Protein : Qrob_P0208760.2 Q. robur
Protein Identifier  ? Qrob_P0208760.2 Organism . Name  Quercus robur
Score  82.0 Score Type  egn
Protein Description  (M=4) KOG1030//KOG1327 - Predicted Ca2+-dependent phospholipid-binding protein [General function prediction only]. // Copine [Signal transduction mechanisms]. Gene Prediction Quality  validated
Protein length 

Sequence

Length: 653  
Paste the following link
Lists
This Protein isn't in any lists. Upload a list.

Sequence Feature Displayer

Protein Sequence Displayer

J Browse Displayer

0 Synonyms

3 GO Terms

Identifier Name Description
GO:0005515 protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
GO:0005544 calcium-dependent phospholipid binding Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium.
GO:0060548 negative regulation of cell death Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100241932 1 652 + 652 Gaps:65 99.16 594 78.10 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100263993 1 652 + 652 Gaps:65 99.16 594 78.27 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250185 1 652 + 652 Gaps:65 99.16 594 78.27 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100247065 1 652 + 652 Gaps:65 99.16 594 78.44 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250282 1 652 + 652 Gaps:65 99.16 594 77.93 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100262302 1 652 + 652 Gaps:65 99.16 594 77.76 0.0 protein BONZAI 3-like
blastp_kegg lcl|pmum:103344705 1 652 + 652 Gaps:73 99.83 580 76.17 0.0 protein BONZAI 3
blastp_kegg lcl|pxb:103962883 1 648 + 648 Gaps:65 98.31 593 74.79 0.0 protein BONZAI 3-like
blastp_kegg lcl|pxb:103962886 1 652 + 652 Gaps:65 99.66 589 74.11 0.0 protein BONZAI 3-like
blastp_kegg lcl|mdm:103423573 1 652 + 652 Gaps:66 99.66 590 73.81 0.0 protein BONZAI 3-like
blastp_uniprot_sprot sp|Q5XQC7|BON3_ARATH 1 642 + 642 Gaps:66 98.97 584 70.59 0.0 Protein BONZAI 3 OS Arabidopsis thaliana GN BON3 PE 1 SV 1
blastp_uniprot_sprot sp|Q941L3|BON1_ARATH 1 644 + 644 Gaps:75 99.83 578 63.26 0.0 Protein BONZAI 1 OS Arabidopsis thaliana GN BON1 PE 1 SV 2
blastp_uniprot_sprot sp|Q5S1W2|BON2_ARATH 1 640 + 640 Gaps:11 98.29 586 62.67 0.0 Protein BONZAI 2 OS Arabidopsis thaliana GN BON2 PE 1 SV 2
blastp_uniprot_sprot sp|Q9UBL6|CPNE7_HUMAN 50 642 + 593 Gaps:46 94.63 633 37.23 1e-108 Copine-7 OS Homo sapiens GN CPNE7 PE 2 SV 1
blastp_uniprot_sprot sp|Q9HCH3|CPNE5_HUMAN 53 640 + 588 Gaps:73 91.23 593 40.85 6e-108 Copine-5 OS Homo sapiens GN CPNE5 PE 1 SV 2
blastp_uniprot_sprot sp|Q8JZW4|CPNE5_MOUSE 53 640 + 588 Gaps:73 91.23 593 40.67 6e-107 Copine-5 OS Mus musculus GN Cpne5 PE 2 SV 1
blastp_uniprot_sprot sp|Q8BT60|CPNE3_MOUSE 53 648 + 596 Gaps:90 98.69 533 39.92 2e-99 Copine-3 OS Mus musculus GN Cpne3 PE 2 SV 2
blastp_uniprot_sprot sp|O75131|CPNE3_HUMAN 53 648 + 596 Gaps:90 97.95 537 39.92 4e-99 Copine-3 OS Homo sapiens GN CPNE3 PE 1 SV 1
blastp_uniprot_sprot sp|Q0VE82|CPNE7_MOUSE 50 642 + 593 Gaps:84 94.25 557 39.43 3e-96 Copine-7 OS Mus musculus GN Cpne7 PE 2 SV 1
blastp_uniprot_sprot sp|Q99829|CPNE1_HUMAN 53 647 + 595 Gaps:28 97.39 537 42.26 1e-95 Copine-1 OS Homo sapiens GN CPNE1 PE 1 SV 1
rpsblast_cdd gnl|CDD|29232 378 631 + 254 Gaps:10 99.21 254 52.38 2e-85 cd01459 vWA_copine_like VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However the MIDAS motif is not totally conserved in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding..
rpsblast_cdd gnl|CDD|203562 427 573 + 147 Gaps:3 100.00 146 55.48 4e-55 pfam07002 Copine Copine. This family represents a conserved region approximately 180 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking and may also be involved in cell division and growth.
rpsblast_cdd gnl|CDD|176013 53 379 + 327 Gaps:28 100.00 120 58.33 6e-33 cd04048 C2A_Copine C2 domain first repeat in Copine. There are 2 copies of the C2 domain present in copine a protein involved in membrane trafficking protein-protein interactions and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the first C2 repeat C2A and has a type-I topology.
rpsblast_cdd gnl|CDD|176012 55 357 + 303 Gaps:18 96.36 110 56.60 1e-32 cd04047 C2B_Copine C2 domain second repeat in Copine. There are 2 copies of the C2 domain present in copine a protein involved in membrane trafficking protein-protein interactions and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the second C2 repeat C2B and has a type-I topology.
rpsblast_cdd gnl|CDD|197596 59 357 + 299 Gaps:20 96.04 101 48.45 4e-11 smart00239 C2 Protein kinase C conserved region 2 (CalB). Ca2+-binding motif present in phospholipases protein kinases C and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids inositol polyphosphates and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
rpsblast_cdd gnl|CDD|201052 59 349 + 291 Gaps:18 96.47 85 50.00 1e-10 pfam00168 C2 C2 domain.
rpsblast_cdd gnl|CDD|175973 59 362 + 304 Gaps:22 90.20 102 43.48 2e-09 cd00030 C2 C2 domain. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions.
rpsblast_cdd gnl|CDD|197656 408 590 + 183 Gaps:33 91.43 175 21.88 7e-07 smart00327 VWA von Willebrand factor (vWF) type A domain. VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
rpsblast_kog gnl|CDD|36541 19 644 + 626 Gaps:55 99.62 529 49.53 1e-127 KOG1327 KOG1327 KOG1327 Copine [Signal transduction mechanisms].
rpsblast_kog gnl|CDD|36248 59 152 + 94 Gaps:18 45.24 168 39.47 4e-07 KOG1030 KOG1030 KOG1030 Predicted Ca2+-dependent phospholipid-binding protein [General function prediction only].

18 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
ProSiteProfiles 408 627 220 PS50234 none VWFA domain profile. IPR002035
SUPERFAMILY 59 169 111 SSF49562 none none IPR000008
PANTHER 220 644 425 PTHR10857 none none none
Gene3D 241 356 116 G3DSA:2.60.40.150 none none IPR000008
Gene3D 59 164 106 G3DSA:2.60.40.150 none none IPR000008
PANTHER 1 156 156 PTHR10857:SF24 none none IPR031116
ProSiteProfiles 265 349 85 PS50004 none C2 domain profile. IPR000008
Pfam 265 348 84 PF00168 none C2 domain IPR000008
Pfam 59 151 93 PF00168 none C2 domain IPR000008
ProSiteProfiles 59 152 94 PS50004 none C2 domain profile. IPR000008
SUPERFAMILY 264 357 94 SSF49562 none none IPR000008
SMART 260 364 105 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 54 167 114 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SUPERFAMILY 406 591 186 SSF53300 none none IPR002035
Pfam 427 573 147 PF07002 none Copine IPR010734
PANTHER 220 644 425 PTHR10857:SF24 none none IPR031116
SMART 406 608 203 SM00327 none von Willebrand factor (vWF) type A domain IPR002035
PANTHER 1 156 156 PTHR10857 none none none

0 Localization

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_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
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