Protein : Qrob_P0500140.2 Q. robur
Protein Identifier  ? Qrob_P0500140.2 Organism . Name  Quercus robur
Protein Description  (M=1) PF00610 - Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP) Alias (in v1)  Qrob_P0939260.1
Gene Prediction Quality  manual_v1 Protein length 

Sequence

Length: 645  
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0035556 intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
GO:0009055 electron carrier activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
GO:0015035 protein disulfide oxidoreductase activity Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
GO:0045454 cell redox homeostasis Any process that maintains the redox environment of a cell or compartment within a cell.

22 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa002508mg 6 644 + 639 Gaps:22 98.95 664 69.10 0.0 hypothetical protein
blastp_kegg lcl|pmum:103321036 46 644 + 599 Gaps:19 86.12 706 72.37 0.0 uncharacterized LOC103321036
blastp_kegg lcl|vvi:100263256 9 644 + 636 Gaps:22 90.75 703 68.34 0.0 uncharacterized LOC100263256
blastp_kegg lcl|rcu:RCOM_0814310 45 644 + 600 Gaps:19 91.67 660 71.07 0.0 electron transporter putative
blastp_kegg lcl|mdm:103403432 75 644 + 570 Gaps:19 82.23 709 74.10 0.0 uncharacterized LOC103403432
blastp_kegg lcl|pop:POPTR_0010s10770g 34 644 + 611 Gaps:40 88.21 704 69.57 0.0 POPTRDRAFT_566346 hypothetical protein
blastp_kegg lcl|pxb:103933123 75 644 + 570 Gaps:15 83.24 698 73.32 0.0 uncharacterized LOC103933123
blastp_kegg lcl|pxb:103943172 75 644 + 570 Gaps:15 83.24 698 73.32 0.0 uncharacterized LOC103943172
blastp_kegg lcl|fve:101295807 42 644 + 603 Gaps:22 92.96 653 69.19 0.0 uncharacterized protein LOC101295807
blastp_kegg lcl|mdm:103451481 75 644 + 570 Gaps:15 82.29 706 72.46 0.0 uncharacterized LOC103451481
blastp_pdb 3grx_A 178 257 + 80 none 97.56 82 27.50 5e-06 mol:protein length:82 GLUTAREDOXIN 3
rpsblast_cdd gnl|CDD|191092 441 571 + 131 Gaps:26 99.11 112 41.44 1e-27 pfam04784 DUF547 Protein of unknown function DUF547. Family of uncharacterized proteins from C. elegans and A. thaliana.
rpsblast_cdd gnl|CDD|48576 176 248 + 73 none 100.00 73 64.38 4e-25 cd03027 GRX_DEP Glutaredoxin (GRX) family Dishevelled Egl-10 and Pleckstrin (DEP) subfamily composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547 both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins GRX is involved in many cellular functions..
rpsblast_cdd gnl|CDD|197488 296 367 + 72 Gaps:3 97.40 77 36.00 3e-14 smart00049 DEP Domain found in Dishevelled Egl-10 and Pleckstrin. Domain of unknown function present in signalling proteins that contain PH rasGEF rhoGEF rhoGAP RGS PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94 109-118).
rpsblast_cdd gnl|CDD|201339 299 367 + 69 Gaps:5 100.00 74 35.14 2e-13 pfam00610 DEP Domain found in Dishevelled Egl-10 and Pleckstrin (DEP). The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules including Regulator of G protein Signaling (RGS) proteins and has been implicated in membrane targeting. New findings in yeast however demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR thus placing RGS in close proximity with its substrate G protein alpha subunit.
rpsblast_cdd gnl|CDD|48495 177 246 + 70 none 97.22 72 34.29 7e-13 cd02066 GRX_family Glutaredoxin (GRX) family composed of GRX approximately 10 kDa in size and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX GRX has preference for mixed GSH disulfide substrates in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins GRX is involved in many cellular functions including DNA synthesis signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2 as well as E. coli GRX1 and GRX3 which are members of this family. E. coli GRX2 however is a 24-kDa protein that belongs to the GSH S-transferase (GST) family..
rpsblast_cdd gnl|CDD|80317 288 366 + 79 Gaps:2 100.00 81 33.33 7e-13 cd04371 DEP DEP domain named after Dishevelled Egl-10 and Pleckstrin where this domain was first discovered. The function of this domain is still not clear but it is believed to be important for the membrane association of the signaling proteins in which it is present. New studies show that the DEP domain of Sst2 a yeast RGS protein is necessary and sufficient for receptor interaction..
rpsblast_cdd gnl|CDD|201243 181 237 + 57 none 95.00 60 29.82 4e-11 pfam00462 Glutaredoxin Glutaredoxin.
rpsblast_cdd gnl|CDD|162749 178 254 + 77 none 97.47 79 28.57 4e-09 TIGR02181 GRX_bact Glutaredoxin GrxC family. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides.
rpsblast_cdd gnl|CDD|48633 178 250 + 73 Gaps:1 98.67 75 29.73 3e-08 cd03418 GRX_GRXb_1_3_like Glutaredoxin (GRX) family GRX bacterial class 1 and 3 (b_1_3)-like subfamily composed of bacterial GRXs approximately 10 kDa in size and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX GRX has preference for mixed GSH disulfide substrates in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins GRX is involved in many cellular functions including DNA synthesis signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3 which are members of this subfamily..
rpsblast_cdd gnl|CDD|31039 178 253 + 76 Gaps:2 97.50 80 26.92 3e-08 COG0695 GrxC Glutaredoxin and related proteins [Posttranslational modification protein turnover chaperones].
rpsblast_kog gnl|CDD|36963 181 258 + 78 Gaps:3 77.88 104 27.16 2e-08 KOG1752 KOG1752 KOG1752 Glutaredoxin and related proteins [Posttranslational modification protein turnover chaperones].

13 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
ProSiteProfiles 296 369 74 PS50186 none DEP domain profile. IPR000591
Gene3D 293 394 102 G3DSA:1.10.10.10 none none IPR011991
SUPERFAMILY 175 258 84 SSF52833 none none IPR012336
ProSiteProfiles 166 263 98 PS51354 none Glutaredoxin domain profile. IPR002109
PANTHER 124 643 520 PTHR23054:SF12 none none none
SMART 296 369 74 SM00049 none Domain found in Dishevelled, Egl-10, and Pleckstrin IPR000591
SUPERFAMILY 286 391 106 SSF46785 none none none
Pfam 441 571 131 PF04784 none Protein of unknown function, DUF547 IPR006869
Pfam 300 367 68 PF00610 none Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP) IPR000591
Gene3D 177 258 82 G3DSA:3.40.30.10 none none IPR012336
PANTHER 124 643 520 PTHR23054 none none none
Pfam 180 236 57 PF00462 none Glutaredoxin IPR002109
Coils 28 58 31 Coil none none none

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
Bourran_2000_2002_QTL6_Delta.F Qrob_Chr03 3 s_2HYXJ2_207 s_1AUAXK_317 29.12 6,3 45,37 lod 3.1666 0.026
Bourran2_2014_nLBD_3P Qrob_Chr03 3 s_1ET7H8_604 s_1BYNB5_834 23,73 0 46,72 lod 1,7573 3,8
PM_1999_QTL14_peak_Bud_burst_3P Qrob_Chr03 3 s_2F0SI1_756 v_6056_735 11,78 3,78 50,78 lod 2,5 4,5
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_rEpiBC*_3P Qrob_Chr03 3 s_1A3B3X_1163 s_1DKGMO_450 23,04 4,92 41,12 lod 2,5668 7

0 Targeting