Protein : Qrob_P0173400.2 Q. robur
Protein Identifier  ? Qrob_P0173400.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=1) PF00168//PF00614//PF12357//PF13091 - C2 domain // Phospholipase D Active site motif // Phospholipase D C terminal // PLD-like domain Code Enzyme  EC:3.1.4.4
Gene Prediction Quality  validated Protein length 

Sequence

Length: 857  
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|rcu:RCOM_0320830 4 856 + 853 Gaps:12 99.88 856 78.36 0.0 phospholipase d beta putative (EC:3.1.4.4)
blastp_kegg lcl|pper:PRUPE_ppa001322mg 1 856 + 856 Gaps:14 100.00 854 77.87 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_006943 1 856 + 856 Gaps:16 100.00 848 78.77 0.0 Phospholipase D
blastp_kegg lcl|pmum:103318921 1 856 + 856 Gaps:18 100.00 850 77.76 0.0 phospholipase D delta-like
blastp_kegg lcl|vvi:100261019 1 856 + 856 Gaps:10 100.00 856 76.17 0.0 phospholipase D delta-like
blastp_kegg lcl|pxb:103946322 1 856 + 856 Gaps:23 100.00 845 77.28 0.0 phospholipase D delta-like
blastp_kegg lcl|mdm:103421386 1 856 + 856 Gaps:23 100.00 845 77.16 0.0 phospholipase D delta-like
blastp_kegg lcl|cit:102615105 1 856 + 856 Gaps:14 100.00 852 75.12 0.0 phospholipase D delta-like
blastp_kegg lcl|cic:CICLE_v10003162mg 1 856 + 856 Gaps:14 100.00 852 75.00 0.0 hypothetical protein
blastp_kegg lcl|cam:101494388 2 856 + 855 Gaps:30 99.53 857 73.86 0.0 phospholipase D delta-like
blastp_uniprot_sprot sp|Q9C5Y0|PLDD1_ARATH 19 856 + 838 Gaps:45 99.42 868 60.95 0.0 Phospholipase D delta OS Arabidopsis thaliana GN PLDDELTA PE 1 SV 2
blastp_uniprot_sprot sp|P93733|PLDB1_ARATH 23 855 + 833 Gaps:39 75.16 1083 57.00 0.0 Phospholipase D beta 1 OS Arabidopsis thaliana GN PLDBETA1 PE 2 SV 4
blastp_uniprot_sprot sp|Q9T053|PLDG1_ARATH 24 855 + 832 Gaps:31 95.45 858 55.19 0.0 Phospholipase D gamma 1 OS Arabidopsis thaliana GN PLDGAMMA1 PE 1 SV 1
blastp_uniprot_sprot sp|O23078|PLDB2_ARATH 18 855 + 838 Gaps:29 88.35 927 55.80 0.0 Phospholipase D beta 2 OS Arabidopsis thaliana GN PLDBETA2 PE 2 SV 3
blastp_uniprot_sprot sp|Q9T052|PLDG3_ARATH 24 846 + 823 Gaps:27 94.00 866 54.79 0.0 Phospholipase D gamma 3 OS Arabidopsis thaliana GN PLDGAMMA3 PE 2 SV 1
blastp_uniprot_sprot sp|Q9T051|PLDG2_ARATH 24 855 + 832 Gaps:27 96.14 856 53.71 0.0 Phospholipase D gamma 2 OS Arabidopsis thaliana GN PLDGAMMA2 PE 1 SV 3
blastp_uniprot_sprot sp|O04865|PLDA1_VIGUN 78 856 + 779 Gaps:49 93.94 809 48.82 0.0 Phospholipase D alpha 1 OS Vigna unguiculata GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|P93400|PLDA1_TOBAC 78 856 + 779 Gaps:46 93.94 808 48.22 0.0 Phospholipase D alpha 1 OS Nicotiana tabacum GN PLD1 PE 1 SV 2
blastp_uniprot_sprot sp|P86387|PLDA1_CARPA 24 856 + 833 Gaps:55 99.50 808 46.89 0.0 Phospholipase D alpha 1 OS Carica papaya GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q70EW5|PLDA1_CYNCA 23 856 + 834 Gaps:55 99.63 808 45.84 0.0 Phospholipase D alpha 1 OS Cynara cardunculus GN PLD1 PE 1 SV 2
rpsblast_cdd gnl|CDD|178585 19 856 + 838 Gaps:45 99.42 868 60.95 0.0 PLN03008 PLN03008 Phospholipase D delta.
rpsblast_cdd gnl|CDD|165912 74 856 + 783 Gaps:46 94.43 808 47.58 0.0 PLN02270 PLN02270 phospholipase D alpha.
rpsblast_cdd gnl|CDD|165993 78 856 + 779 Gaps:89 94.99 758 46.25 1e-176 PLN02352 PLN02352 phospholipase D epsilon.
rpsblast_cdd gnl|CDD|197296 542 752 + 211 none 100.00 211 71.09 1e-101 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 542 749 + 208 Gaps:2 100.00 208 60.58 5e-92 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 229 413 + 185 Gaps:5 100.00 180 68.89 2e-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 542 747 + 206 Gaps:5 99.05 211 58.37 5e-73 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 229 411 + 183 Gaps:9 100.00 176 48.86 2e-61 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 229 411 + 183 Gaps:11 100.00 178 52.25 8e-53 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|175982 22 175 + 154 Gaps:3 99.37 158 46.50 2e-49 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.

27 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 686 739 54 PF13091 none PLD-like domain IPR025202
Gene3D 26 176 151 G3DSA:2.60.40.150 none none IPR000008
ProSiteProfiles 702 729 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
SUPERFAMILY 25 177 153 SSF49562 none none IPR000008
SMART 28 151 124 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
Pfam 775 846 72 PF12357 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" Phospholipase D C terminal IPR024632
SMART 362 397 36 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 702 729 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
PANTHER 547 682 136 PTHR18896:SF15 none none none
PANTHER 15 216 202 PTHR18896:SF15 none none none
PANTHER 700 845 146 PTHR18896:SF15 none none none
PANTHER 237 531 295 PTHR18896:SF15 none none none
SUPERFAMILY 231 404 174 SSF56024 none none none
SUPERFAMILY 430 463 34 SSF56024 none none none
SUPERFAMILY 698 786 89 SSF56024 none none none
SUPERFAMILY 548 650 103 SSF56024 none none none
PANTHER 15 216 202 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 700 845 146 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 239 468 230 G3DSA:3.30.870.10 none none none
Gene3D 549 741 193 G3DSA:3.30.870.10 none none none
PIRSF 14 856 843 PIRSF036470 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR011402
PANTHER 547 682 136 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 237 531 295 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
ProSiteProfiles 14 136 123 PS50004 none C2 domain profile. IPR000008
Pfam 362 397 36 PF00614 none Phospholipase D Active site motif IPR001736
Pfam 29 135 107 PF00168 none C2 domain IPR000008
ProSiteProfiles 362 397 36 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736

0 Localization

0 Qtllist

0 Targeting