Protein : Qrob_P0053760.2 Q. robur
Protein Identifier  ? Qrob_P0053760.2 Organism . Name  Quercus robur
Score  94.1 Score Type  egn
Protein Description  (M=12) KOG0513 - Ca2+-independent phospholipase A2 [Lipid transport and metabolism]. Gene Prediction Quality  validated
Protein length 

Sequence

Length: 438  
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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.

34 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100250815 6 431 + 426 Gaps:29 97.54 407 69.27 0.0 patatin group A-3-like
blastp_kegg lcl|pop:POPTR_0007s11200g 6 434 + 429 Gaps:28 98.53 407 68.33 0.0 POPTRDRAFT_562990 hypothetical protein
blastp_kegg lcl|tcc:TCM_000589 9 436 + 428 Gaps:33 98.50 401 69.62 0.0 hypothetical protein
blastp_kegg lcl|pmum:103339930 5 430 + 426 Gaps:30 98.77 405 71.25 0.0 patatin-like protein 3
blastp_kegg lcl|vvi:100249295 7 437 + 431 Gaps:28 99.02 407 66.25 0.0 patatin group A-3-like
blastp_kegg lcl|pper:PRUPE_ppa019010mg 7 430 + 424 Gaps:29 97.54 407 71.03 0.0 hypothetical protein
blastp_kegg lcl|rcu:RCOM_1407190 1 434 + 434 Gaps:35 100.00 405 70.86 0.0 Patatin precursor putative
blastp_kegg lcl|vvi:100254055 12 434 + 423 Gaps:28 97.29 406 66.33 0.0 patatin group A-3-like
blastp_kegg lcl|fve:101299417 4 435 + 432 Gaps:30 99.26 407 67.57 0.0 patatin group A-3-like
blastp_kegg lcl|vvi:100267749 12 434 + 423 Gaps:28 97.29 406 67.09 0.0 patatin group A-3-like
blastp_pdb 1oxw_C 19 430 + 412 Gaps:63 96.25 373 50.42 2e-96 mol:protein length:373 Patatin
blastp_pdb 1oxw_B 19 430 + 412 Gaps:63 96.25 373 50.42 2e-96 mol:protein length:373 Patatin
blastp_pdb 1oxw_A 19 430 + 412 Gaps:63 96.25 373 50.42 2e-96 mol:protein length:373 Patatin
blastp_uniprot_sprot sp|Q2MY58|PATA3_SOLTU 5 430 + 426 Gaps:66 95.61 387 48.65 7e-106 Patatin group A-3 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|Q3YJS9|PT3K1_SOLTU 5 430 + 426 Gaps:61 98.66 374 51.49 2e-98 Patatin-3-Kuras 1 OS Solanum tuberosum GN pat3-k1 PE 1 SV 1
blastp_uniprot_sprot sp|P15478|PATT5_SOLTU 5 430 + 426 Gaps:65 95.60 386 50.14 7e-98 Patatin-T5 OS Solanum tuberosum PE 1 SV 1
blastp_uniprot_sprot sp|Q2MY40|PAT11_SOLTU 5 430 + 426 Gaps:62 95.61 387 48.38 1e-97 Patatin-11 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|Q3YJT2|PT2K2_SOLTU 19 430 + 412 Gaps:59 93.01 386 49.30 1e-97 Patatin-2-Kuras 2 OS Solanum tuberosum GN pat2-k2 PE 2 SV 1
blastp_uniprot_sprot sp|Q42502|PT2K3_SOLTU 19 430 + 412 Gaps:59 93.01 386 49.03 8e-97 Patatin-2-Kuras 3 OS Solanum tuberosum GN pat2-k3 PE 1 SV 1
blastp_uniprot_sprot sp|Q8LPW4|PAT17_SOLCD 5 430 + 426 Gaps:67 95.60 386 50.95 2e-96 Patatin-17 OS Solanum cardiophyllum PE 1 SV 1
blastp_uniprot_sprot sp|Q3YJT3|PT2K1_SOLTU 19 430 + 412 Gaps:59 95.99 374 48.75 2e-96 Patatin-2-Kuras 1 OS Solanum tuberosum GN pat2-k1 PE 1 SV 1
blastp_uniprot_sprot sp|Q2MY37|PAT14_SOLTU 21 430 + 410 Gaps:59 92.49 386 49.58 7e-95 Patatin-14 OS Solanum tuberosum PE 2 SV 1
blastp_uniprot_sprot sp|Q2MY42|PAT04_SOLTU 21 430 + 410 Gaps:59 92.49 386 49.02 8e-95 Patatin-04/09 OS Solanum tuberosum PE 2 SV 1
rpsblast_cdd gnl|CDD|132853 19 396 + 378 Gaps:29 100.00 349 63.32 1e-152 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 24 392 + 369 Gaps:49 97.87 329 38.82 2e-67 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 24 385 + 362 Gaps:40 100.00 258 43.80 2e-36 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 20 367 + 348 Gaps:45 80.46 394 27.13 2e-29 COG3621 COG3621 Patatin [General function prediction only].
rpsblast_cdd gnl|CDD|132852 24 354 + 331 Gaps:99 88.89 288 34.77 2e-27 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|132856 24 291 + 268 Gaps:77 67.15 344 34.63 1e-23 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|201943 25 258 + 234 Gaps:57 100.00 189 28.57 5e-19 pfam01734 Patatin Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 25 258 234 PF01734 none Patatin-like phospholipase IPR002641
PANTHER 14 114 101 PTHR32176 none none none
PANTHER 146 427 282 PTHR32176 none none none
Gene3D 142 428 287 G3DSA:3.40.1090.10 none none none
Gene3D 12 109 98 G3DSA:3.40.1090.10 none none none
SUPERFAMILY 20 109 90 SSF52151 none none IPR016035
SUPERFAMILY 148 398 251 SSF52151 none none IPR016035

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