Protein : Qrob_P0238260.2 Q. robur
Protein Identifier  ? Qrob_P0238260.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=1) KOG1028//KOG1030//KOG1329//KOG2059 - Ca2+-dependent phospholipid-binding protein Synaptotagmin required for synaptic vesicle and secretory granule exocytosis [Signal transduction mechanisms Intracellular trafficking secretion and vesicular transport]. // Predicted Ca2+-dependent phospholipid-binding protein [General function prediction only]. // Phospholipase D1 [Lipid transport and metabolism]. // Ras GTPase-activating protein [Signal transduction mechanisms]. Code Enzyme  EC:3.1.4.4
Gene Prediction Quality  validated Protein length 

Sequence

Length: 882  
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.

34 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103340375 20 881 + 862 Gaps:20 98.71 853 77.20 0.0 phospholipase D delta
blastp_kegg lcl|pper:PRUPE_ppa001300mg 20 881 + 862 Gaps:24 98.72 859 76.53 0.0 hypothetical protein
blastp_kegg lcl|mdm:103401038 9 881 + 873 Gaps:18 100.00 855 74.74 0.0 phospholipase D delta
blastp_kegg lcl|vvi:100252422 9 881 + 873 Gaps:35 100.00 872 72.59 0.0 phospholipase D delta-like
blastp_kegg lcl|pxb:103953430 9 881 + 873 Gaps:18 100.00 855 74.85 0.0 phospholipase D delta-like
blastp_kegg lcl|fve:101310737 9 881 + 873 Gaps:17 100.00 856 73.25 0.0 phospholipase D delta-like
blastp_kegg lcl|gmx:100814486 20 881 + 862 Gaps:24 98.61 866 72.60 0.0 phospholipase D delta-like
blastp_kegg lcl|gmx:100801787 20 881 + 862 Gaps:20 98.38 864 72.59 0.0 phospholipase D delta-like
blastp_kegg lcl|pvu:PHAVU_002G104200g 20 881 + 862 Gaps:20 98.49 859 71.87 0.0 hypothetical protein
blastp_kegg lcl|cit:102618083 11 881 + 871 Gaps:18 99.42 862 71.88 0.0 phospholipase D delta-like
blastp_uniprot_sprot sp|Q9C5Y0|PLDD1_ARATH 18 881 + 864 Gaps:39 98.96 868 69.50 0.0 Phospholipase D delta OS Arabidopsis thaliana GN PLDDELTA PE 1 SV 2
blastp_uniprot_sprot sp|P93733|PLDB1_ARATH 16 880 + 865 Gaps:71 75.35 1083 54.17 0.0 Phospholipase D beta 1 OS Arabidopsis thaliana GN PLDBETA1 PE 2 SV 4
blastp_uniprot_sprot sp|Q9T053|PLDG1_ARATH 20 880 + 861 Gaps:71 95.34 858 53.18 0.0 Phospholipase D gamma 1 OS Arabidopsis thaliana GN PLDGAMMA1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9T052|PLDG3_ARATH 20 873 + 854 Gaps:70 94.23 866 52.82 0.0 Phospholipase D gamma 3 OS Arabidopsis thaliana GN PLDGAMMA3 PE 2 SV 1
blastp_uniprot_sprot sp|O23078|PLDB2_ARATH 16 880 + 865 Gaps:65 88.03 927 53.31 0.0 Phospholipase D beta 2 OS Arabidopsis thaliana GN PLDBETA2 PE 2 SV 3
blastp_uniprot_sprot sp|Q9T051|PLDG2_ARATH 20 880 + 861 Gaps:71 96.03 856 52.80 0.0 Phospholipase D gamma 2 OS Arabidopsis thaliana GN PLDGAMMA2 PE 1 SV 3
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 86 881 + 796 Gaps:73 93.94 808 49.67 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|Q41142|PLDA1_RICCO 86 881 + 796 Gaps:73 93.94 808 49.01 0.0 Phospholipase D alpha 1 OS Ricinus communis GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|P86387|PLDA1_CARPA 86 881 + 796 Gaps:77 93.94 808 49.14 0.0 Phospholipase D alpha 1 OS Carica papaya GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|O04865|PLDA1_VIGUN 86 881 + 796 Gaps:74 93.94 809 49.74 0.0 Phospholipase D alpha 1 OS Vigna unguiculata GN PLD1 PE 1 SV 1
rpsblast_cdd gnl|CDD|178585 20 881 + 862 Gaps:39 98.73 868 69.66 0.0 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|165912 82 881 + 800 Gaps:73 94.43 808 49.41 0.0 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|165993 86 881 + 796 Gaps:112 94.99 758 44.44 1e-166 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|197296 572 776 + 205 Gaps:6 100.00 211 65.88 7e-93 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|197240 572 773 + 202 Gaps:8 100.00 208 58.17 1e-87 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|197294 238 418 + 181 Gaps:1 100.00 180 67.78 5e-83 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|197295 572 771 + 200 Gaps:11 99.05 211 57.89 3e-70 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|197237 238 416 + 179 Gaps:5 100.00 176 52.27 3e-63 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 20 183 + 164 Gaps:10 97.47 158 49.35 3e-56 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|197293 238 416 + 179 Gaps:7 100.00 178 51.69 9e-55 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.

32 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 578 680 103 SSF56024 none none none
SUPERFAMILY 722 806 85 SSF56024 none none none
Gene3D 82 183 102 G3DSA:2.60.40.150 none none IPR000008
Gene3D 15 41 27 G3DSA:2.60.40.150 none none IPR000008
PANTHER 246 516 271 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 82 224 143 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 577 880 304 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
PIRSF 9 881 873 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
Pfam 727 753 27 PF00614 none Phospholipase D Active site motif IPR001736
Pfam 368 402 35 PF00614 none Phospholipase D Active site motif IPR001736
PANTHER 82 224 143 PTHR18896:SF11 none none none
PANTHER 533 561 29 PTHR18896:SF11 none none none
PANTHER 533 561 29 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 800 872 73 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 435 471 37 SSF56024 none none none
SUPERFAMILY 204 409 206 SSF56024 none none none
SMART 726 753 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 367 402 36 SM00155 none Phospholipase D. Active site motifs. IPR001736
PANTHER 246 516 271 PTHR18896:SF11 none none none
SMART 23 159 137 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
ProSiteProfiles 367 402 36 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Gene3D 582 677 96 G3DSA:3.30.870.10 none none none
Gene3D 719 765 47 G3DSA:3.30.870.10 none none none
Gene3D 209 468 260 G3DSA:3.30.870.10 none none none
SUPERFAMILY 82 185 104 SSF49562 none none IPR000008
SUPERFAMILY 20 52 33 SSF49562 none none IPR000008
ProSiteProfiles 726 753 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Pfam 24 143 120 PF00168 none C2 domain IPR000008
ProSiteProfiles 24 144 121 PS50004 none C2 domain profile. IPR000008
PANTHER 12 62 51 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

0 Localization

0 Qtllist

0 Targeting