198 SSF56024 none none none
SUPERFAMILY 371 422 52 SSF56024 none none none

0 Localization

2 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_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC_3P Qrob_Chr05 5 s_2GDU0O_517 s_1BT8O3_239 25,81 0 55,45 lod 2,2101 5,5

0 Targeting