Protein : Qrob_P0371440.2 Q. robur
Protein Identifier  ? Qrob_P0371440.2 Organism . Name  Quercus robur
Score  99.0 Score Type  egn
Gene Prediction Quality  validated Protein length 

Sequence

Length: 328  
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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.

15 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|gmx:100806782 1 325 + 325 none 89.29 364 78.46 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pper:PRUPE_ppa007503mg 7 325 + 319 none 87.40 365 78.37 0.0 hypothetical protein
blastp_kegg lcl|pmum:103329571 7 325 + 319 none 87.40 365 78.06 0.0 PI-PLC X domain-containing protein At5g67130
blastp_kegg lcl|rcu:RCOM_0917970 1 325 + 325 none 89.53 363 75.69 0.0 phospholipase C putative
blastp_kegg lcl|pvu:PHAVU_008G031000g 16 325 + 310 none 85.16 364 79.68 0.0 hypothetical protein
blastp_kegg lcl|pop:POPTR_0017s13330g 1 325 + 325 Gaps:2 90.58 361 77.68 0.0 hypothetical protein
blastp_kegg lcl|vvi:100246342 1 325 + 325 none 89.29 364 77.23 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pop:POPTR_0011s14800g 7 325 + 319 Gaps:1 87.67 365 78.12 0.0 POPTRDRAFT_772086 hypothetical protein
blastp_kegg lcl|cit:102612382 7 325 + 319 none 87.64 364 75.86 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|cic:CICLE_v10012018mg 8 325 + 318 none 86.89 366 76.10 0.0 hypothetical protein
blastp_uniprot_sprot sp|Q93XX5|Y5713_ARATH 21 325 + 305 Gaps:2 71.60 426 58.03 2e-128 PI-PLC X domain-containing protein At5g67130 OS Arabidopsis thaliana GN At5g67130 PE 1 SV 1
rpsblast_cdd gnl|CDD|176530 70 324 + 255 Gaps:17 93.33 270 40.48 3e-79 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 69 323 + 255 Gaps:19 94.46 271 24.22 2e-35 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 69 176 + 108 Gaps:14 41.95 267 40.18 2e-13 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 83 174 + 92 Gaps:19 28.32 279 35.44 1e-07 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.

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 17 21 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
SUPERFAMILY 66 323 258 SSF51695 none none IPR017946
PANTHER 3 324 322 PTHR13593:SF27 none none none
ProSiteProfiles 74 182 109 PS50007 none Phosphatidylinositol-specific phospholipase X-box domain profile. IPR000909
PANTHER 3 324 322 PTHR13593 none none none
Phobius 1 21 21 SIGNAL_PEPTIDE none Signal peptide region none
Phobius 5 16 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
Phobius 1 4 4 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Phobius 22 327 306 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Gene3D 69 242 174 G3DSA:3.20.20.190 none none IPR017946

3 Localization

Analysis Start End Length
SignalP_GRAM_NEGATIVE 1 21 20
SignalP_GRAM_POSITIVE 1 21 20
SignalP_EUK 1 21 20

9 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL1_peak_Bud_burst_A4 Qrob_Chr01 1 s_1AMVCC_444 s_1BE1VC_321 4 0 31 lod 3,2 7,4
Bourran2_2003_QTL8_peak_Bud_burst_A4 Qrob_Chr01 1 s_1AH7I_610 s_1BE1VC_321 4,6 0 28 lod 3,5 7,4
Bourran2_2007_QTL6_peak_Bud_burst_3P Qrob_Chr01 1 s_1BE1VC_321 s_1A5JRZ_890 5 0 25 lod 2,4 6
Bourran2_2014_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
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_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Bourran2_2002_QTL7_peak_Bud_burst_A4 Qrob_Chr01 1 s_1DFK66_275 s_1AMVCC_444 3,3 0 7,3 lod 9,4 14,8
Bourran2_2014_nSeqBC*_A4 Qrob_Chr01 1 s_1CFE4C_2114 s_1BDNCB_819 15,25 2 28,5 lod 2,9903 8,3

0 Targeting