Protein : Qrob_P0152340.2 Q. robur
Protein Identifier  ? Qrob_P0152340.2 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: 427  
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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.

32 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100245570 16 426 + 411 Gaps:38 98.39 436 52.68 2e-132 aspartic proteinase nepenthesin-1-like
blastp_kegg lcl|cam:101506105 3 426 + 424 Gaps:32 98.67 452 48.21 4e-132 aspartic proteinase nepenthesin-1-like
blastp_kegg lcl|cmo:103486136 5 426 + 422 Gaps:43 99.57 461 48.58 8e-132 aspartic proteinase nepenthesin-1
blastp_kegg lcl|pop:POPTR_0001s31370g 6 426 + 421 Gaps:24 99.09 439 51.72 2e-131 POPTRDRAFT_549896 aspartyl protease family protein
blastp_kegg lcl|rcu:RCOM_1697100 22 426 + 405 Gaps:24 94.80 442 52.51 1e-130 Aspartic proteinase nepenthesin-1 precursor putative
blastp_kegg lcl|sot:102603034 40 426 + 387 Gaps:33 91.89 444 49.02 3e-130 aspartic proteinase nepenthesin-1-like
blastp_kegg lcl|tcc:TCM_001628 11 426 + 416 Gaps:24 97.51 441 51.63 3e-130 Eukaryotic aspartyl protease family protein
blastp_kegg lcl|pmum:103327300 7 426 + 420 Gaps:43 99.13 461 48.80 4e-130 aspartic proteinase nepenthesin-1
blastp_kegg lcl|csv:101227608 40 426 + 387 Gaps:31 89.37 461 50.24 6e-130 aspartic proteinase nepenthesin-1-like
blastp_kegg lcl|sly:101268575 40 426 + 387 Gaps:30 91.84 441 49.63 6e-130 aspartic proteinase nepenthesin-1-like
blastp_pdb 3aup_D 181 418 + 238 Gaps:27 62.28 403 27.49 1e-07 mol:protein length:403 Basic 7S globulin
blastp_pdb 3aup_C 181 418 + 238 Gaps:27 62.28 403 27.49 1e-07 mol:protein length:403 Basic 7S globulin
blastp_pdb 3aup_B 181 418 + 238 Gaps:27 62.28 403 27.49 1e-07 mol:protein length:403 Basic 7S globulin
blastp_pdb 3aup_A 181 418 + 238 Gaps:27 62.28 403 27.49 1e-07 mol:protein length:403 Basic 7S globulin
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 5 423 + 419 Gaps:32 99.08 437 47.11 2e-112 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 38 423 + 386 Gaps:29 90.64 438 43.07 7e-96 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 84 423 + 340 Gaps:32 71.60 500 33.80 3e-52 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LHE3|ASPG2_ARATH 53 423 + 371 Gaps:35 81.70 470 33.07 5e-46 Protein ASPARTIC PROTEASE IN GUARD CELL 2 OS Arabidopsis thaliana GN ASPG2 PE 2 SV 1
blastp_uniprot_sprot sp|Q3EBM5|ASPR1_ARATH 18 423 + 406 Gaps:63 98.21 447 31.44 5e-41 Probable aspartic protease At2g35615 OS Arabidopsis thaliana GN At2g35615 PE 3 SV 1
blastp_uniprot_sprot sp|Q6XBF8|CDR1_ARATH 38 426 + 389 Gaps:61 93.82 437 33.17 1e-39 Aspartic proteinase CDR1 OS Arabidopsis thaliana GN CDR1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LZL3|PCS1L_ARATH 123 424 + 302 Gaps:47 73.07 453 29.91 7e-26 Aspartic proteinase PCS1 OS Arabidopsis thaliana GN PCS1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 108 423 + 316 Gaps:51 67.58 475 27.73 5e-16 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|P69477|NEP2_NEPDI 87 196 + 110 Gaps:16 52.81 178 45.74 3e-12 Aspartic proteinase nepenthesin-2 (Fragments) OS Nepenthes distillatoria PE 1 SV 1
blastp_uniprot_sprot sp|P69476|NEP1_NEPDI 87 191 + 105 Gaps:38 57.93 164 45.26 6e-09 Aspartic proteinase nepenthesin-1 (Fragments) OS Nepenthes distillatoria PE 1 SV 1
rpsblast_cdd gnl|CDD|133143 98 423 + 326 Gaps:75 100.00 265 49.81 6e-74 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|178691 17 425 + 409 Gaps:57 99.30 431 36.45 2e-65 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133139 98 423 + 326 Gaps:41 100.00 299 36.12 1e-62 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_cdd gnl|CDD|133138 99 420 + 322 Gaps:71 100.00 283 26.86 7e-31 cd05471 pepsin_like Pepsin-like aspartic proteases bilobal enzymes that cleave bonds in peptides at acidic pH. Pepsin-like aspartic proteases are found in mammals plants fungi and bacteria. These well known and extensively characterized enzymes include pepsins chymosin renin cathepsins and fungal aspartic proteases. Several have long been known to be medically (renin cathepsin D and E pepsin) or commercially (chymosin) important. Structurally aspartic proteases are bilobal enzymes each lobe contributing a catalytic Aspartate 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. Most members of the pepsin family specifically cleave bonds in peptides that are 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. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_cdd gnl|CDD|133156 108 418 + 311 Gaps:64 96.96 362 25.07 2e-23 cd05489 xylanase_inhibitor_I_like TAXI-I inhibits degradation of xylan in the cell wall. Xylanase inhibitor-I (TAXI-I) is a member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases. Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes which hinder a possible invasion and colonization by antagonists. Xylanases of fungal and bacterial pathogens are the key enzymes in the degradation of xylan in the cell wall. Plants secrete proteins that inhibit these degradation glycosidases including xylanase. Surprisingly TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional because one or more residues of the essential catalytic triad are absent. The structure of the TAXI-inhibitor Aspergillus niger xylanase I complex illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors. This family also contains pepsin-like aspartic proteinases homologous to TAXI-I. Unlike TAXI-I they have active site aspartates and are functionally active. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_cdd gnl|CDD|133142 151 423 + 273 Gaps:83 87.18 273 31.93 4e-14 cd05475 nucellin_like Nucellins plant aspartic proteases specifically expressed in nucellar cells during degradation. Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. This degradation is a characteristic of programmed cell death. Nucellins are plant aspartic proteases specifically expressed in nucellar cells during degradation. 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 and two other regions nearly identical to two regions of plant aspartic proteases. 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. Although the three-dimensional structures of the two lobes are very similar the amino acid sequences are more divergent except for the conserved catalytic site motif.

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 99 243 145 PF14543 none Xylanase inhibitor N-terminal none
Phobius 32 426 395 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Gene3D 96 243 148 G3DSA:2.40.70.10 none none IPR021109
Phobius 1 31 31 SIGNAL_PEPTIDE none Signal peptide region none
Gene3D 250 425 176 G3DSA:2.40.70.10 none none IPR021109
Pfam 268 419 152 PF14541 none Xylanase inhibitor C-terminal none
SUPERFAMILY 93 424 332 SSF50630 none none IPR021109
Phobius 1 10 10 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
PANTHER 1 426 426 PTHR13683:SF223 none none none
Phobius 27 31 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
PANTHER 1 426 426 PTHR13683 none none IPR001461
Phobius 11 26 16 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none

2 Localization

Analysis Start End Length
TMHMM 7 26 19
SignalP_EUK 1 27 26

4 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
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
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

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 27   Secretory pathway 1 0.986 0.011 NON-PLANT 27