Protein : Qrob_P0133230.2 Q. robur
Protein Identifier  ? Qrob_P0133230.2 Organism . Name  Quercus robur
Score  100.0 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: 371  
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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).

32 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pxb:103946167 1 256 + 256 none 32.78 781 74.61 1e-134 subtilisin-like protease SBT5.3
blastp_kegg lcl|vvi:100243842 1 272 + 272 Gaps:8 36.04 777 71.79 4e-134 subtilisin-like protease
blastp_kegg lcl|mdm:103438630 1 256 + 256 none 32.99 776 75.00 4e-134 subtilisin-like protease
blastp_kegg lcl|mdm:103409241 1 256 + 256 none 32.78 781 73.83 4e-132 subtilisin-like protease
blastp_kegg lcl|fve:101301621 1 254 + 254 none 32.99 770 72.83 1e-129 subtilisin-like protease-like
blastp_kegg lcl|pper:PRUPE_ppa001918mg 1 256 + 256 none 34.55 741 76.17 2e-128 hypothetical protein
blastp_kegg lcl|tcc:TCM_024130 1 256 + 256 none 33.60 762 76.56 6e-128 Subtilisin-like serine endopeptidase family protein
blastp_kegg lcl|pvu:PHAVU_011G190300g 1 256 + 256 none 37.76 678 71.48 4e-127 hypothetical protein
blastp_kegg lcl|pmum:103330892 1 256 + 256 none 33.03 775 75.00 3e-126 subtilisin-like protease
blastp_kegg lcl|cic:CICLE_v10000349mg 1 256 + 256 none 32.86 779 74.22 2e-124 hypothetical protein
blastp_pdb 3i74_B 1 222 + 222 Gaps:5 33.44 649 47.47 2e-53 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i74_A 1 222 + 222 Gaps:5 33.44 649 47.47 2e-53 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_B 1 222 + 222 Gaps:5 33.44 649 47.47 2e-53 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_A 1 222 + 222 Gaps:5 33.44 649 47.47 2e-53 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3afg_B 69 210 + 142 Gaps:20 26.35 539 33.10 2e-10 mol:protein length:539 Subtilisin-like serine protease
blastp_pdb 3afg_A 69 210 + 142 Gaps:20 26.35 539 33.10 2e-10 mol:protein length:539 Subtilisin-like serine protease
blastp_uniprot_sprot sp|O65351|SUBL_ARATH 1 245 + 245 Gaps:3 31.97 757 48.76 2e-66 Subtilisin-like protease OS Arabidopsis thaliana GN ARA12 PE 1 SV 1
blastp_uniprot_sprot sp|Q39547|CUCM1_CUCME 1 244 + 244 Gaps:14 31.46 731 53.48 4e-66 Cucumisin OS Cucumis melo PE 1 SV 1
blastp_uniprot_sprot sp|Q9LLL8|XSP1_ARATH 1 255 + 255 Gaps:13 32.58 749 51.23 6e-60 Xylem serine proteinase 1 OS Arabidopsis thaliana GN XSP1 PE 2 SV 1
blastp_uniprot_sprot sp|O64495|SDD1_ARATH 1 225 + 225 Gaps:12 29.03 775 48.00 4e-59 Subtilisin-like protease SDD1 OS Arabidopsis thaliana GN SDD1 PE 2 SV 1
blastp_uniprot_sprot sp|P29141|SUBV_BACSU 13 189 + 177 Gaps:27 19.11 806 34.42 8e-07 Minor extracellular protease vpr OS Bacillus subtilis (strain 168) GN vpr PE 1 SV 1
blastp_uniprot_sprot sp|O31788|APRX_BACSU 69 201 + 133 Gaps:17 30.77 442 29.41 2e-06 Serine protease AprX OS Bacillus subtilis (strain 168) GN aprX PE 1 SV 1
rpsblast_cdd gnl|CDD|173795 1 204 + 204 Gaps:5 65.47 307 54.23 1e-81 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 1 204 + 204 Gaps:34 59.66 295 37.50 6e-23 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|173812 27 202 + 176 Gaps:33 60.23 264 32.08 3e-18 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|173787 2 205 + 204 Gaps:51 67.63 241 33.74 3e-16 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|173815 70 207 + 138 Gaps:19 48.43 254 33.33 5e-14 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|173801 48 203 + 156 Gaps:30 48.55 346 30.36 7e-14 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|173803 69 185 + 117 Gaps:24 44.98 229 37.86 2e-12 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|200986 72 207 + 136 Gaps:16 48.38 277 26.87 1e-11 pfam00082 Peptidase_S8 Subtilase family. Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet order 2314567.

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 2 239 238 PTHR10795 none none IPR015500
Pfam 2 213 212 PF00082 none Subtilase family IPR000209
SUPERFAMILY 2 30 29 SSF52743 none none IPR000209
SUPERFAMILY 69 208 140 SSF52743 none none IPR000209
Gene3D 2 223 222 G3DSA:3.40.50.200 none none IPR000209
PANTHER 2 239 238 PTHR10795:SF328 none none none

0 Localization

6 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL5_peak_Bud_burst_A4 Qrob_Chr10 10 s_1C8OKQ_688 v_12844_707 25,6 13,9 39,9 lod 2,7 6,1
Bourran2_2002_QTL13_peak_Bud_burst_3P Qrob_Chr10 10 s_1B1AG7_637 s_1A3A1N_709 19,44 0 49,44 lod 3 5,6
Bourran2_2002_QTL15_peak_Bud_burst_A4 Qrob_Chr10 10 v_7579_71 s_1ATZMJ_189 23,94 0 43,64 lod 3,7 5,4
Bourran2_2014_vSeqBC_A4 Qrob_Chr10 10 s_1BAM4E_1326 s_1C0HD0_1012 36,88 7,71 46,03 lod 2,6164 7,3
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5
PM_1999_QTL16_peak_Bud_burst_3P Qrob_Chr10 10 s_1B6YNI_505 s_1A1ZO_1322 7,48 0 31,48 lod 4 7,1

0 Targeting