Protein : Qrob_P0274880.2 Q. robur
Protein Identifier  ? Qrob_P0274880.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=1) 4.6.1.13 - Phosphatidylinositol diacylglycerol-lyase. Code Enzyme  EC:3.1.4.11, EC:4.6.1.13
Gene Prediction Quality  validated Protein length 

Sequence

Length: 321  
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0006629 lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
GO:0008081 phosphoric diester hydrolase activity Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.

34 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|rcu:RCOM_0739740 1 318 + 318 none 100.00 318 82.39 0.0 phospholipase C putative
blastp_kegg lcl|cic:CICLE_v10028852mg 1 318 + 318 none 100.00 318 80.50 0.0 hypothetical protein
blastp_kegg lcl|pmum:103334799 1 318 + 318 none 87.36 364 80.50 0.0 uncharacterized LOC103334799
blastp_kegg lcl|tcc:TCM_006664 1 317 + 317 none 99.69 318 81.70 0.0 PLC-like phosphodiesterases superfamily protein
blastp_kegg lcl|cit:102612699 1 318 + 318 none 100.00 318 80.19 0.0 uncharacterized LOC102612699
blastp_kegg lcl|pper:PRUPE_ppa007525mg 1 318 + 318 none 87.12 365 80.50 0.0 hypothetical protein
blastp_kegg lcl|pop:POPTR_0004s17770g 1 318 + 318 none 100.00 318 81.45 0.0 POPTRDRAFT_713245 1-phosphatidylinositol phosphodiesterase-related family protein
blastp_kegg lcl|mdm:103438283 1 318 + 318 none 100.00 318 79.56 0.0 uncharacterized LOC103438283
blastp_kegg lcl|pxb:103966250 1 318 + 318 none 100.00 318 79.25 0.0 PI-PLC X-box domain-containing protein DDB_G0293730-like
blastp_kegg lcl|pxb:103966241 1 318 + 318 none 100.00 318 79.25 0.0 PI-PLC X-box domain-containing protein DDB_G0293730-like
blastp_pdb 2plc_A 44 156 + 113 Gaps:3 41.61 274 34.21 2e-14 mol:protein length:274 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 1aod_A 44 156 + 113 Gaps:3 39.45 289 34.21 2e-14 mol:protein length:289 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 7ptd_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 2ptd_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 4ptd_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 3ptd_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 1ptg_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 1ptd_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 1gym_A 46 152 + 107 Gaps:11 38.26 298 34.21 1e-08 mol:protein length:298 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
blastp_pdb 1t6m_B 46 148 + 103 Gaps:7 35.45 299 33.96 2e-08 mol:protein length:299 1-phosphatidylinositol phosphodiesterase
blastp_uniprot_sprot sp|P34024|PLC_LISMO 44 156 + 113 Gaps:3 35.96 317 34.21 1e-13 1-phosphatidylinositol phosphodiesterase OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) GN plcA PE 1 SV 1
blastp_uniprot_sprot sp|P14262|PLC_BACCE 46 152 + 107 Gaps:11 34.65 329 34.21 7e-08 1-phosphatidylinositol phosphodiesterase OS Bacillus cereus PE 1 SV 1
blastp_uniprot_sprot sp|P08954|PLC_BACTU 46 148 + 103 Gaps:7 32.22 329 33.96 1e-07 1-phosphatidylinositol phosphodiesterase OS Bacillus thuringiensis PE 1 SV 1
rpsblast_cdd gnl|CDD|176556 33 313 + 281 Gaps:4 100.00 285 71.58 1e-133 cd08619 PI-PLCXDc_plant Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing proteins found in plants. The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast plant PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
rpsblast_cdd gnl|CDD|176529 54 310 + 257 Gaps:38 98.26 288 25.09 1e-47 cd08587 PI-PLCXDc_like Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain X domain which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may be distinct from that of typical eukaryotic PI-PLCs.
rpsblast_cdd gnl|CDD|176500 55 309 + 255 Gaps:23 97.42 271 28.79 2e-36 cd08557 PI-PLCc_bacteria_like Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC EC 3.1.4.11) which have a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG) releasing dimyristyl glycerol (DMG) which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs but not mammalian PI-PLCs.
rpsblast_cdd gnl|CDD|176528 47 164 + 118 Gaps:11 42.65 279 31.09 2e-18 cd08586 PI-PLCc_BcPLC_like Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins. This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) and its sequence homologs found in bacteria and eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Their catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines and consists of two steps a phosphotransfer and a phosphodiesterase reaction. This family also includes some uncharacterized eukaryotic homologs which contains a single TIM-barrel type catalytic domain X domain. They are similar to bacterial PI-PLCs and distinct from typical eukaryotic PI-PLCs which have a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC which has a moderate thermal stability and is active as a monomer.
rpsblast_cdd gnl|CDD|176555 51 307 + 257 Gaps:70 98.97 290 24.04 8e-17 cd08616 PI-PLCXD1c Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing 1. This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1) 2 (PI-PLCXD2) and 3 (PI-PLCXD3) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast members in this group contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
rpsblast_cdd gnl|CDD|176559 55 189 + 135 Gaps:28 54.71 276 29.80 1e-15 cd08622 PI-PLCXDc_CG14945_like Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to phosphatidylinositol-specific phospholipase C X domain containing. This subfamily corresponds to the catalytic domain present in uncharacterized metazoan Drosophila melanogaster CG14945-like proteins which are similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.
rpsblast_cdd gnl|CDD|176558 54 167 + 114 Gaps:23 43.00 300 26.36 2e-14 cd08621 PI-PLCXDc_like_2 Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi which are similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs.

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 42 308 267 SSF51695 none none IPR017946
PANTHER 26 316 291 PTHR13593:SF37 none none none
SMART 51 192 142 SM00148 none Phospholipase C, catalytic domain (part) IPR000909
PANTHER 26 316 291 PTHR13593 none none none
Gene3D 42 309 268 G3DSA:3.20.20.190 none none IPR017946
Pfam 63 175 113 PF00388 none Phosphatidylinositol-specific phospholipase C, X domain IPR000909
ProSiteProfiles 57 185 129 PS50007 none Phosphatidylinositol-specific phospholipase X-box domain profile. IPR000909

0 Localization

4 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2015_nP_3P Qrob_Chr12 12 v_10140_295 v_838_303 16 14,69 18,01 lod 5.1 13.7
Bourran2_2002_QTL17_peak_Bud_burst_A4 Qrob_Chr12 12 s_1CTJ3J_556 s_1CTJ3J_556 0 0 25 lod 2,9 6
Bourran2_2014_nSeqBC_3P Qrob_Chr12 12 s_1EO8V5_710 s_1A2VMU_355 11,04 0 32,58 lod 1,7196 4,7

0 Targeting