Protein : Qrob_P0023150.2 Q. robur
Protein Identifier  ? Qrob_P0023150.2 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: 431  
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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).

20 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0014s02640g 1 430 + 430 Gaps:96 67.63 760 50.78 8e-160 hypothetical protein
blastp_kegg lcl|vvi:100248833 1 428 + 428 Gaps:93 69.43 736 51.86 2e-158 subtilisin-like protease-like
blastp_kegg lcl|pmum:103320443 1 430 + 430 Gaps:91 65.94 781 47.57 4e-148 subtilisin-like protease
blastp_kegg lcl|fve:101313186 1 430 + 430 Gaps:94 67.72 759 48.05 9e-147 subtilisin-like protease-like
blastp_kegg lcl|pper:PRUPEppa1027224mg 1 430 + 430 Gaps:91 67.76 760 47.57 2e-146 hypothetical protein
blastp_kegg lcl|tcc:TCM_033805 1 425 + 425 Gaps:96 66.36 761 47.33 3e-145 Subtilisin-like serine protease 2 putative
blastp_kegg lcl|cic:CICLE_v10003898mg 1 428 + 428 Gaps:99 66.71 757 47.92 8e-141 hypothetical protein
blastp_kegg lcl|cit:102618416 1 428 + 428 Gaps:107 66.71 757 48.12 4e-139 subtilisin-like protease-like
blastp_kegg lcl|pper:PRUPE_ppa023578mg 1 429 + 429 Gaps:79 70.14 710 45.98 4e-129 hypothetical protein
blastp_kegg lcl|fve:101313482 1 429 + 429 Gaps:92 84.92 590 45.91 2e-126 subtilisin-like protease-like
blastp_pdb 3i74_B 1 427 + 427 Gaps:110 78.74 649 33.86 9e-63 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i74_A 1 427 + 427 Gaps:110 78.74 649 33.86 9e-63 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_B 1 427 + 427 Gaps:110 78.74 649 33.86 9e-63 mol:protein length:649 Subtilisin-like protease
blastp_pdb 3i6s_A 1 427 + 427 Gaps:110 78.74 649 33.86 9e-63 mol:protein length:649 Subtilisin-like protease
blastp_uniprot_sprot sp|O65351|SUBL_ARATH 1 425 + 425 Gaps:109 67.64 757 31.45 8e-63 Subtilisin-like protease OS Arabidopsis thaliana GN ARA12 PE 1 SV 1
blastp_uniprot_sprot sp|O64495|SDD1_ARATH 1 425 + 425 Gaps:113 66.84 775 31.47 2e-57 Subtilisin-like protease SDD1 OS Arabidopsis thaliana GN SDD1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LLL8|XSP1_ARATH 3 425 + 423 Gaps:128 66.89 749 31.34 8e-41 Xylem serine proteinase 1 OS Arabidopsis thaliana GN XSP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q39547|CUCM1_CUCME 3 425 + 423 Gaps:118 67.17 731 29.94 2e-37 Cucumisin OS Cucumis melo PE 1 SV 1
rpsblast_cdd gnl|CDD|173795 1 100 + 100 Gaps:2 31.92 307 50.00 1e-30 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 1 108 + 108 Gaps:5 36.27 295 33.64 1e-08 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.

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 1 425 425 PTHR10795 none none IPR015500
PANTHER 1 425 425 PTHR10795:SF335 none none none
SUPERFAMILY 220 311 92 SSF52743 none none IPR000209
SUPERFAMILY 1 116 116 SSF52743 none none IPR000209
Gene3D 216 252 37 G3DSA:3.40.50.200 none none IPR000209
Gene3D 1 110 110 G3DSA:3.40.50.200 none none IPR000209
Pfam 2 251 250 PF00082 none Subtilase family IPR000209

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

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 23   Secretory pathway 2 0.803 0.038 NON-PLANT 23