Protein : Qrob_P0154300.2 Q. robur
Protein Identifier  ? Qrob_P0154300.2 Organism . Name  Quercus robur
Score  96.0 Score Type  egn
Protein Description  (M=2) PTHR18896//PTHR18896:SF58 - PHOSPHOLIPASE D // SUBFAMILY NOT NAMED Code Enzyme  EC:3.1.4.4
Gene Prediction Quality  validated Protein length 

Sequence

Length: 1120  
Kegg Orthology  K01115
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0 Synonyms

6 GO Terms

Identifier Name Description
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:0004630 phospholipase D activity Catalysis of the reaction: a phosphatidylcholine + H2O = choline + a phosphatidate.
GO:0006654 phosphatidic acid biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.
GO:0030334 regulation of cell migration Any process that modulates the frequency, rate or extent of cell migration.
GO:0048017 inositol lipid-mediated signaling A series of molecular signals in which a cell uses an inositol-containing lipid to convert a signal into a response. Inositol lipids include the phosphoinositides (phosphatidylinositol and its phosphorylated derivatives), ceramides containing inositol, and inositol glycolipids.
GO:0050764 regulation of phagocytosis Any process that modulates the frequency, rate or extent of phagocytosis, the process in which phagocytes engulf external particulate material.

31 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa000572mg 1 1118 + 1118 Gaps:57 99.91 1092 76.81 0.0 hypothetical protein
blastp_kegg lcl|pmum:103343749 1 1118 + 1118 Gaps:69 99.91 1080 77.02 0.0 phospholipase D p1
blastp_kegg lcl|mdm:103433898 1 1119 + 1119 Gaps:70 100.00 1085 75.94 0.0 phospholipase D p1
blastp_kegg lcl|pxb:103930592 1 1119 + 1119 Gaps:83 100.00 1086 75.23 0.0 phospholipase D p1
blastp_kegg lcl|mdm:103451296 1 1118 + 1118 Gaps:74 99.91 1077 75.09 0.0 phospholipase D p1-like
blastp_kegg lcl|fve:101297849 1 1118 + 1118 Gaps:80 99.91 1095 73.40 0.0 phospholipase D p1-like
blastp_kegg lcl|cic:CICLE_v10000089mg 17 1119 + 1103 Gaps:78 97.05 1120 71.39 0.0 hypothetical protein
blastp_kegg lcl|cit:102606741 17 1119 + 1103 Gaps:86 97.07 1128 70.96 0.0 phospholipase D p1-like
blastp_kegg lcl|pop:POPTR_0013s01380g 21 1119 + 1099 Gaps:48 98.92 1111 70.88 0.0 POPTRDRAFT_1096093 hypothetical protein
blastp_kegg lcl|pvu:PHAVU_007G198600g 1 1119 + 1119 Gaps:80 100.00 1071 72.64 0.0 hypothetical protein
blastp_uniprot_sprot sp|Q9M9W8|PLDP2_ARATH 1 1119 + 1119 Gaps:119 100.00 1046 69.12 0.0 Phospholipase D p2 OS Arabidopsis thaliana GN PLDP2 PE 2 SV 2
blastp_uniprot_sprot sp|Q9LRZ5|PLDP1_ARATH 33 1119 + 1087 Gaps:71 95.99 1096 69.11 0.0 Phospholipase D p1 OS Arabidopsis thaliana GN PLDP1 PE 2 SV 1
blastp_uniprot_sprot sp|P70496|PLD1_RAT 195 1100 + 906 Gaps:73 66.01 1074 43.72 2e-79 Phospholipase D1 OS Rattus norvegicus GN Pld1 PE 1 SV 3
blastp_uniprot_sprot sp|Q13393|PLD1_HUMAN 195 1100 + 906 Gaps:77 66.01 1074 43.02 8e-79 Phospholipase D1 OS Homo sapiens GN PLD1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9Z280|PLD1_MOUSE 195 1100 + 906 Gaps:73 66.01 1074 43.72 2e-78 Phospholipase D1 OS Mus musculus GN Pld1 PE 2 SV 1
blastp_uniprot_sprot sp|O08684|PLD1_CRIGR 195 1100 + 906 Gaps:79 68.44 1036 43.44 5e-78 Phospholipase D1 OS Cricetulus griseus GN PLD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q0V8L6|PLD2_BOVIN 165 1099 + 935 Gaps:117 79.10 933 42.14 1e-72 Phospholipase D2 OS Bos taurus GN PLD2 PE 2 SV 1
blastp_uniprot_sprot sp|P70498|PLD2_RAT 165 1100 + 936 Gaps:120 83.07 933 41.16 4e-72 Phospholipase D2 OS Rattus norvegicus GN Pld2 PE 1 SV 2
blastp_uniprot_sprot sp|P97813|PLD2_MOUSE 195 1105 + 911 Gaps:116 79.53 933 41.24 1e-71 Phospholipase D2 OS Mus musculus GN Pld2 PE 1 SV 2
blastp_uniprot_sprot sp|O14939|PLD2_HUMAN 165 1105 + 941 Gaps:116 80.17 933 41.04 3e-70 Phospholipase D2 OS Homo sapiens GN PLD2 PE 1 SV 2
rpsblast_cdd gnl|CDD|178457 28 1119 + 1092 Gaps:70 99.81 1068 75.33 0.0 PLN02866 PLN02866 phospholipase D.
rpsblast_cdd gnl|CDD|197239 774 958 + 185 Gaps:2 100.00 183 60.11 8e-85 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.
rpsblast_cdd gnl|CDD|197236 400 545 + 146 none 100.00 146 56.85 1e-67 cd09138 PLDc_vPLD1_2_yPLD_like_1 Catalytic domain repeat 1 of vertebrate phospholipases PLD1 and PLD2 yeast PLDs and similar proteins. Catalytic domain repeat 1 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.
rpsblast_cdd gnl|CDD|197303 772 958 + 187 Gaps:5 100.00 182 52.20 2e-55 cd09845 PLDc_vPLD2_2 Catalytic domain repeat 2 of vertebrate phospholipase D2. Catalytic domain repeat 2 of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily the monomer of vertebrate 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. 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.
rpsblast_cdd gnl|CDD|197302 774 958 + 185 Gaps:3 100.00 182 51.65 3e-54 cd09844 PLDc_vPLD1_2 Catalytic domain repeat 2 of vertebrate phospholipase D1. Catalytic domain repeat 2 of vertebrate phospholipase D1 (PLD1). PLDs 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. Vertebrate PLD1 is a membrane associated phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily the monomer of vertebrate 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. 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.
rpsblast_cdd gnl|CDD|197300 400 544 + 145 none 96.03 151 48.28 1e-45 cd09842 PLDc_vPLD1_1 Catalytic domain repeat 1 of vertebrate phospholipase D1. Catalytic domain repeat 1 of vertebrate phospholipase D1 (PLD1). PLDs 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. Vertebrate PLD1 is a membrane associated phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily the monomer of vertebrate 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. 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.
rpsblast_cdd gnl|CDD|197301 400 544 + 145 Gaps:3 99.31 145 48.61 8e-43 cd09843 PLDc_vPLD2_1 Catalytic domain repeat 1 of vertebrate phospholipase D2. Catalytic domain repeat 1 of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily the monomer of vertebrate 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. 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.
rpsblast_cdd gnl|CDD|197204 779 956 + 178 Gaps:37 96.58 146 34.04 2e-27 cd09105 PLDc_vPLD1_2_like_2 Catalytic domain repeat 2 of vertebrate phospholipases PLD1 and PLD2 and similar proteins. Catalytic domain repeat 2 of phospholipase D (PLD EC 3.1.4.4) found in yeast plants and vertebrates and their bacterial homologs. PLDs are involved in signal transduction vesicle formation protein transport and mitosis by participating in phospholipid metabolism. 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. Both prokaryotic and eukaryotic PLDs have two HKD motifs (H-x-K-x(4)-D where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. PLDs are active as bi-lobed monomers. Each monomer contains two domains each of which carries one copy of the HKD motif. Two HKD motifs from two domains form a single active site. 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.
rpsblast_cdd gnl|CDD|197240 779 950 + 172 Gaps:30 92.31 208 34.38 2e-27 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|132805 36 221 + 186 Gaps:49 99.29 140 32.37 1e-26 cd06895 PX_PLD The phosphoinositide binding Phox Homology domain of Phospholipase D. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling vesicular trafficking protein sorting and lipid modification among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. Members of this subfamily contain PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. PLD activity has been detected in viruses bacteria yeast plants and mammals but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling cytoskeletal reorganization vesicular transport stress responses and the control of differentiation proliferation and survival. Vertebrates contain two PLD isozymes PLD1 and PLD2. PLD1 is located mainly in intracellular membranes while PLD2 is associated with plasma membranes. The PX domain is involved in targeting of proteins to PI-enriched membranes and may also be involved in protein-protein interaction.

26 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 228 301 74 SSF50729 none none none
SUPERFAMILY 335 370 36 SSF50729 none none none
SUPERFAMILY 366 538 173 SSF56024 none none none
SUPERFAMILY 581 627 47 SSF56024 none none none
ProSiteProfiles 231 372 142 PS50003 none PH domain profile. IPR001849
Pfam 509 534 26 PF00614 none Phospholipase D Active site motif IPR001736
PIRSF 6 1119 1114 PIRSF009376 "KEGG:00564+3.1.4.4","KEGG:00565+3.1.4.4","MetaCyc:PWY-3561","MetaCyc:PWY-7039" none IPR016555
SMART 232 374 143 SM00233 none Pleckstrin homology domain. IPR001849
SUPERFAMILY 755 960 206 SSF56024 none none none
Pfam 788 959 172 PF13091 none PLD-like domain IPR025202
PANTHER 94 322 229 PTHR18896:SF58 none none none
PANTHER 38 71 34 PTHR18896:SF58 none none none
PANTHER 342 645 304 PTHR18896:SF58 none none none
PANTHER 753 1119 367 PTHR18896:SF58 none none none
ProSiteProfiles 507 534 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
Gene3D 231 370 140 G3DSA:2.30.29.30 none none IPR011993
PANTHER 38 71 34 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 94 322 229 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 342 645 304 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
PANTHER 753 1119 367 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 778 961 184 G3DSA:3.30.870.10 none none none
Gene3D 582 628 47 G3DSA:3.30.870.10 none none none
Gene3D 395 539 145 G3DSA:3.30.870.10 none none none
ProSiteProfiles 914 941 28 PS50035 none Phospholipase D phosphodiesterase active site profile. IPR001736
SMART 914 941 28 SM00155 none Phospholipase D. Active site motifs. IPR001736
SMART 507 534 28 SM00155 none Phospholipase D. Active site motifs. IPR001736

0 Localization

0 Qtllist

0 Targeting