Protein : Qrob_P0177000.2 Q. robur
Protein Identifier  ? Qrob_P0177000.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=17) PTHR13683:SF223 - ASPARTYL PROTEASE FAMILY PROTEIN (PTHR13683:SF223) Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 214  
Paste the following link
Lists
This Protein isn't in any lists. Upload a list.

Sequence Feature Displayer

Protein Sequence Displayer

J Browse Displayer

0 Synonyms

2 GO Terms

Identifier Name Description
GO:0006508 proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0004190 aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.

18 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa022155mg 20 212 + 193 Gaps:10 54.78 345 58.73 6e-62 hypothetical protein
blastp_kegg lcl|mdm:103419560 20 212 + 193 Gaps:10 44.37 426 56.08 8e-58 aspartic proteinase CDR1-like
blastp_kegg lcl|pxb:103961355 20 212 + 193 Gaps:10 44.37 426 56.08 1e-57 aspartic proteinase CDR1-like
blastp_kegg lcl|pvu:PHAVU_002G037100g 13 212 + 200 Gaps:14 45.86 423 55.15 1e-55 hypothetical protein
blastp_kegg lcl|pvu:PHAVU_002G037200g 13 212 + 200 Gaps:14 45.86 423 54.64 9e-55 hypothetical protein
blastp_kegg lcl|pvu:PHAVU_002G037300g 13 210 + 198 Gaps:13 43.02 444 54.97 1e-53 hypothetical protein
blastp_kegg lcl|pvu:PHAVU_002G037000g 13 212 + 200 Gaps:14 46.19 420 53.61 4e-52 hypothetical protein
blastp_kegg lcl|mtr:MTR_5g008150 13 212 + 200 Gaps:14 47.46 413 53.06 4e-52 Aspartic proteinase nepenthesin-1
blastp_kegg lcl|gmx:100814140 13 212 + 200 Gaps:15 45.14 432 52.82 2e-51 aspartic proteinase CDR1-like
blastp_kegg lcl|cam:101514531 13 212 + 200 Gaps:15 46.76 417 52.82 4e-51 aspartic proteinase CDR1-like
blastp_uniprot_sprot sp|Q6XBF8|CDR1_ARATH 20 213 + 194 Gaps:14 43.48 437 40.53 1e-28 Aspartic proteinase CDR1 OS Arabidopsis thaliana GN CDR1 PE 1 SV 1
blastp_uniprot_sprot sp|Q3EBM5|ASPR1_ARATH 43 211 + 169 Gaps:24 38.70 447 36.99 7e-23 Probable aspartic protease At2g35615 OS Arabidopsis thaliana GN At2g35615 PE 3 SV 1
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 56 210 + 155 Gaps:14 35.47 437 30.32 1e-12 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 29 210 + 182 Gaps:19 42.24 438 28.11 2e-09 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
rpsblast_cdd gnl|CDD|178691 13 212 + 200 Gaps:17 44.78 431 45.08 5e-47 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133143 15 210 + 196 Gaps:53 60.00 265 38.36 2e-23 cd05476 pepsin_A_like_plant Chroloplast Nucleoids DNA-binding Protease and Nucellin pepsin-like aspartic proteases from plants. This family contains pepsin like aspartic proteases from plants including Chloroplast Nucleoids DNA-binding Protease and Nucellin. Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1 5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco and Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. Structurally aspartic proteases are bilobal enzymes each lobe contributing a catalytic Asp residue with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains although structurally related by a 2-fold axis have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes with an extended loop projecting over the cleft to form an 11-residue flap which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH.
rpsblast_cdd gnl|CDD|133139 13 210 + 198 Gaps:31 64.55 299 29.53 2e-09 cd05472 cnd41_like Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1 5-bisphosphate carboxylase/oxygenase. Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1 5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco. Antisense tobacco with reduced amount of CND41 maintained green leaves and constant protein levels especially Rubisco. CND41 has DNA-binding as well as aspartic protease activities. The pepsin-like aspartic protease domain is located at the C-terminus of the protein. The enzyme is characterized by having two aspartic protease catalytic site motifs the Asp-Thr-Gly-Ser in the N-terminal and Asp-Ser-Gly-Ser in the C-terminal region. Aspartic proteases are bilobal enzymes each lobe contributing a catalytic Asp residue with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_kog gnl|CDD|36553 29 211 + 183 Gaps:12 45.98 398 28.96 3e-12 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 29 213 185 PTHR13683 none none IPR001461
Gene3D 38 212 175 G3DSA:2.40.70.10 none none IPR021109
PANTHER 29 213 185 PTHR13683:SF223 none none none
Pfam 55 207 153 PF14541 none Xylanase inhibitor C-terminal none
SUPERFAMILY 29 211 183 SSF50630 none none IPR021109

0 Localization

8 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran_2000_2002_QTL7_Delta.F Qrob_Chr09 9 v_5944_442 s_1BA1PC_866 23.51 10,96 35,74 lod 4.1466 0.041
Bourran2_2003_QTL11_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 4,16 48,16 lod 2,3 5,1
Bourran2_2004_QTL12_peak_Bud_burst_3P Qrob_Chr09 9 s_1BDO6G_250 s_1A83AM_496 34,31 9,31 44,31 lod 3,6 7,6
Bourran2_2004_QTL14_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,83 10,33 22,33 lod 3,8 9
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran2_2015_nSecLBD_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 35,81 34,88 37,45 lod 4.4 10.4
PM_1999_QTL15_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 9,16 47,16 lod 3,6 6,5
Bourran1_2003_QTL5_peak_Bud_burst_3P Qrob_Chr09 9 s_1ATM17_504 s_1AYZFM_899 29,81 19,81 41,81 lod 3,3 8,9

0 Targeting