Protein : Qrob_P0354900.2 Q. robur
Protein Identifier  ? Qrob_P0354900.2 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: 639  
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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.

29 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100262302 1 632 + 632 Gaps:47 98.82 594 74.79 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100263993 1 632 + 632 Gaps:47 98.82 594 74.96 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250185 1 632 + 632 Gaps:47 98.82 594 74.96 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250282 1 632 + 632 Gaps:47 98.82 594 74.62 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100241932 1 632 + 632 Gaps:81 98.82 594 74.96 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100247065 1 632 + 632 Gaps:81 98.82 594 74.96 0.0 protein BONZAI 3-like
blastp_kegg lcl|rcu:RCOM_1429710 1 629 + 629 Gaps:57 99.83 581 73.45 0.0 copine putative
blastp_kegg lcl|pxb:103962886 1 631 + 631 Gaps:53 99.15 589 71.92 0.0 protein BONZAI 3-like
blastp_kegg lcl|gmx:100818746 1 628 + 628 Gaps:48 98.32 594 73.29 0.0 protein BONZAI 3-like
blastp_kegg lcl|pop:POPTR_0013s03010g 1 630 + 630 Gaps:53 100.00 581 74.35 0.0 POPTRDRAFT_570912 bonzai 3 family protein
blastp_uniprot_sprot sp|Q5XQC7|BON3_ARATH 1 624 + 624 Gaps:54 98.97 584 66.96 0.0 Protein BONZAI 3 OS Arabidopsis thaliana GN BON3 PE 1 SV 1
blastp_uniprot_sprot sp|Q941L3|BON1_ARATH 1 626 + 626 Gaps:57 99.83 578 62.05 0.0 Protein BONZAI 1 OS Arabidopsis thaliana GN BON1 PE 1 SV 2
blastp_uniprot_sprot sp|Q5S1W2|BON2_ARATH 1 622 + 622 Gaps:60 98.29 586 60.07 0.0 Protein BONZAI 2 OS Arabidopsis thaliana GN BON2 PE 1 SV 2
blastp_uniprot_sprot sp|Q9UBL6|CPNE7_HUMAN 49 627 + 579 Gaps:49 95.10 633 36.54 1e-105 Copine-7 OS Homo sapiens GN CPNE7 PE 2 SV 1
blastp_uniprot_sprot sp|Q8IYJ1|CPNE9_HUMAN 52 623 + 572 Gaps:76 94.39 553 41.76 1e-105 Copine-9 OS Homo sapiens GN CPNE9 PE 1 SV 3
blastp_uniprot_sprot sp|Q96FN4|CPNE2_HUMAN 48 625 + 578 Gaps:74 95.62 548 41.41 2e-105 Copine-2 OS Homo sapiens GN CPNE2 PE 1 SV 3
blastp_uniprot_sprot sp|Q86YQ8|CPNE8_HUMAN 52 623 + 572 Gaps:76 92.55 564 43.68 2e-104 Copine-8 OS Homo sapiens GN CPNE8 PE 1 SV 2
blastp_uniprot_sprot sp|Q1RLL3|CPNE9_MOUSE 52 623 + 572 Gaps:76 94.39 553 41.38 2e-104 Copine-9 OS Mus musculus GN Cpne9 PE 2 SV 1
blastp_uniprot_sprot sp|Q5BJS7|CPNE9_RAT 52 623 + 572 Gaps:76 94.39 553 41.38 3e-104 Copine-9 OS Rattus norvegicus GN Cpne9 PE 2 SV 1
blastp_uniprot_sprot sp|P59108|CPNE2_MOUSE 46 625 + 580 Gaps:74 95.99 548 42.21 9e-104 Copine-2 OS Mus musculus GN Cpne2 PE 2 SV 1
rpsblast_cdd gnl|CDD|29232 360 613 + 254 Gaps:10 99.21 254 51.59 1e-84 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 409 555 + 147 Gaps:3 100.00 146 54.79 1e-53 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|176012 244 339 + 96 Gaps:2 89.09 110 44.90 2e-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|176013 52 361 + 310 Gaps:31 100.00 120 53.33 8e-27 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|201052 58 331 + 274 Gaps:13 96.47 85 46.34 1e-10 pfam00168 C2 C2 domain.
rpsblast_cdd gnl|CDD|197596 58 339 + 282 Gaps:23 96.04 101 49.48 9e-10 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|175973 58 344 + 287 Gaps:17 90.20 102 42.39 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_kog gnl|CDD|36541 62 628 + 567 Gaps:88 100.00 529 43.86 1e-135 KOG1327 KOG1327 KOG1327 Copine [Signal transduction mechanisms].
rpsblast_kog gnl|CDD|36248 58 134 + 77 Gaps:13 45.24 168 35.53 8e-07 KOG1030 KOG1030 KOG1030 Predicted Ca2+-dependent phospholipid-binding protein [General function prediction only].

17 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 409 555 147 PF07002 none Copine IPR010734
SUPERFAMILY 58 151 94 SSF49562 none none IPR000008
ProSiteProfiles 247 331 85 PS50004 none C2 domain profile. IPR000008
PANTHER 1 138 138 PTHR10857:SF24 none none IPR031116
PANTHER 202 638 437 PTHR10857:SF24 none none IPR031116
Pfam 58 131 74 PF00168 none C2 domain IPR000008
Pfam 247 330 84 PF00168 none C2 domain IPR000008
Gene3D 58 145 88 G3DSA:2.60.40.150 none none IPR000008
Gene3D 219 339 121 G3DSA:2.60.40.150 none none IPR000008
SUPERFAMILY 246 339 94 SSF49562 none none IPR000008
SUPERFAMILY 388 572 185 SSF53300 none none IPR002035
SMART 53 149 97 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 242 346 105 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 388 585 198 SM00327 none von Willebrand factor (vWF) type A domain IPR002035
PANTHER 1 138 138 PTHR10857 none none none
PANTHER 202 638 437 PTHR10857 none none none
ProSiteProfiles 58 134 77 PS50004 none C2 domain profile. IPR000008

0 Localization

6 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_rEpiBC*_3P Qrob_Chr03 3 s_1A3B3X_1163 s_1DKGMO_450 23,04 4,92 41,12 lod 2,5668 7

0 Targeting