Protein : Qrob_P0162840.2 Q. robur
Protein Identifier  ? Qrob_P0162840.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Gene Prediction Quality  validated Protein length 

Sequence

Length: 435  
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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|pmum:103339906 1 434 + 434 Gaps:14 98.60 430 81.13 0.0 PI-PLC X domain-containing protein At5g67130
blastp_kegg lcl|pxb:103956948 1 434 + 434 Gaps:14 100.00 424 80.42 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pxb:103935245 1 434 + 434 Gaps:14 100.00 424 80.19 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|mdm:103403236 1 434 + 434 Gaps:14 100.00 424 79.95 0.0 PI-PLC X domain-containing protein At5g67130
blastp_kegg lcl|gmx:100810371 7 434 + 428 Gaps:14 98.13 428 78.81 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|tcc:TCM_000654 1 434 + 434 Gaps:13 100.00 425 78.59 0.0 PLC-like phosphodiesterases superfamily protein isoform 1
blastp_kegg lcl|gmx:100798171 1 427 + 427 Gaps:11 96.52 431 78.12 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|gmx:100793490 5 427 + 423 Gaps:12 95.60 432 78.69 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|mdm:103401393 1 434 + 434 Gaps:14 100.00 424 78.54 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|gmx:100798420 1 434 + 434 Gaps:16 99.53 430 77.57 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_uniprot_sprot sp|Q93XX5|Y5713_ARATH 32 425 + 394 Gaps:17 91.31 426 74.04 0.0 PI-PLC X domain-containing protein At5g67130 OS Arabidopsis thaliana GN At5g67130 PE 1 SV 1
rpsblast_cdd gnl|CDD|176530 77 361 + 285 Gaps:31 99.26 270 38.43 4e-81 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 79 361 + 283 Gaps:33 99.63 271 22.96 9e-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 82 250 + 169 Gaps:18 61.80 267 28.48 4e-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 94 230 + 137 Gaps:42 43.37 279 29.75 7e-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.

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 80 256 177 G3DSA:3.20.20.190 none none IPR017946
Phobius 434 434 1 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
Phobius 1 15 15 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Phobius 414 433 20 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 33 413 381 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 28 32 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
SUPERFAMILY 79 365 287 SSF51695 none none IPR017946
Phobius 16 27 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
PANTHER 42 390 349 PTHR13593 none none none
PANTHER 42 390 349 PTHR13593:SF31 none none none
ProSiteProfiles 85 204 120 PS50007 none Phosphatidylinositol-specific phospholipase X-box domain profile. IPR000909
Phobius 1 32 32 SIGNAL_PEPTIDE none Signal peptide region none

3 Localization

Analysis Start End Length
SignalP_EUK 1 32 31
SignalP_GRAM_NEGATIVE 1 32 31
SignalP_GRAM_POSITIVE 1 32 31

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_2014_nEpis*_A4 Qrob_Chr07 7 v_12400_446 s_1BPEBU_1211 6,93 0 15,13 lod 4,7411 11
Bourran2_2014_nLBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,41 9,8 50,1 lod 1,9524 4,1
Bourran2_2014_nPriBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,51 3,36 51,86 lod 1,6747 3,9
Bourran2_2014_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5
Bourran2_2014_vEpiBC_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,55 14,41 50,01 lod 1,7882 4,8
Champenoux_2015_nEpis_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,53 25,47 27,72 lod 4.4 8.9

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 32   Secretory pathway 3 0.629 0.097 NON-PLANT 32