Protein : Qrob_P0036570.2 Q. robur
Protein Identifier  ? Qrob_P0036570.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=44) 3.4.14.10 - Tripeptidyl-peptidase II. Code Enzyme  EC:3.4.14.10
Gene Prediction Quality  validated Protein length 

Sequence

Length: 648  
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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:0004252 serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0014s02640g 22 647 + 626 Gaps:127 97.50 760 53.98 0.0 hypothetical protein
blastp_kegg lcl|vvi:100248833 28 645 + 618 Gaps:127 99.59 736 52.52 0.0 subtilisin-like protease-like
blastp_kegg lcl|pmum:103320443 2 647 + 646 Gaps:135 97.44 781 51.51 0.0 subtilisin-like protease
blastp_kegg lcl|cic:CICLE_v10003898mg 2 645 + 644 Gaps:132 99.34 757 51.20 0.0 hypothetical protein
blastp_kegg lcl|pper:PRUPEppa1027224mg 17 647 + 631 Gaps:130 98.82 760 51.66 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_033805 26 647 + 622 Gaps:124 96.45 761 51.63 0.0 Subtilisin-like serine protease 2 putative
blastp_kegg lcl|cit:102618416 2 645 + 644 Gaps:132 99.34 757 50.40 0.0 subtilisin-like protease-like
blastp_kegg lcl|fve:101313186 14 647 + 634 Gaps:132 99.34 759 51.06 0.0 subtilisin-like protease-like
blastp_kegg lcl|pxb:103952443 26 647 + 622 Gaps:143 97.14 769 47.93 0.0 subtilisin-like protease
blastp_kegg lcl|tcc:TCM_033806 30 647 + 618 Gaps:224 99.48 1160 47.14 0.0 Subtilisin-like serine protease 2 putative
blastp_pdb 3i74_B 105 643 + 539 Gaps:124 98.77 649 34.63 3e-89 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i74_A 105 643 + 539 Gaps:124 98.77 649 34.63 3e-89 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_B 105 643 + 539 Gaps:124 98.77 649 34.63 3e-89 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_A 105 643 + 539 Gaps:124 98.77 649 34.63 3e-89 mol:protein length:649 Subtilisin-like protease
blastp_uniprot_sprot sp|O65351|SUBL_ARATH 3 642 + 640 Gaps:166 99.34 757 32.98 2e-94 Subtilisin-like protease OS Arabidopsis thaliana GN ARA12 PE 1 SV 1
blastp_uniprot_sprot sp|O64495|SDD1_ARATH 19 639 + 621 Gaps:147 94.97 775 30.57 3e-81 Subtilisin-like protease SDD1 OS Arabidopsis thaliana GN SDD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LLL8|XSP1_ARATH 27 643 + 617 Gaps:163 95.59 749 31.28 4e-54 Xylem serine proteinase 1 OS Arabidopsis thaliana GN XSP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q39547|CUCM1_CUCME 37 643 + 607 Gaps:81 72.37 731 34.59 4e-33 Cucumisin OS Cucumis melo PE 1 SV 1
blastp_uniprot_sprot sp|P29141|SUBV_BACSU 194 463 + 270 Gaps:90 38.46 806 27.74 1e-09 Minor extracellular protease vpr OS Bacillus subtilis (strain 168) GN vpr PE 1 SV 1
blastp_uniprot_sprot sp|P29139|ISP_PAEPO 88 300 + 213 Gaps:44 54.29 326 33.90 1e-06 Intracellular serine protease OS Paenibacillus polymyxa GN isp PE 1 SV 1
rpsblast_cdd gnl|CDD|173795 105 467 + 363 Gaps:25 86.32 307 47.92 1e-67 cd04852 Peptidases_S8_3 Peptidase S8 family domain uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173800 127 509 + 383 Gaps:112 100.00 295 35.93 9e-29 cd07474 Peptidases_S8_subtilisin_Vpr-like Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases along with WprA that are capable of processing subtilin. Asp Ser His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173815 129 487 + 359 Gaps:118 97.24 254 35.63 3e-18 cd07490 Peptidases_S8_6 Peptidase S8 family domain uncharacterized subfamily 6. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173787 130 317 + 188 Gaps:32 65.56 241 29.11 7e-18 cd00306 Peptidases_S8_S53 Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile aspartate as an electrophile and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family while glutamic acid has the same role here as the histidine base. However the aspartic acid residue that acts as an electrophile is quite different. In S53 it follows glutamic acid while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds some are intracellular while others are extracellular some function at extreme temperatures and others at high or low pH values.
rpsblast_cdd gnl|CDD|173814 126 300 + 175 Gaps:27 49.36 312 31.17 4e-14 cd07489 Peptidases_S8_5 Peptidase S8 family domain uncharacterized subfamily 5. gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173803 129 319 + 191 Gaps:64 64.19 229 40.14 1e-13 cd07477 Peptidases_S8_Subtilisin_subset Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin subtilisin Carlsberg serine protease Pb92 subtilisin and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide a propeptide and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92 the serine protease from the alkalophilic Bacillus strain PB92 also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173812 127 466 + 340 Gaps:48 80.68 264 33.33 3e-13 cd07487 Peptidases_S8_1 Peptidase S8 family domain uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173806 122 300 + 179 Gaps:69 56.57 297 30.36 7e-12 cd07480 Peptidases_S8_12 Peptidase S8 family domain uncharacterized subfamily 12. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173801 194 318 + 125 Gaps:12 34.97 346 32.23 1e-11 cd07475 Peptidases_S8_C5a_Peptidase Peptidase S8 family domain in Streptococcal C5a peptidases. Streptococcal C5a peptidase (SCP) is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values.
rpsblast_cdd gnl|CDD|173808 130 300 + 171 Gaps:33 52.38 294 30.52 8e-11 cd07482 Peptidases_S8_Lantibiotic_specific_protease Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases. Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP nsuP mutP and nisP. EpiP from Staphylococcus is thought to cleave matured epidermin. NsuP a dehydratase from Streptococcus and NisP a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile aspartate as an electrophile and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family while glutamic acid has the same role here as the histidine base. However the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds some are intracellular while others are extracellular some function at extreme temperatures and others at high or low pH values.

16 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 13 22 10 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
Pfam 132 510 379 PF00082 none Subtilase family IPR000209
Phobius 28 647 620 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 23 27 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
PRINTS 452 468 17 PR00723 none Subtilisin serine protease family (S8) signature IPR015500
PRINTS 127 146 20 PR00723 none Subtilisin serine protease family (S8) signature IPR015500
PRINTS 190 203 14 PR00723 none Subtilisin serine protease family (S8) signature IPR015500
Phobius 1 12 12 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Gene3D 80 336 257 G3DSA:3.40.50.200 none none IPR000209
Gene3D 401 514 114 G3DSA:3.40.50.200 none none IPR000209
Phobius 1 27 27 SIGNAL_PEPTIDE none Signal peptide region none
ProSitePatterns 453 463 11 PS00138 none Serine proteases, subtilase family, serine active site. IPR023828
SUPERFAMILY 103 327 225 SSF52743 none none IPR000209
SUPERFAMILY 400 514 115 SSF52743 none none IPR000209
PANTHER 12 643 632 PTHR10795:SF335 none none none
PANTHER 12 643 632 PTHR10795 none none IPR015500

1 Localization

Analysis Start End Length
SignalP_EUK 1 27 26

0 Qtllist

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 0.897 0.088 NON-PLANT 27