Protein : Qrob_P0430400.2 Q. robur
Protein Identifier  ? Qrob_P0430400.2 Organism . Name  Quercus robur
Score  90.1 Score Type  egn
Protein Description  (M=5) PF00388 - Phosphatidylinositol-specific phospholipase C, X domain Gene Prediction Quality  validated
Protein length 

Sequence

Length: 349  
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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.

16 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_007081 6 347 + 342 Gaps:6 86.22 399 74.13 0.0 PLC-like phosphodiesterases superfamily protein
blastp_kegg lcl|gmx:100819253 1 347 + 347 Gaps:6 86.17 405 71.06 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|cam:101506445 24 347 + 324 Gaps:8 80.39 408 75.30 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pop:POPTR_0004s14730g 1 347 + 347 Gaps:6 85.96 406 70.49 0.0 hypothetical protein
blastp_kegg lcl|pper:PRUPE_ppa006614mg 3 347 + 345 Gaps:6 86.10 403 70.03 1e-179 hypothetical protein
blastp_kegg lcl|mtr:MTR_4g085750 1 347 + 347 Gaps:34 87.67 430 66.05 7e-178 PI-PLC X domain-containing protein
blastp_kegg lcl|pmum:103335240 3 347 + 345 Gaps:6 85.68 405 69.45 9e-178 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|cit:102621424 1 347 + 347 Gaps:6 86.82 402 68.19 1e-177 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pvu:PHAVU_003G048300g 20 347 + 328 Gaps:6 82.09 402 71.52 7e-177 hypothetical protein
blastp_kegg lcl|cic:CICLE_v10028578mg 1 347 + 347 Gaps:6 86.82 402 67.62 6e-176 hypothetical protein
blastp_uniprot_sprot sp|Q93XX5|Y5713_ARATH 28 347 + 320 Gaps:6 75.59 426 53.11 2e-118 PI-PLC X domain-containing protein At5g67130 OS Arabidopsis thaliana GN At5g67130 PE 1 SV 1
rpsblast_cdd gnl|CDD|176530 60 333 + 274 Gaps:19 99.63 270 41.64 5e-82 cd08588 PI-PLCc_At5g67130_like Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. This subfamily corresponds to the catalytic domain present in Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. Members in this family show high sequence similarity to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) which participates in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG).
rpsblast_cdd gnl|CDD|176500 66 333 + 268 Gaps:21 98.52 271 26.97 3e-38 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|176532 66 226 + 161 Gaps:16 64.04 267 29.82 5e-17 cd08590 PI-PLCc_Rv2075c_like Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins. This subfamily corresponds to the catalytic domain present in uncharacterized Mycobacterium tuberculosis Rv2075c and its homologs. Members in this family are more closely related to the Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1(SaPLC1)-like proteins rather than the typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC EC 4.6.1.13) which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). In contrast SaPLC1-like proteins have two Ca2+-chelating amino acid substitutions which convert them to metal-dependent bacterial PI-PLC. Rv2075c and its homologs have the same amino acid substitutions as well which might suggest they have metal-dependent PI-PLC activity.
rpsblast_cdd gnl|CDD|176528 78 206 + 129 Gaps:21 43.01 279 30.83 2e-09 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|176529 63 315 + 253 Gaps:73 95.14 288 21.90 7e-08 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.

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 12 347 336 PTHR13593 none none none
Phobius 23 348 326 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Pfam 69 173 105 PF00388 none Phosphatidylinositol-specific phospholipase C, X domain IPR000909
ProSiteProfiles 69 172 104 PS50007 none Phosphatidylinositol-specific phospholipase X-box domain profile. IPR000909
Phobius 4 17 14 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
Gene3D 68 316 249 G3DSA:3.20.20.190 none none IPR017946
PANTHER 12 347 336 PTHR13593:SF27 none none none
Phobius 18 22 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Phobius 1 3 3 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Phobius 1 22 22 SIGNAL_PEPTIDE none Signal peptide region none
SUPERFAMILY 66 316 251 SSF51695 none none IPR017946
ProSiteProfiles 1 19 19 PS51257 none Prokaryotic membrane lipoprotein lipid attachment site profile. none

3 Localization

Analysis Start End Length
SignalP_EUK 1 22 21
SignalP_GRAM_POSITIVE 1 24 23
SignalP_GRAM_NEGATIVE 1 22 21

6 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_nEpis_3P Qrob_Chr12 12 s_1AOES6_1466 s_1B0DDG_1094 28,97 28,55 30,1 lod 3.6 8.4
Champenoux_2015_nEpis_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,53 25,47 27,72 lod 4.4 8.9
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2002_QTL16_peak_Bud_burst_A4 Qrob_Chr11 11 s_A9OIA_166 s_1C6WBF_114 21,23 2,83 42,83 lod 5,1 7,2
Bourran2_2015_nSeqBC_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,06 25,47 27,72 lod 3.6 7.1
Champenoux_2015_nSecLBD_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 25,78 25,47 27,72 lod 6.3 16.6

0 Targeting