Protein : Qrob_P0540270.2 Q. robur

Protein Identifier  ? Qrob_P0540270.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=44) PF00407 - Pathogenesis-related protein Bet v I family Gene Prediction Quality  validated
Protein length 

Sequence

Length: 70  

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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0006952 defense response Reactions, triggered in response to the presence of a foreign body or the occurrence of an injury, which result in restriction of damage to the organism attacked or prevention/recovery from the infection caused by the attack.
GO:0009607 response to biotic stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a biotic stimulus, a stimulus caused or produced by a living organism.

19 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|cic:CICLE_v10017638mg 1 65 + 65 none 89.04 73 47.69 2e-11 hypothetical protein
blastp_kegg lcl|pop:POPTR_0010s12110g 1 60 + 60 none 37.97 158 50.00 3e-11 POPTRDRAFT_822077 Csf-2 family protein
blastp_kegg lcl|brp:103831620 2 69 + 68 none 43.31 157 42.65 4e-11 MLP-like protein 31
blastp_kegg lcl|cmo:103483946 1 65 + 65 Gaps:1 42.31 156 46.97 4e-10 MLP-like protein 43
blastp_kegg lcl|cit:102614114 1 61 + 61 none 33.33 183 49.18 6e-10 MLP-like protein 34-like
blastp_kegg lcl|brp:103852686 2 62 + 61 none 38.61 158 44.26 1e-09 MLP-like protein 31
blastp_kegg lcl|aly:ARALYDRAFT_894906 2 64 + 63 none 34.62 182 47.62 2e-09 hypothetical protein
blastp_kegg lcl|fve:101293540 3 65 + 63 Gaps:1 41.29 155 43.75 2e-09 MLP-like protein 43-like
blastp_kegg lcl|aly:ARALYDRAFT_894909 2 64 + 63 none 42.00 150 46.03 2e-09 hypothetical protein
blastp_kegg lcl|csv:101209301 1 65 + 65 Gaps:1 42.04 157 46.97 2e-09 MLP-like protein 34-like
blastp_pdb 2i9y_A 2 60 + 59 none 35.54 166 42.37 2e-08 mol:protein length:166 major latex protein-like protein 28 or MLP-li
blastp_uniprot_sprot sp|Q9SSK5|MLP43_ARATH 2 68 + 67 none 42.41 158 37.31 4e-09 MLP-like protein 43 OS Arabidopsis thaliana GN MLP43 PE 2 SV 1
blastp_uniprot_sprot sp|Q9SSK9|MLP28_ARATH 2 69 + 68 none 37.91 335 40.16 1e-08 MLP-like protein 28 OS Arabidopsis thaliana GN MLP28 PE 1 SV 1
blastp_uniprot_sprot sp|Q941R6|MLP31_ARATH 2 60 + 59 none 34.50 171 44.07 9e-08 MLP-like protein 31 OS Arabidopsis thaliana GN MLP31 PE 2 SV 2
blastp_uniprot_sprot sp|Q9SSK7|MLP34_ARATH 2 60 + 59 none 18.67 316 44.07 9e-08 MLP-like protein 34 OS Arabidopsis thaliana GN MLP34 PE 2 SV 1
blastp_uniprot_sprot sp|P85524|KIRO_ACTDE 1 62 + 62 none 41.33 150 38.71 4e-07 Kirola OS Actinidia deliciosa PE 1 SV 1
rpsblast_cdd gnl|CDD|144121 5 63 + 59 none 39.33 150 44.07 1e-11 pfam00407 Bet_v_1 Pathogenesis-related protein Bet v I family. This family is named after Bet v 1 the major birch pollen allergen. This protein belongs to family 10 of plant pathogenesis-related proteins (PR-10) cytoplasmic proteins of 15-17 kd that are wide-spread among dicotyledonous plants. In recent years a number of diverse plant proteins with low sequence similarity to Bet v 1 was identified. A classification by sequence similarity yielded several subfamilies related to PR-10: - Pathogenesis-related proteins PR-10: These proteins were identified as major tree pollen allergens in birch and related species (hazel alder) as plant food allergens expressed in high levels in fruits vegetables and seeds (apple celery hazelnut) and as pathogenesis-related proteins whose expression is induced by pathogen infection wounding or abiotic stress. Hyp-1 an enzyme involved in the synthesis of the bioactive naphthodianthrone hypericin in St. John's wort (Hypericum perforatum) also belongs to this family. Most of these proteins were found in dicotyledonous plants. In addition related sequences were identified in monocots and conifers. - Cytokinin-specific binding proteins: These legume proteins bind cytokinin plant hormones. - (S)-Norcoclaurine synthases are enzymes catalyzing the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine. -Major latex proteins and ripening-related proteins are proteins of unknown biological function that were first discovered in the latex of opium poppy (Papaver somniferum) and later found to be upregulated during ripening of fruits such as strawberry and cucumber. The occurrence of Bet v 1-related proteins is confined to seed plants with the exception of a cytokinin-binding protein from the moss Physcomitrella patens.
rpsblast_cdd gnl|CDD|198105 2 55 + 54 none 35.76 151 46.30 5e-09 smart01037 Bet_v_1 Pathogenesis-related protein Bet v I family. This family is named after Bet v 1 the major birch pollen allergen. This protein belongs to family 10 of plant pathogenesis-related proteins (PR-10) cytoplasmic proteins of 15-17 kd that are wide-spread among dicotyledonous plants. In recent years a number of diverse plant proteins with low sequence similarity to Bet v 1 was identified. A classification by sequence similarity yielded several subfamilies related to PR-10.- Pathogenesis-related proteins PR-10: These proteins were identified as major tree pollen allergens in birch and related species (hazel alder) as plant food allergens expressed in high levels in fruits vegetables and seeds (apple celery hazelnut) and as pathogenesis-related proteins whose expression is induced by pathogen infection wounding or abiotic stress. Hyp-1 an enzyme involved in the synthesis of the bioactive naphthodianthrone hypericin in St. John's wort (Hypericum perforatum) also belongs to this family. Most of these proteins were found in dicotyledonous plants. In addition related sequences were identified in monocots and conifers. - Cytokinin-specific binding proteins: These legume proteins bind cytokinin plant hormones. - (S)-Norcoclaurine synthases are enzymes catalysing the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine. -Major latex proteins and ripening-related proteins are proteins of unknown biological function that were first discovered in the latex of opium poppy (Papaver somniferum) and later found to be upregulated during ripening of fruits such as strawberry and cucumber. The occurrence of Bet v 1-related proteins is confined to seed plants with the exception of a cytokinin-binding protein from the moss Physcomitrella patens.
rpsblast_cdd gnl|CDD|176858 5 63 + 59 Gaps:1 39.19 148 37.93 2e-08 cd07816 Bet_v1-like Ligand-binding bet_v_1 domain of major pollen allergen of white birch (Betula verrucosa) Bet v 1 and related proteins. This family includes the ligand binding domain of Bet v 1 (the major pollen allergen of white birch Betula verrucosa) and related proteins. In addition to birch Bet v 1 this family includes other plant intracellular pathogenesis-related class 10 (PR-10) proteins norcoclaurine synthases (NCSs) cytokinin binding proteins (CSBPs) major latex proteins (MLPs) and ripening-related proteins. It belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Members of this family binds a diverse range of ligands. Bet v 1 can bind brassinosteroids cytokinins flavonoids and fatty acids. Hyp-1 a PR-10 from Hypericum perforatum/St. John's wort catalyzes the condensation of two molecules of emodin to the bioactive naphthodianthrone hypericin. NCSs catalyze the condensation of dopamine and 4-hydroxyphenylacetaldehyde to (S)-norcoclaurine the first committed step in the biosynthesis of benzylisoquinoline alkaloids such as morphine. The role of MLPs is unclear however they are associated with fruit and flower development and in pathogen defense responses. A number of PR-10 proteins in this subgroup including Bet v 1 have in vitro RNase activity the biological significance of which is unclear. Bet v 1 family proteins have a conserved glycine-rich P (phosphate-binding)-loop proximal to the entrance of the ligand-binding pocket. However its conformation differs from that of the canonical P-loop structure found in nucleotide-binding proteins. Several PR-10 members including Bet v1 are allergenic. Cross-reactivity of Bet v 1 with homologs from plant foods results in birch-fruit syndrome.

4 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 1 56 56 PTHR31907 none none none
Gene3D 1 64 64 G3DSA:3.30.530.20 none none IPR023393
SUPERFAMILY 5 64 60 SSF55961 none none none
Pfam 3 66 64 PF00407 none Pathogenesis-related protein Bet v I family IPR000916

0 Localization

2 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_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC_3P Qrob_Chr05 5 s_2GDU0O_517 s_1BT8O3_239 25,81 0 55,45 lod 2,2101 5,5

0 Targeting