Protein : Qrob_P0023200.2 Q. robur
Protein Identifier  ? Qrob_P0023200.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=22) PTHR10795:SF335 - SUBTILISIN-LIKE PROTEASE (PTHR10795:SF335) Code Enzyme  EC:3.4.21.25
Gene Prediction Quality  validated Protein length 

Sequence

Length: 260  
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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).

28 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0014s02640g 1 249 + 249 Gaps:5 32.11 760 61.89 9e-99 hypothetical protein
blastp_kegg lcl|tcc:TCM_033805 1 247 + 247 Gaps:5 31.80 761 60.74 2e-96 Subtilisin-like serine protease 2 putative
blastp_kegg lcl|vvi:100248833 1 249 + 249 Gaps:5 33.15 736 58.20 3e-91 subtilisin-like protease-like
blastp_kegg lcl|pmum:103320443 1 252 + 252 Gaps:5 31.63 781 57.49 2e-90 subtilisin-like protease
blastp_kegg lcl|pper:PRUPEppa1027224mg 1 252 + 252 Gaps:5 32.50 760 57.49 2e-90 hypothetical protein
blastp_kegg lcl|cit:102618416 1 249 + 249 Gaps:14 31.31 757 63.29 2e-89 subtilisin-like protease-like
blastp_kegg lcl|fve:101313186 1 252 + 252 Gaps:7 32.54 759 57.89 3e-89 subtilisin-like protease-like
blastp_kegg lcl|cic:CICLE_v10003898mg 1 249 + 249 Gaps:14 31.31 757 63.29 3e-89 hypothetical protein
blastp_kegg lcl|fve:101313482 1 252 + 252 Gaps:6 41.69 590 54.88 3e-85 subtilisin-like protease-like
blastp_kegg lcl|tcc:TCM_033806 1 251 + 251 Gaps:6 32.59 1160 57.14 6e-85 Subtilisin-like serine protease 2 putative
blastp_pdb 3i74_B 3 247 + 245 Gaps:8 37.75 649 44.08 1e-51 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i74_A 3 247 + 245 Gaps:8 37.75 649 44.08 1e-51 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_B 3 247 + 245 Gaps:8 37.75 649 44.08 1e-51 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_A 3 247 + 245 Gaps:8 37.75 649 44.08 1e-51 mol:protein length:649 Subtilisin-like protease
blastp_uniprot_sprot sp|O65351|SUBL_ARATH 1 248 + 248 Gaps:25 32.10 757 40.33 2e-44 Subtilisin-like protease OS Arabidopsis thaliana GN ARA12 PE 1 SV 1
blastp_uniprot_sprot sp|O64495|SDD1_ARATH 24 248 + 225 Gaps:21 29.16 775 37.17 9e-34 Subtilisin-like protease SDD1 OS Arabidopsis thaliana GN SDD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LLL8|XSP1_ARATH 1 247 + 247 Gaps:20 31.64 749 35.86 8e-33 Xylem serine proteinase 1 OS Arabidopsis thaliana GN XSP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q39547|CUCM1_CUCME 1 247 + 247 Gaps:24 31.33 731 36.68 2e-27 Cucumisin OS Cucumis melo PE 1 SV 1
rpsblast_cdd gnl|CDD|173795 2 66 + 65 Gaps:3 20.20 307 56.45 6e-19 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 15 99 + 85 Gaps:10 25.42 295 45.33 4e-15 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|173814 25 99 + 75 Gaps:6 23.40 312 42.47 1e-09 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|173815 23 66 + 44 none 17.32 254 54.55 1e-09 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 14 64 + 51 none 21.16 241 39.22 4e-09 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|173812 17 66 + 50 none 18.94 264 36.00 4e-08 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|173799 24 65 + 42 none 16.22 259 42.86 4e-08 cd07473 Peptidases_S8_Subtilisin_like Peptidase S8 family domain in Subtilisin-like proteins. 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|200986 17 101 + 85 Gaps:12 26.35 277 36.99 8e-08 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.
rpsblast_cdd gnl|CDD|173803 21 64 + 44 none 19.21 229 47.73 1e-07 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|173810 24 65 + 42 Gaps:1 15.77 260 53.66 2e-07 cd07484 Peptidases_S8_Thermitase_like Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. 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.

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 23 106 84 SSF52743 none none IPR000209
Pfam 23 101 79 PF00082 none Subtilase family IPR000209
PANTHER 1 248 248 PTHR10795:SF335 none none none
PANTHER 1 248 248 PTHR10795 none none IPR015500
Gene3D 23 114 92 G3DSA:3.40.50.200 none none IPR000209
ProSitePatterns 30 40 11 PS00138 none Serine proteases, subtilase family, serine active site. IPR023828

0 Localization

5 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_vSeqBC_3P Qrob_Chr10 10 s_1A6CK6_610 v_7092_29 4,28 0 23,27 lod 2,8619 7
Bourran2_2015_nEpis_3P Qrob_Chr12 12 s_1AOES6_1466 s_1B0DDG_1094 28,97 28,55 30,1 lod 3.6 8.4
Bourran2_2014_nFork*_3P Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,28 7,43 41,48 lod 2,4044 5,5
Bourran1_2004_QTL4_peak_Bud_burst_3P Qrob_Chr04 4 s_1AHUWN_1101 s_1BRNG7_1618 30,55 0 47,55 lod 2,8 7,4
Bourran2_2002_QTL10_peak_Bud_burst_A4 Qrob_Chr04 4 s_1B59MJ_737 s_1BGLSD_999 15,86 0 41,66 lod 2,8 4

0 Targeting