Protein : Qrob_P0630430.2 Q. robur
Protein Identifier  ? Qrob_P0630430.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Gene Prediction Quality  validated Protein length 

Sequence

Length: 412  
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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|mus:103968595 1 356 + 356 Gaps:3 96.71 365 73.65 0.0 PI-PLC X domain-containing protein At5g67130
blastp_kegg lcl|mdm:103425899 9 356 + 348 Gaps:1 95.07 365 72.91 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|mdm:103404649 9 356 + 348 Gaps:1 95.07 365 72.91 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|cic:CICLE_v10012018mg 1 361 + 361 Gaps:6 98.09 366 69.92 0.0 hypothetical protein
blastp_kegg lcl|pper:PRUPE_ppa007503mg 9 356 + 348 Gaps:1 95.07 365 72.33 0.0 hypothetical protein
blastp_kegg lcl|gmx:100806782 4 356 + 353 Gaps:1 96.70 364 69.89 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|cit:102613576 1 361 + 361 Gaps:8 90.20 398 69.36 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_kegg lcl|pmum:103329571 9 356 + 348 Gaps:1 95.07 365 72.33 0.0 PI-PLC X domain-containing protein At5g67130
blastp_kegg lcl|pxb:103962744 20 356 + 337 Gaps:1 90.32 372 74.40 0.0 PI-PLC X domain-containing protein At5g67130
blastp_kegg lcl|mdm:103442441 1 356 + 356 Gaps:2 93.65 378 72.03 0.0 PI-PLC X domain-containing protein At5g67130-like
blastp_uniprot_sprot sp|Q93XX5|Y5713_ARATH 24 356 + 333 Gaps:3 77.93 426 54.22 1e-129 PI-PLC X domain-containing protein At5g67130 OS Arabidopsis thaliana GN At5g67130 PE 1 SV 1
rpsblast_cdd gnl|CDD|176530 74 343 + 270 Gaps:20 97.78 270 41.67 1e-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 73 343 + 271 Gaps:22 99.26 271 24.91 6e-41 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 73 289 + 217 Gaps:28 79.78 267 26.29 7e-14 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 87 194 + 108 Gaps:34 34.41 279 35.42 4e-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.
rpsblast_cdd gnl|CDD|176529 87 230 + 144 Gaps:63 53.82 288 22.58 9e-07 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.

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 25 411 387 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 20 24 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Phobius 9 19 11 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
PANTHER 35 356 322 PTHR13593 none none none
ProSiteProfiles 79 186 108 PS50007 none Phosphatidylinositol-specific phospholipase X-box domain profile. IPR000909
Phobius 1 24 24 SIGNAL_PEPTIDE none Signal peptide region none
SUPERFAMILY 73 346 274 SSF51695 none none IPR017946
Phobius 1 8 8 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Gene3D 73 346 274 G3DSA:3.20.20.190 none none IPR017946
PANTHER 35 356 322 PTHR13593:SF27 none none none

1 Localization

Analysis Start End Length
SignalP_EUK 1 24 23

0 Qtllist

0 Targeting