Protein : Qrob_P0002880.2 Q. robur
Protein Identifier  ? Qrob_P0002880.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=3) PTHR22953//PTHR22953:SF14 - ACID PHOSPHATASE RELATED // SUBFAMILY NOT NAMED Code Enzyme  EC:3.1.4.1
Gene Prediction Quality  validated Protein length 

Sequence

Length: 191  
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0 Synonyms

1 GO Terms

Identifier Name Description
GO:0016787 hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.

19 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pvu:PHAVU_002G168300g 3 178 + 176 Gaps:2 26.32 661 85.63 9e-103 hypothetical protein
blastp_kegg lcl|cit:102616214 3 179 + 177 none 26.58 666 81.92 1e-101 probable inactive purple acid phosphatase 2-like
blastp_kegg lcl|cam:101492338 3 178 + 176 Gaps:2 26.48 657 83.91 2e-101 probable inactive purple acid phosphatase 2-like
blastp_kegg lcl|cic:CICLE_v10030896mg 3 178 + 176 none 26.43 666 82.39 4e-101 hypothetical protein
blastp_kegg lcl|rcu:RCOM_1621460 3 178 + 176 none 27.08 650 83.52 4e-101 Nucleotide pyrophosphatase/phosphodiesterase putative
blastp_kegg lcl|pop:POPTR_0010s16790g 3 178 + 176 none 27.20 647 80.11 3e-98 POPTRDRAFT_566952 purple acid phosphatase family protein
blastp_kegg lcl|gmx:100799931 3 178 + 176 Gaps:3 26.44 662 82.86 9e-98 probable inactive purple acid phosphatase 2-like
blastp_kegg lcl|mtr:MTR_4g082940 3 178 + 176 Gaps:2 26.98 645 81.61 1e-97 hypothetical protein
blastp_kegg lcl|fve:101292893 3 178 + 176 none 28.07 627 77.27 1e-96 probable inactive purple acid phosphatase 2-like
blastp_kegg lcl|obr:102713925 3 178 + 176 none 31.43 560 76.70 3e-96 probable inactive purple acid phosphatase 2-like
blastp_uniprot_sprot sp|Q9LMG7|PPA2_ARATH 3 178 + 176 none 26.83 656 71.02 1e-90 Probable inactive purple acid phosphatase 2 OS Arabidopsis thaliana GN PAP2 PE 2 SV 1
blastp_uniprot_sprot sp|Q9ZQ81|PPA9_ARATH 3 178 + 176 Gaps:2 27.34 651 71.35 2e-89 Probable inactive purple acid phosphatase 9 OS Arabidopsis thaliana GN PAP9 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LMX4|PPA1_ARATH 1 174 + 174 Gaps:34 25.77 613 41.77 1e-19 Probable inactive purple acid phosphatase 1 OS Arabidopsis thaliana GN PAP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q5MAU8|PPA27_ARATH 1 174 + 174 Gaps:28 25.86 611 40.51 2e-19 Probable inactive purple acid phosphatase 27 OS Arabidopsis thaliana GN PAP27 PE 2 SV 1
blastp_uniprot_sprot sp|Q8H1R2|PPA24_ARATH 3 174 + 172 Gaps:26 25.37 615 36.54 8e-18 Probable inactive purple acid phosphatase 24 OS Arabidopsis thaliana GN PAP24 PE 2 SV 1
blastp_uniprot_sprot sp|Q687E1|NPP_HORVU 22 174 + 153 Gaps:24 36.68 368 39.26 2e-15 Nucleotide pyrophosphatase/phosphodiesterase (Fragments) OS Hordeum vulgare GN npp PE 1 SV 2
blastp_uniprot_sprot sp|A5D6U8|PAPL_DANRE 3 180 + 178 Gaps:49 30.47 443 37.78 8e-07 Iron/zinc purple acid phosphatase-like protein OS Danio rerio GN papl PE 2 SV 1
rpsblast_cdd gnl|CDD|163615 15 177 + 163 Gaps:38 43.88 294 38.76 2e-24 cd00839 MPP_PAPs purple acid phosphatases of the metallophosphatase superfamily metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants animals and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse but all share a conserved domain with an active site consisting of two metal ions (usually manganese iron or zinc) coordinated with octahedral geometry by a cage of histidine aspartate and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases Dbr1-like RNA lariat debranching enzymes YfcE-like phosphodiesterases purple acid phosphatases (PAPs) YbbF-like UDP-2 3-diacylglucosamine hydrolases and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
rpsblast_kog gnl|CDD|36592 3 177 + 175 Gaps:40 30.31 452 55.47 4e-29 KOG1378 KOG1378 KOG1378 Purple acid phosphatase [Carbohydrate transport and metabolism].

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 21 176 156 G3DSA:3.60.21.10 none none IPR029052
SUPERFAMILY 23 176 154 SSF56300 none none IPR029052
PANTHER 3 174 172 PTHR22953 none none none
Pfam 55 110 56 PF00149 none Calcineurin-like phosphoesterase IPR004843
PANTHER 3 174 172 PTHR22953:SF14 none none none

0 Localization

14 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_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
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*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran_2000_2002_QTL3_Delta.F Qrob_Chr08 8 s_1A3EF7_1406 s_1AIWYC_607 30.17 21,01 40,21 lod 6.8553 0.055
Bourran2_2014_aSeqBC_A4 Qrob_Chr08 8 v_15999_278 v_AP13YL15_395 32,52 4,22 57,22 lod 2,7561 6,7
Bourran2_2014_nFork*_A4 Qrob_Chr08 8 PIE175 s_1CD7GJ_1398 31,22 5,24 57,24 lod 2,6724 6,8
Bourran2_2014_nLBD*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,25 0 35,55 lod 2,5951 6
Bourran2_2014_nP*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,19 0 31,97 lod 2,8472 6
Bourran2_2014_nPriLBD_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,36 0 30,43 lod 2,5806 5,1
Bourran2_2014_nPriLBD_A4 Qrob_Chr08 8 PIE175 v_9164_159 31,85 15,39 48,29 lod 2,8308 6,8
Bourran2_2015_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Champenoux_2015_nSeqBC_A4 Qrob_Chr08 8 v_AD7YD13_501 s_1A7IED_780 43,44 43,42 43,99 lod 3.7 8.9
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL3_d13Cf Qrob_Chr08 8 v_5216_549 v_11625_20 37.08 12,26 54,9 lod 6.5888 0.04

0 Targeting