Protein : Qrob_P0138730.2 Q. robur

Protein Identifier  ? Qrob_P0138730.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=1) PTHR31080:SF1 - CELL WALL / VACUOLAR INHIBITOR OF FRUCTOSIDASE 2-RELATED (PTHR31080:SF1) Code Enzyme  EC:3.1.1.11
Gene Prediction Quality  validated Protein length 

Sequence

Length: 184  

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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0030599 pectinesterase activity Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
GO:0004857 enzyme inhibitor activity Binds to and stops, prevents or reduces the activity of an enzyme.

18 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa021753mg 1 183 + 183 Gaps:6 100.00 181 78.45 2e-93 hypothetical protein
blastp_kegg lcl|pmum:103334312 1 183 + 183 Gaps:10 100.00 181 78.45 1e-92 cell wall / vacuolar inhibitor of fructosidase 2-like
blastp_kegg lcl|mdm:103449338 3 183 + 181 Gaps:6 98.35 182 74.30 2e-84 cell wall / vacuolar inhibitor of fructosidase 2
blastp_kegg lcl|mdm:103422929 1 182 + 182 Gaps:5 81.53 222 77.90 2e-82 cell wall / vacuolar inhibitor of fructosidase 2-like
blastp_kegg lcl|pxb:103937439 3 182 + 180 Gaps:4 97.80 182 76.40 3e-81 cell wall / vacuolar inhibitor of fructosidase 2-like
blastp_kegg lcl|pxb:103937431 3 182 + 180 Gaps:4 97.80 182 76.40 3e-81 cell wall / vacuolar inhibitor of fructosidase 2-like
blastp_kegg lcl|pop:POPTR_0007s03920g 1 182 + 182 Gaps:1 69.58 263 71.04 4e-81 POPTRDRAFT_764002 hypothetical protein
blastp_kegg lcl|tcc:TCM_001440 1 183 + 183 Gaps:8 73.84 237 68.57 2e-80 Cell wall / vacuolar inhibitor of fructosidase 2
blastp_kegg lcl|fve:101300097 18 183 + 166 none 90.22 184 70.48 9e-80 cell wall / vacuolar inhibitor of fructosidase 2-like
blastp_kegg lcl|cic:CICLE_v10002604mg 1 179 + 179 Gaps:3 96.77 186 75.00 2e-79 hypothetical protein
blastp_pdb 1xg2_B 30 181 + 152 Gaps:3 97.39 153 30.20 4e-14 mol:protein length:153 Pectinesterase inhibitor
blastp_uniprot_sprot sp|O49603|CVIF2_ARATH 1 181 + 181 Gaps:9 98.89 180 50.56 7e-60 Cell wall / vacuolar inhibitor of fructosidase 2 OS Arabidopsis thaliana GN C/VIF2 PE 1 SV 1
blastp_uniprot_sprot sp|P83326|PMEI_ACTDE 27 181 + 155 Gaps:3 82.16 185 30.92 1e-14 Pectinesterase inhibitor OS Actinidia deliciosa GN PMEI PE 1 SV 2
blastp_uniprot_sprot sp|Q8GT41|PLA1_PLAAC 11 182 + 172 Gaps:16 99.44 179 24.72 1e-12 Putative invertase inhibitor OS Platanus acerifolia PE 1 SV 1
blastp_uniprot_sprot sp|Q9LUV1|PMEI2_ARATH 34 181 + 148 Gaps:12 83.24 173 27.78 1e-06 Pectinesterase inhibitor 2 OS Arabidopsis thaliana GN PMEI2 PE 1 SV 1
rpsblast_cdd gnl|CDD|162447 5 181 + 177 Gaps:5 96.63 178 31.98 3e-34 TIGR01614 PME_inhib pectinesterase inhibitor domain. This model describes a plant domain of about 200 amino acids characterized by four conserved Cys residues shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this HMM followed immediately by a pectinesterase domain pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family.
rpsblast_cdd gnl|CDD|202862 32 177 + 146 Gaps:2 99.31 145 32.64 1e-21 pfam04043 PMEI Plant invertase/pectin methylesterase inhibitor. This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences (personal obs:C Yeats) suggesting that both PMEs and their inhibitor are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
rpsblast_cdd gnl|CDD|197924 28 177 + 150 Gaps:2 100.00 148 31.08 1e-21 smart00856 PMEI Plant invertase/pectin methylesterase inhibitor. This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 32 181 150 PTHR31080:SF1 none none none
Phobius 17 183 167 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
PANTHER 32 181 150 PTHR31080 none none none
SMART 29 177 149 SM00856 "KEGG:00040+3.1.1.11","KEGG:00500+3.1.1.11","MetaCyc:PWY-1081","MetaCyc:PWY-7246","MetaCyc:PWY-7248","UniPathway:UPA00545" Plant invertase/pectin methylesterase inhibitor IPR006501
Gene3D 29 181 153 G3DSA:1.20.140.40 "KEGG:00040+3.1.1.11","KEGG:00500+3.1.1.11","MetaCyc:PWY-1081","MetaCyc:PWY-7246","MetaCyc:PWY-7248","UniPathway:UPA00545" none IPR006501
Pfam 30 175 146 PF04043 "KEGG:00040+3.1.1.11","KEGG:00500+3.1.1.11","MetaCyc:PWY-1081","MetaCyc:PWY-7246","MetaCyc:PWY-7248","UniPathway:UPA00545" Plant invertase/pectin methylesterase inhibitor IPR006501
TIGRFAM 4 180 177 TIGR01614 "KEGG:00040+3.1.1.11","KEGG:00500+3.1.1.11","MetaCyc:PWY-1081","MetaCyc:PWY-7246","MetaCyc:PWY-7248","UniPathway:UPA00545" PME_inhib: pectinesterase inhibitor domain IPR006501
Phobius 1 16 16 SIGNAL_PEPTIDE none Signal peptide region none
SUPERFAMILY 31 181 151 SSF101148 "KEGG:00040+3.1.1.11","KEGG:00500+3.1.1.11","MetaCyc:PWY-1081","MetaCyc:PWY-7246","MetaCyc:PWY-7248","UniPathway:UPA00545" none IPR006501
Phobius 4 11 8 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
Phobius 12 16 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Phobius 1 3 3 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none

1 Localization

Analysis Start End Length
SignalP_EUK 1 21 20

7 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_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2014_nLBD*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,25 0 35,55 lod 2,5951 6
Bourran2_2014_nP*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,19 0 31,97 lod 2,8472 6
Bourran2_2014_nPriLBD_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,36 0 30,43 lod 2,5806 5,1
Bourran2_2014_nEpis*_3P Qrob_Chr08 8 s_1DA4QW_688 s_1DNI7D_820 17,96 0 37,75 lod 2,9745 7,5
Bourran2_2014_nPriBD_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 5,54 0,4 20,6 lod 2,6345 5,9

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 21   Secretory pathway 1 0.975 0.017 NON-PLANT 21