Protein : Qrob_P0255590.2 Q. robur
Protein Identifier  ? Qrob_P0255590.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=4) 2.7.9.5 - Phosphoglucan, water dikinase. Code Enzyme  EC:2.7.9.5
Gene Prediction Quality  validated Protein length 

Sequence

Length: 279  
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0030246 carbohydrate binding Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
GO:2001070 starch binding Interacting selectively and non-covalently with starch.

27 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100256560 1 273 + 273 Gaps:14 22.14 1188 62.36 1e-90 phosphoglucan water dikinase chloroplastic-like
blastp_kegg lcl|pop:POPTR_0002s23550g 1 273 + 273 Gaps:10 23.11 1138 61.60 1e-89 POPTRDRAFT_645328 hypothetical protein
blastp_kegg lcl|rcu:RCOM_1305250 1 273 + 273 Gaps:15 21.98 1174 60.85 4e-88 chloroplast alpha-glucan water dikinase putative (EC:2.7.9.5)
blastp_kegg lcl|tcc:TCM_020150 1 273 + 273 Gaps:19 22.03 1180 63.46 7e-85 Catalytics carbohydrate kinases phosphoglucan
blastp_kegg lcl|pop:POPTR_0014s14510g 1 273 + 273 Gaps:34 22.17 1159 60.70 8e-85 POPTRDRAFT_664666 hypothetical protein
blastp_kegg lcl|pmum:103322572 1 273 + 273 Gaps:25 22.52 1190 61.57 1e-83 phosphoglucan water dikinase chloroplastic
blastp_kegg lcl|pper:PRUPE_ppa000429mg 1 273 + 273 Gaps:24 22.59 1191 60.59 3e-82 hypothetical protein
blastp_kegg lcl|cic:CICLE_v10004968mg 1 273 + 273 Gaps:30 73.94 353 60.92 3e-82 hypothetical protein
blastp_kegg lcl|cit:102621268 1 273 + 273 Gaps:28 22.10 1190 60.46 4e-79 phosphoglucan water dikinase chloroplastic-like
blastp_kegg lcl|pxb:103960380 1 273 + 273 Gaps:26 22.19 1185 57.03 9e-79 phosphoglucan water dikinase chloroplastic
blastp_pdb 1kum_A 86 167 + 82 Gaps:7 82.41 108 30.34 2e-07 mol:protein length:108 GLUCOAMYLASE
blastp_pdb 1kul_A 86 167 + 82 Gaps:7 82.41 108 30.34 2e-07 mol:protein length:108 GLUCOAMYLASE
blastp_pdb 1acz_A 86 167 + 82 Gaps:7 82.41 108 30.34 2e-07 mol:protein length:108 GLUCOAMYLASE
blastp_pdb 1ac0_A 86 167 + 82 Gaps:7 82.41 108 30.34 2e-07 mol:protein length:108 GLUCOAMYLASE
blastp_pdb 2vn7_A 97 175 + 79 Gaps:7 14.36 599 31.40 5e-07 mol:protein length:599 GLUCOAMYLASE
blastp_pdb 2vn4_A 97 175 + 79 Gaps:7 14.36 599 31.40 5e-07 mol:protein length:599 GLUCOAMYLASE
blastp_uniprot_sprot sp|Q6ZY51|PWD_ARATH 30 273 + 244 Gaps:31 21.32 1196 49.41 9e-67 Phosphoglucan water dikinase chloroplastic OS Arabidopsis thaliana GN GWD3 PE 1 SV 1
blastp_uniprot_sprot sp|Q2QTC2|PWD_ORYSJ 57 273 + 217 Gaps:22 18.99 1206 51.53 3e-60 Phosphoglucan water dikinase chloroplastic OS Oryza sativa subsp. japonica GN GWD3 PE 3 SV 2
blastp_uniprot_sprot sp|P23176|AMYG_ASPKA 85 167 + 83 Gaps:7 14.08 639 31.11 1e-05 Glucoamylase I OS Aspergillus kawachii GN gaI PE 1 SV 1
blastp_uniprot_sprot sp|P22832|AMYG_ASPSH 85 167 + 83 Gaps:7 14.08 639 31.11 1e-05 Glucoamylase OS Aspergillus shirousami GN glaA PE 3 SV 1
rpsblast_cdd gnl|CDD|99892 85 176 + 92 none 100.00 92 73.91 5e-41 cd05818 CBM20_water_dikinase Phosphoglucan water dikinase (also known as alpha-glucan water dikinase) N-terminal CBM20 (carbohydrate-binding module family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch..
rpsblast_cdd gnl|CDD|189668 86 168 + 83 Gaps:8 90.62 96 31.03 3e-15 pfam00686 CBM_20 Starch binding domain.
rpsblast_cdd gnl|CDD|119437 85 176 + 92 Gaps:8 100.00 96 36.46 3e-15 cd05467 CBM20 The family 20 carbohydrate-binding module (CBM20) also known as the starch-binding domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch..
rpsblast_cdd gnl|CDD|198133 85 166 + 82 Gaps:7 98.86 88 37.93 8e-13 smart01065 CBM_2 Starch binding domain.
rpsblast_cdd gnl|CDD|99886 86 167 + 82 Gaps:9 82.08 106 34.48 2e-10 cd05811 CBM20_glucoamylase Glucoamylase (glucan1 4-alpha-glucosidase) C-terminal CBM20 (carbohydrate-binding module family 20) domain. Glucoamylases are inverting exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1 4-glycosidic bonds but also have some activity towards 1 6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain a C-terminal CBM20 domain and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch..
rpsblast_cdd gnl|CDD|99883 98 170 + 73 Gaps:3 80.00 95 31.58 6e-07 cd05808 CBM20_alpha_amylase Alpha-amylase C-terminal CBM20 (carbohydrate-binding module family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have in addition to the C-terminal CBM20 domain an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 which hydrolyzes internal alpha-1 4-glucosidic bonds in starch and related saccharides yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch..
rpsblast_cdd gnl|CDD|99891 95 162 + 68 Gaps:5 73.00 100 31.51 8e-07 cd05817 CBM20_DSP Dual-specificity phosphatase (DSP) N-terminal CBM20 (carbohydrate-binding module family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch..

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
ProSiteProfiles 78 178 101 PS51166 none CBM20 (carbohydrate binding type-20) domain profile. IPR002044
SMART 85 174 90 SM01065 none Starch binding domain IPR002044
PANTHER 86 173 88 PTHR15048 none none none
PANTHER 86 173 88 PTHR15048:SF0 none none none
Gene3D 85 177 93 G3DSA:2.60.40.10 none none IPR013783
Pfam 86 169 84 PF00686 none Starch binding domain IPR002044
SUPERFAMILY 85 177 93 SSF49452 none none IPR013784

0 Localization

16 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
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_2002_QTL11_peak_Bud_burst_A4 Qrob_Chr06 6 s_1C41PA_791 s_1AM1AV_1141 19,17 0 34,57 lod 2,3 2,9
Bourran2_2014_aSeqBC_3P Qrob_Chr06 6 v_506_189 v_686_77 30,72 13,58 43,48 lod 2,2746 6,3
Bourran2_2014_aSeqBC*_A4 Qrob_Chr06 6 s_2F5MK3_712 v_444_355 27,13 14,86 39,46 lod 3,7847 9,8
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_nEpis*_A4 Qrob_Chr07 7 v_12400_446 s_1BPEBU_1211 6,93 0 15,13 lod 4,7411 11
Bourran2_2014_nFork*_3P Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,28 7,43 41,48 lod 2,4044 5,5
Bourran2_2014_nLBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,41 9,8 50,1 lod 1,9524 4,1
Bourran2_2014_nPriBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,51 3,36 51,86 lod 1,6747 3,9
Bourran2_2014_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5
Bourran2_2014_vEpiBC_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,55 14,41 50,01 lod 1,7882 4,8
Champenoux_2015_nEpis_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,53 25,47 27,72 lod 4.4 8.9
Champenoux_2015_nP_3P Qrob_Chr06 6 s_1A386O_228 s_1AYZFS_603 27,03 26,47 27,34 lod 2.8 7.2

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 10   Mitochondrion 3 0.016 0.828 NON-PLANT 10