Protein : Qrob_P0053750.2 Q. robur
Protein Identifier  ? Qrob_P0053750.2 Organism . Name  Quercus robur
Score  14.1 Score Type  egn
Protein Description  (M=8) KOG0513//KOG4231 - Ca2+-independent phospholipase A2 [Lipid transport and metabolism]. // Intracellular membrane-bound Ca2+-independent phospholipase A2 [Lipid transport and metabolism]. Gene Prediction Quality  validated
Protein length 

Sequence

Length: 377  
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0008152 metabolic process The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
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.

35 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100250815 6 376 + 371 Gaps:16 93.61 407 66.93 0.0 patatin group A-3-like
blastp_kegg lcl|pop:POPTR_0007s11200g 6 376 + 371 Gaps:17 93.86 407 67.28 0.0 POPTRDRAFT_562990 hypothetical protein
blastp_kegg lcl|tcc:TCM_000589 9 376 + 368 Gaps:22 93.27 401 68.45 0.0 hypothetical protein
blastp_kegg lcl|vvi:100254055 12 376 + 365 Gaps:17 92.61 406 65.16 2e-179 patatin group A-3-like
blastp_kegg lcl|vvi:100249295 7 376 + 370 Gaps:17 93.61 407 64.83 2e-176 patatin group A-3-like
blastp_kegg lcl|rcu:RCOM_1407190 1 376 + 376 Gaps:21 94.57 405 69.19 3e-175 Patatin precursor putative
blastp_kegg lcl|pmum:103339930 5 376 + 372 Gaps:19 95.06 405 67.27 2e-174 patatin-like protein 3
blastp_kegg lcl|pper:PRUPE_ppa019010mg 7 376 + 370 Gaps:18 93.86 407 67.54 4e-173 hypothetical protein
blastp_kegg lcl|vvi:100267749 12 376 + 365 Gaps:17 92.61 406 65.69 2e-171 patatin group A-3-like
blastp_kegg lcl|vvi:100252227 12 376 + 365 Gaps:17 91.48 411 64.10 1e-169 patatin group A-3-like
blastp_pdb 1oxw_C 19 376 + 358 Gaps:38 92.23 373 47.97 2e-91 mol:protein length:373 Patatin
blastp_pdb 1oxw_B 19 376 + 358 Gaps:38 92.23 373 47.97 2e-91 mol:protein length:373 Patatin
blastp_pdb 1oxw_A 19 376 + 358 Gaps:38 92.23 373 47.97 2e-91 mol:protein length:373 Patatin
blastp_uniprot_sprot sp|Q2MY58|PATA3_SOLTU 5 376 + 372 Gaps:41 91.73 387 46.48 1e-100 Patatin group A-3 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|P15478|PATT5_SOLTU 5 376 + 372 Gaps:42 91.71 386 47.74 4e-95 Patatin-T5 OS Solanum tuberosum PE 1 SV 1
blastp_uniprot_sprot sp|Q42502|PT2K3_SOLTU 19 376 + 358 Gaps:38 89.12 386 48.26 2e-94 Patatin-2-Kuras 3 OS Solanum tuberosum GN pat2-k3 PE 1 SV 1
blastp_uniprot_sprot sp|Q3YJT2|PT2K2_SOLTU 19 376 + 358 Gaps:38 89.12 386 47.97 6e-94 Patatin-2-Kuras 2 OS Solanum tuberosum GN pat2-k2 PE 2 SV 1
blastp_uniprot_sprot sp|Q3YJT3|PT2K1_SOLTU 19 376 + 358 Gaps:38 91.98 374 47.97 3e-93 Patatin-2-Kuras 1 OS Solanum tuberosum GN pat2-k1 PE 1 SV 1
blastp_uniprot_sprot sp|Q2MY40|PAT11_SOLTU 5 376 + 372 Gaps:41 91.73 387 47.04 1e-92 Patatin-11 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|Q8LPW4|PAT17_SOLCD 5 376 + 372 Gaps:42 91.71 386 47.74 2e-91 Patatin-17 OS Solanum cardiophyllum PE 1 SV 1
blastp_uniprot_sprot sp|Q2MY42|PAT04_SOLTU 22 376 + 355 Gaps:38 88.34 386 48.09 2e-91 Patatin-04/09 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|Q2MY45|PAT06_SOLTU 22 376 + 355 Gaps:38 88.34 386 48.09 4e-91 Patatin-06 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|Q2MY36|PAT15_SOLTU 22 376 + 355 Gaps:38 88.34 386 48.09 4e-91 Patatin-15 OS Solanum tuberosum PE 1 SV 1
rpsblast_cdd gnl|CDD|132853 19 358 + 340 Gaps:19 100.00 349 60.17 1e-143 cd07214 Pat17_isozyme_like Patatin-like phospholipase of plants. Pat17 is an isozyme of patatin cloned from Solanum cardiophyllum. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2 EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids glycolipids sulfolipids and mono- and diacylglycerols thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm small residue X any residue and Nu nucleophile). Patatin-like phospholipase are included in this group. Members of this family have also been found in vertebrates.
rpsblast_cdd gnl|CDD|132854 24 354 + 331 Gaps:29 97.87 329 36.65 2e-66 cd07215 Pat17_PNPLA8_PNPLA9_like2 Patatin-like phospholipase of bacteria. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2 EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids glycolipids sulfolipids and mono- and diacylglycerols thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm small residue X any residue and Nu nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
rpsblast_cdd gnl|CDD|132838 24 347 + 324 Gaps:84 100.00 258 40.31 9e-56 cd07199 Pat17_PNPLA8_PNPLA9_like Patatin-like phospholipase includes PNPLA8 PNPLA9 and Pat17. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2 EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids glycolipids sulfolipids and mono- and diacylglycerols thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm small residue X any residue and Nu nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
rpsblast_cdd gnl|CDD|33420 20 290 + 271 Gaps:41 61.93 394 33.20 5e-30 COG3621 COG3621 Patatin [General function prediction only].
rpsblast_cdd gnl|CDD|132856 24 267 + 244 Gaps:63 67.15 344 35.50 3e-27 cd07217 Pat17_PNPLA8_PNPLA9_like4 Patatin-like phospholipase. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2 EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids glycolipids sulfolipids and mono- and diacylglycerols thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm small residue X any residue and Nu nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
rpsblast_cdd gnl|CDD|132852 24 316 + 293 Gaps:79 88.89 288 32.42 2e-26 cd07213 Pat17_PNPLA8_PNPLA9_like1 Patatin-like phospholipase. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2 EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids glycolipids sulfolipids and mono- and diacylglycerols thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm small residue X any residue and Nu nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
rpsblast_cdd gnl|CDD|132850 15 315 + 301 Gaps:55 89.61 308 27.17 6e-22 cd07211 Pat_PNPLA8 Patatin-like phospholipase domain containing protein 8. PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.

4 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 14 376 363 PTHR32176 none none none
SUPERFAMILY 21 360 340 SSF52151 none none IPR016035
Pfam 25 234 210 PF01734 none Patatin-like phospholipase IPR002641
Gene3D 12 375 364 G3DSA:3.40.1090.10 none none none

0 Localization

1 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_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5

0 Targeting