Protein : Qrob_P0430420.2 Q. robur
Protein Identifier  ? Qrob_P0430420.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Gene Prediction Quality  validated Protein length 

Sequence

Length: 375  
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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|gmx:100819253 6 357 + 352 Gaps:1 86.67 405 85.19 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|cam:101506445 32 358 + 327 Gaps:2 80.64 408 87.84 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pop:POPTR_0004s14730g 8 357 + 350 Gaps:1 85.96 406 81.95 0.0 hypothetical protein
blastp_kegg lcl|mtr:MTR_4g085750 12 357 + 346 Gaps:28 86.51 430 78.76 0.0 PI-PLC X domain-containing protein
blastp_kegg lcl|tcc:TCM_007081 16 361 + 346 none 86.72 399 81.50 0.0 PLC-like phosphodiesterases superfamily protein
blastp_kegg lcl|pvu:PHAVU_003G048300g 28 357 + 330 none 82.09 402 86.36 0.0 hypothetical protein
blastp_kegg lcl|pper:PRUPE_ppa006614mg 12 361 + 350 Gaps:1 86.60 403 81.09 0.0 hypothetical protein
blastp_kegg lcl|pmum:103335240 12 361 + 350 Gaps:1 86.17 405 79.66 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|mdm:103436478 9 357 + 349 Gaps:1 86.35 403 78.16 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|vvi:100252205 17 358 + 342 Gaps:9 87.75 400 78.92 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_uniprot_sprot sp|Q93XX5|Y5713_ARATH 36 357 + 322 none 75.59 426 57.76 8e-137 PI-PLC X domain-containing protein At5g67130 OS Arabidopsis thaliana GN At5g67130 PE 1 SV 1
rpsblast_cdd gnl|CDD|176530 69 343 + 275 Gaps:20 99.63 270 43.49 3e-85 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 75 331 + 257 Gaps:19 95.20 271 24.03 7e-40 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 75 232 + 158 Gaps:13 61.80 267 29.09 3e-15 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 87 220 + 134 Gaps:24 43.73 279 36.07 4e-12 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 72 230 + 159 Gaps:55 59.03 288 22.35 2e-09 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.

9 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 11 372 362 PTHR13593 none none none
ProSiteProfiles 78 186 109 PS50007 none Phosphatidylinositol-specific phospholipase X-box domain profile. IPR000909
ProSiteProfiles 1 27 27 PS51257 none Prokaryotic membrane lipoprotein lipid attachment site profile. none
Phobius 12 31 20 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
PANTHER 11 372 362 PTHR13593:SF27 none none none
Phobius 1 11 11 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
SUPERFAMILY 76 347 272 SSF51695 none none IPR017946
Phobius 32 374 343 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Gene3D 77 246 170 G3DSA:3.20.20.190 none none IPR017946

0 Localization

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