Protein : Qrob_P0204290.2 Q. robur
Protein Identifier  ? Qrob_P0204290.2 Organism . Name  Quercus robur
Score  99.0 Score Type  egn
Protein Description  (M=2) PF00168//PF00614 - C2 domain // Phospholipase D Active site motif Code Enzyme  EC:3.1.4.4
Gene Prediction Quality  validated Protein length 

Sequence

Length: 701  
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.

32 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|mdm:103450340 6 694 + 689 Gaps:17 79.81 847 81.66 0.0 phospholipase D delta-like
blastp_kegg lcl|pmum:103321189 6 694 + 689 Gaps:17 79.91 846 81.66 0.0 phospholipase D delta-like
blastp_kegg lcl|cmo:103488380 8 691 + 684 Gaps:12 79.72 848 80.62 0.0 phospholipase D delta-like
blastp_kegg lcl|csv:101225692 8 691 + 684 Gaps:12 79.81 847 80.92 0.0 phospholipase D delta-like
blastp_kegg lcl|csv:101213442 8 691 + 684 Gaps:12 79.81 847 80.92 0.0 phospholipase D delta-like
blastp_kegg lcl|pxb:103927338 6 694 + 689 Gaps:24 79.98 854 80.23 0.0 phospholipase D delta-like
blastp_kegg lcl|cic:CICLE_v10000269mg 1 691 + 691 Gaps:17 80.43 843 80.97 0.0 hypothetical protein
blastp_kegg lcl|cit:102622948 1 691 + 691 Gaps:17 80.43 843 80.97 0.0 phospholipase D delta-like
blastp_kegg lcl|tcc:TCM_034306 1 678 + 678 Gaps:15 78.93 845 81.41 0.0 Phospholipase D isoform 1
blastp_kegg lcl|gmx:100795859 9 692 + 684 Gaps:11 79.93 847 80.21 0.0 phospholipase D delta-like
blastp_uniprot_sprot sp|Q9C5Y0|PLDD1_ARATH 1 686 + 686 Gaps:26 80.88 868 66.38 0.0 Phospholipase D delta OS Arabidopsis thaliana GN PLDDELTA PE 1 SV 2
blastp_uniprot_sprot sp|P93733|PLDB1_ARATH 10 673 + 664 Gaps:39 58.45 1083 58.61 0.0 Phospholipase D beta 1 OS Arabidopsis thaliana GN PLDBETA1 PE 2 SV 4
blastp_uniprot_sprot sp|O23078|PLDB2_ARATH 10 673 + 664 Gaps:41 68.28 927 56.56 0.0 Phospholipase D beta 2 OS Arabidopsis thaliana GN PLDBETA2 PE 2 SV 3
blastp_uniprot_sprot sp|Q9T053|PLDG1_ARATH 10 673 + 664 Gaps:39 73.78 858 55.13 0.0 Phospholipase D gamma 1 OS Arabidopsis thaliana GN PLDGAMMA1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9T052|PLDG3_ARATH 10 679 + 670 Gaps:36 74.13 866 53.27 0.0 Phospholipase D gamma 3 OS Arabidopsis thaliana GN PLDGAMMA3 PE 2 SV 1
blastp_uniprot_sprot sp|Q9T051|PLDG2_ARATH 10 679 + 670 Gaps:36 75.00 856 53.58 0.0 Phospholipase D gamma 2 OS Arabidopsis thaliana GN PLDGAMMA2 PE 1 SV 3
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 73 686 + 614 Gaps:49 72.90 808 49.24 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q43270|PLDA1_MAIZE 9 673 + 665 Gaps:60 77.46 812 48.17 0.0 Phospholipase D alpha 1 OS Zea mays GN PLD1 PE 2 SV 1
blastp_uniprot_sprot sp|O04865|PLDA1_VIGUN 51 673 + 623 Gaps:50 74.04 809 49.08 0.0 Phospholipase D alpha 1 OS Vigna unguiculata GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q41142|PLDA1_RICCO 73 673 + 601 Gaps:48 71.41 808 49.39 6e-180 Phospholipase D alpha 1 OS Ricinus communis GN PLD1 PE 1 SV 1
rpsblast_cdd gnl|CDD|178585 1 686 + 686 Gaps:26 80.88 868 66.38 0.0 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|165912 69 698 + 630 Gaps:52 74.50 808 48.17 1e-167 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|165993 73 693 + 621 Gaps:86 74.01 758 47.24 1e-135 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|197294 222 409 + 188 Gaps:8 100.00 180 73.33 2e-89 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|197296 542 693 + 152 Gaps:4 73.93 211 71.15 1e-67 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 222 407 + 186 Gaps:12 100.00 176 53.41 2e-64 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|175982 9 170 + 162 Gaps:4 100.00 158 55.06 2e-61 cd04015 C2_plant_PLD C2 domain present in plant phospholipase D (PLD). PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination seedling growth phosphatidylinositol metabolism and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions.
rpsblast_cdd gnl|CDD|197240 542 697 + 156 Gaps:9 73.56 208 58.82 9e-61 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 222 407 + 186 Gaps:14 100.00 178 54.49 3e-57 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|197295 542 690 + 149 Gaps:5 72.04 211 55.92 4e-48 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.

21 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 527 633 107 SSF56024 none none none
Gene3D 14 170 157 G3DSA:2.60.40.150 none none IPR000008
SMART 16 146 131 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
PIRSF 3 699 697 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
SUPERFAMILY 426 467 42 SSF56024 none none none
SUPERFAMILY 191 400 210 SSF56024 none none none
PANTHER 230 339 110 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 357 531 175 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 13 172 160 SSF49562 none none IPR000008
PANTHER 3 209 207 PTHR18896:SF11 none none none
Pfam 358 393 36 PF00614 none Phospholipase D Active site motif IPR001736
PANTHER 230 339 110 PTHR18896:SF11 none none none
PANTHER 357 531 175 PTHR18896:SF11 none none none
PANTHER 547 674 128 PTHR18896:SF11 none none none
PANTHER 3 209 207 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 547 674 128 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 549 616 68 G3DSA:3.30.870.10 none none none
Gene3D 232 463 232 G3DSA:3.30.870.10 none none none
ProSiteProfiles 17 131 115 PS50004 none C2 domain profile. IPR000008
ProSiteProfiles 358 393 36 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Pfam 17 130 114 PF00168 none C2 domain IPR000008

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
Bourran1_2003_QTL2_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 87 lod 3,3 8,7
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_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_nPriLBD_A4 Qrob_Chr02 2 s_1CP5DI_1183 s_1A63ZX_1277 24,87 24,63 26,18 lod 3.8 7
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
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
Champenoux_2015_nSecLBD_A4 Qrob_Chr02 2 s_1AN4ZM_1665 v_8587_238 18,52 18,89 18,27 lod 3.2 7.4

0 Targeting