Protein : Qrob_P0461280.2 Q. robur
Protein Identifier  ? Qrob_P0461280.2 Organism . Name  Quercus robur
Score  66.1 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: 863  
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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:100250185 1 862 + 862 Gaps:54 99.16 594 78.61 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100263993 1 862 + 862 Gaps:54 99.16 594 78.61 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250282 1 862 + 862 Gaps:54 99.16 594 78.44 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100241932 1 862 + 862 Gaps:54 99.16 594 77.08 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100247065 1 862 + 862 Gaps:54 99.16 594 77.25 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100262302 1 862 + 862 Gaps:54 99.16 594 78.10 0.0 protein BONZAI 3-like
blastp_kegg lcl|rcu:RCOM_1429710 1 856 + 856 Gaps:58 99.66 581 77.20 0.0 copine putative
blastp_kegg lcl|pxb:103962883 1 862 + 862 Gaps:53 98.99 593 75.64 0.0 protein BONZAI 3-like
blastp_kegg lcl|pop:POPTR_0013s03010g 1 857 + 857 Gaps:62 99.83 581 78.28 0.0 POPTRDRAFT_570912 bonzai 3 family protein
blastp_kegg lcl|mdm:103423660 56 862 + 807 Gaps:51 98.16 544 76.40 0.0 protein BONZAI 3-like
blastp_uniprot_sprot sp|Q5XQC7|BON3_ARATH 1 852 + 852 Gaps:54 98.97 584 71.63 0.0 Protein BONZAI 3 OS Arabidopsis thaliana GN BON3 PE 1 SV 1
blastp_uniprot_sprot sp|Q941L3|BON1_ARATH 1 854 + 854 Gaps:75 99.83 578 65.68 0.0 Protein BONZAI 1 OS Arabidopsis thaliana GN BON1 PE 1 SV 2
blastp_uniprot_sprot sp|Q5S1W2|BON2_ARATH 1 850 + 850 Gaps:67 98.29 586 61.98 0.0 Protein BONZAI 2 OS Arabidopsis thaliana GN BON2 PE 1 SV 2
blastp_uniprot_sprot sp|Q99829|CPNE1_HUMAN 53 857 + 805 Gaps:91 97.39 537 42.83 6e-93 Copine-1 OS Homo sapiens GN CPNE1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9DC53|CPNE8_MOUSE 53 851 + 799 Gaps:87 90.47 577 45.02 1e-91 Copine-8 OS Mus musculus GN Cpne8 PE 2 SV 3
blastp_uniprot_sprot sp|Q8IYJ1|CPNE9_HUMAN 53 851 + 799 Gaps:87 94.39 553 44.64 1e-91 Copine-9 OS Homo sapiens GN CPNE9 PE 1 SV 3
blastp_uniprot_sprot sp|Q86YQ8|CPNE8_HUMAN 53 851 + 799 Gaps:87 92.55 564 45.21 2e-91 Copine-8 OS Homo sapiens GN CPNE8 PE 1 SV 2
blastp_uniprot_sprot sp|Q1RLL3|CPNE9_MOUSE 53 851 + 799 Gaps:87 94.39 553 44.25 3e-91 Copine-9 OS Mus musculus GN Cpne9 PE 2 SV 1
blastp_uniprot_sprot sp|Q9UBL6|CPNE7_HUMAN 50 855 + 806 Gaps:92 95.10 633 39.87 3e-91 Copine-7 OS Homo sapiens GN CPNE7 PE 2 SV 1
blastp_uniprot_sprot sp|Q5BJS7|CPNE9_RAT 53 851 + 799 Gaps:87 94.39 553 44.25 3e-91 Copine-9 OS Rattus norvegicus GN Cpne9 PE 2 SV 1
rpsblast_cdd gnl|CDD|29232 366 841 + 476 Gaps:11 99.21 254 52.38 8e-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 637 783 + 147 Gaps:3 100.00 146 54.79 2e-54 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 55 567 + 513 Gaps:20 89.09 110 58.16 7e-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 53 589 + 537 Gaps:48 100.00 120 58.33 9e-32 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 59 559 + 501 Gaps:22 96.47 85 48.78 2e-10 pfam00168 C2 C2 domain.
rpsblast_cdd gnl|CDD|197596 59 567 + 509 Gaps:27 96.04 101 47.42 2e-09 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 59 572 + 514 Gaps:28 95.10 102 41.24 4e-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 52 856 + 805 Gaps:109 100.00 529 48.20 1e-126 KOG1327 KOG1327 KOG1327 Copine [Signal transduction mechanisms].
rpsblast_kog gnl|CDD|36248 59 152 + 94 Gaps:18 45.24 168 38.16 7e-07 KOG1030 KOG1030 KOG1030 Predicted Ca2+-dependent phospholipid-binding protein [General function prediction only].

22 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 59 169 111 G3DSA:2.60.40.150 none none IPR000008
PANTHER 1 156 156 PTHR10857:SF24 none none IPR031116
SMART 470 574 105 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 54 167 114 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 248 352 105 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SUPERFAMILY 252 345 94 SSF49562 none none IPR000008
PANTHER 430 854 425 PTHR10857:SF24 none none IPR031116
Pfam 637 783 147 PF07002 none Copine IPR010734
ProSiteProfiles 59 152 94 PS50004 none C2 domain profile. IPR000008
Pfam 253 336 84 PF00168 none C2 domain IPR000008
Pfam 475 558 84 PF00168 none C2 domain IPR000008
Pfam 59 151 93 PF00168 none C2 domain IPR000008
SUPERFAMILY 474 567 94 SSF49562 none none IPR000008
ProSiteProfiles 475 559 85 PS50004 none C2 domain profile. IPR000008
Gene3D 225 344 120 G3DSA:2.60.40.150 none none IPR000008
Gene3D 447 566 120 G3DSA:2.60.40.150 none none IPR000008
SUPERFAMILY 58 167 110 SSF49562 none none IPR000008
PANTHER 1 156 156 PTHR10857 none none none
PANTHER 430 854 425 PTHR10857 none none none
ProSiteProfiles 253 337 85 PS50004 none C2 domain profile. IPR000008
SMART 616 818 203 SM00327 none von Willebrand factor (vWF) type A domain IPR002035
SUPERFAMILY 616 801 186 SSF53300 none none IPR002035

0 Localization

2 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_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

0 Targeting