Protein : Qrob_P0183470.2 Q. robur
Protein Identifier  ? Qrob_P0183470.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=3) PTHR13683//PTHR13683:SF257 - ASPARTYL PROTEASES // SUBFAMILY NOT NAMED Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 409  
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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.

28 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100250885 17 386 + 370 none 72.41 511 74.86 0.0 aspartic proteinase-like protein 1-like
blastp_kegg lcl|tcc:TCM_001186 17 383 + 367 Gaps:2 67.72 539 76.16 0.0 Eukaryotic aspartyl protease family protein
blastp_kegg lcl|rcu:RCOM_0985440 17 383 + 367 Gaps:1 67.53 542 75.41 0.0 Aspartic proteinase nepenthesin-1 precursor putative
blastp_kegg lcl|pmum:103332651 17 383 + 367 Gaps:3 67.91 536 78.02 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103437619 17 382 + 366 Gaps:3 67.98 534 74.10 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|pper:PRUPE_ppa003982mg 17 383 + 367 Gaps:3 67.91 536 76.65 0.0 hypothetical protein
blastp_kegg lcl|fve:101315169 17 383 + 367 Gaps:5 67.16 539 74.31 0.0 aspartic proteinase-like protein 1-like
blastp_kegg lcl|pxb:103967028 17 382 + 366 Gaps:3 67.98 534 73.28 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|pop:POPTR_0005s08170g 17 383 + 367 Gaps:12 68.14 521 76.90 0.0 POPTRDRAFT_207559 hypothetical protein
blastp_kegg lcl|cit:102609510 17 376 + 360 Gaps:1 67.61 531 74.09 0.0 aspartic proteinase-like protein 1-like
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 19 364 + 346 Gaps:10 65.53 528 62.72 3e-149 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 20 321 + 302 Gaps:35 65.05 475 27.18 3e-18 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 23 321 + 299 Gaps:39 68.04 438 26.17 2e-11 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 34 324 + 291 Gaps:52 75.85 410 24.76 5e-10 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
blastp_uniprot_sprot sp|Q0IU52|ASP1_ORYSJ 32 329 + 298 Gaps:56 77.56 410 25.47 5e-10 Aspartic proteinase Asp1 OS Oryza sativa subsp. japonica GN ASP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 23 321 + 299 Gaps:61 68.19 437 26.17 9e-09 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q6XBF8|CDR1_ARATH 23 306 + 284 Gaps:38 66.82 437 25.34 1e-08 Aspartic proteinase CDR1 OS Arabidopsis thaliana GN CDR1 PE 1 SV 1
blastp_uniprot_sprot sp|Q4WDN4|OPSB_ASPFU 124 377 + 254 Gaps:32 52.78 485 24.61 8e-08 Probable aspartic-type endopeptidase opsB OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) GN opsB PE 3 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 23 321 + 299 Gaps:36 59.40 500 25.59 3e-07 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
rpsblast_cdd gnl|CDD|133143 52 321 + 270 Gaps:69 89.43 265 29.54 5e-27 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|133142 53 321 + 269 Gaps:60 86.08 273 32.77 8e-20 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.
rpsblast_cdd gnl|CDD|133138 24 257 + 234 Gaps:39 80.92 283 23.58 2e-19 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|178691 23 321 + 299 Gaps:61 70.07 431 28.48 4e-16 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133160 20 321 + 302 Gaps:71 86.81 326 23.67 2e-15 cd06096 Plasmepsin_5 Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite. The family contains a group of aspartic proteinases homologous to plasmepsin 5. Plasmepsins are a class of at least 10 enzymes produced by the plasmodium parasite. Through their haemoglobin-degrading activity they are an important cause of symptoms in malaria sufferers. This family of enzymes is a potential target for anti-malarial drugs. Plasmepsins are aspartic acid proteases which means their active site contains two aspartic acid residues. These two aspartic acid residue act respectively as proton donor and proton acceptor catalyzing the hydrolysis of peptide bond in proteins. Aspartic proteinases are composed of two structurally similar beta barrel lobes each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. There are four types of plasmepsins closely related but varying in the specificity of cleavage site. The name plasmepsin may come from plasmodium (the organism) and pepsin (a common aspartic acid protease with similar molecular structure). This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_cdd gnl|CDD|133139 54 321 + 268 Gaps:46 88.96 299 29.32 2e-14 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|200939 23 314 + 292 Gaps:57 84.49 316 26.97 4e-09 pfam00026 Asp Eukaryotic aspartyl protease. Aspartyl (acid) proteases include pepsins cathepsins and renins. Two-domain structure probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (pfam00077) which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.
rpsblast_cdd gnl|CDD|133141 55 314 + 260 Gaps:60 88.14 295 25.77 1e-08 cd05474 SAP_like SAPs pepsin-like proteinases secreted from pathogens to degrade host proteins. SAPs (Secreted aspartic proteinases) are secreted from a group of pathogenic fungi predominantly Candida species. They are secreted from the pathogen to degrade host proteins. SAP is one of the most significant extracellular hydrolytic enzymes produced by C. albicans. SAP proteins encoded by a family of 10 SAP genes. All 10 SAP genes of C. albicans encode preproenzymes approximately 60 amino acid longer than the mature enzyme which are processed when transported via the secretory pathway. The mature enzymes contain sequence motifs typical for all aspartyl proteinases including the two conserved aspartate residues other active site and conserved cysteine residues implicated in the maintenance of the three-dimensional structure. Most Sap proteins contain putative N-glycosylation sites but it remains to be determined which Sap proteins are glycosylated. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA). The overall structure of Sap protein conforms to the classical aspartic proteinase fold typified by pepsin. SAP is a bilobal enzyme 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. More recently evolved enzymes have similar three-dimensional structures however their amino acid sequences are more divergent except for the conserved catalytic site motif. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_kog gnl|CDD|36553 23 319 + 297 Gaps:30 76.13 398 30.03 1e-38 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

8 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 163 323 161 G3DSA:2.40.70.10 none none IPR021109
Pfam 194 317 124 PF14541 none Xylanase inhibitor C-terminal none
Pfam 21 155 135 PF14543 none Xylanase inhibitor N-terminal none
Gene3D 28 155 128 G3DSA:2.40.70.10 none none IPR021109
PANTHER 16 338 323 PTHR13683 none none IPR001461
SUPERFAMILY 18 323 306 SSF50630 none none IPR021109
ProSitePatterns 197 208 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
PANTHER 16 338 323 PTHR13683:SF257 none none none

0 Localization

0 Qtllist

0 Targeting