Protein : Qrob_P0027220.2 Q. robur
Protein Identifier  ? Qrob_P0027220.2 Organism . Name  Quercus robur
Score  15.0 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: 622  
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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.

31 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100250282 1 621 + 621 Gaps:42 99.16 594 79.46 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100263993 1 621 + 621 Gaps:42 99.16 594 79.29 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250185 1 621 + 621 Gaps:42 99.16 594 79.29 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100262302 1 621 + 621 Gaps:42 99.16 594 79.12 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100241932 1 621 + 621 Gaps:42 99.16 594 79.12 0.0 protein BONZAI 3-like
blastp_kegg lcl|pxb:103962883 1 617 + 617 Gaps:40 98.31 593 77.36 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100247065 1 621 + 621 Gaps:42 99.16 594 78.27 0.0 protein BONZAI 3-like
blastp_kegg lcl|rcu:RCOM_1429710 1 616 + 616 Gaps:40 99.83 581 78.45 0.0 copine putative
blastp_kegg lcl|pmum:103344705 1 621 + 621 Gaps:42 99.83 580 77.72 0.0 protein BONZAI 3
blastp_kegg lcl|mdm:103423573 1 621 + 621 Gaps:41 99.66 590 76.02 0.0 protein BONZAI 3-like
blastp_uniprot_sprot sp|Q5XQC7|BON3_ARATH 1 611 + 611 Gaps:43 98.97 584 73.01 0.0 Protein BONZAI 3 OS Arabidopsis thaliana GN BON3 PE 1 SV 1
blastp_uniprot_sprot sp|Q941L3|BON1_ARATH 1 613 + 613 Gaps:40 99.83 578 64.47 0.0 Protein BONZAI 1 OS Arabidopsis thaliana GN BON1 PE 1 SV 2
blastp_uniprot_sprot sp|Q5S1W2|BON2_ARATH 1 609 + 609 Gaps:47 98.29 586 61.81 0.0 Protein BONZAI 2 OS Arabidopsis thaliana GN BON2 PE 1 SV 2
blastp_uniprot_sprot sp|Q99829|CPNE1_HUMAN 48 614 + 567 Gaps:74 96.65 537 43.55 6e-117 Copine-1 OS Homo sapiens GN CPNE1 PE 1 SV 1
blastp_uniprot_sprot sp|O75131|CPNE3_HUMAN 48 611 + 564 Gaps:72 96.83 537 43.08 1e-115 Copine-3 OS Homo sapiens GN CPNE3 PE 1 SV 1
blastp_uniprot_sprot sp|Q8BT60|CPNE3_MOUSE 48 611 + 564 Gaps:74 97.56 533 43.08 3e-115 Copine-3 OS Mus musculus GN Cpne3 PE 2 SV 2
blastp_uniprot_sprot sp|Q9DC53|CPNE8_MOUSE 48 610 + 563 Gaps:69 90.47 577 43.87 3e-115 Copine-8 OS Mus musculus GN Cpne8 PE 2 SV 3
blastp_uniprot_sprot sp|Q86YQ8|CPNE8_HUMAN 48 610 + 563 Gaps:69 92.55 564 43.68 1e-114 Copine-8 OS Homo sapiens GN CPNE8 PE 1 SV 2
blastp_uniprot_sprot sp|Q5RAE1|CPNE3_PONAB 48 611 + 564 Gaps:72 96.83 537 42.50 1e-112 Copine-3 OS Pongo abelii GN CPNE3 PE 2 SV 1
blastp_uniprot_sprot sp|Q8IYJ1|CPNE9_HUMAN 48 610 + 563 Gaps:65 94.39 553 43.10 2e-111 Copine-9 OS Homo sapiens GN CPNE9 PE 1 SV 3
rpsblast_cdd gnl|CDD|29232 310 600 + 291 Gaps:47 99.21 254 52.78 6e-79 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 359 542 + 184 Gaps:40 100.00 146 55.48 2e-48 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 48 245 + 198 Gaps:9 98.33 120 56.78 3e-36 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 50 289 + 240 Gaps:18 96.36 110 52.83 1e-31 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|201052 54 281 + 228 Gaps:18 96.47 85 46.34 3e-11 pfam00168 C2 C2 domain.
rpsblast_cdd gnl|CDD|197596 54 289 + 236 Gaps:20 93.07 101 45.74 1e-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 54 294 + 241 Gaps:33 96.08 102 45.92 1e-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|176005 54 302 + 249 Gaps:30 97.39 115 42.86 2e-07 cd04040 C2D_Tricalbin-like C2 domain fourth repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin a yeast homolog of Synaptotagmin which is involved in membrane trafficking and sorting. 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 fifth C2 repeat C2E and has a type-II topology.
rpsblast_cdd gnl|CDD|176007 57 166 + 110 Gaps:19 76.86 121 36.56 5e-07 cd04042 C2A_MCTP_PRT C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP). MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence three C2 domains two transmembrane regions (TMRs) and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region the others being synaptotagmins extended synaptotagmins and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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-II topology.
rpsblast_kog gnl|CDD|36541 58 615 + 558 Gaps:79 100.00 529 45.94 1e-144 KOG1327 KOG1327 KOG1327 Copine [Signal transduction mechanisms].

18 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 197 280 84 PF00168 none C2 domain IPR000008
Pfam 54 146 93 PF00168 none C2 domain IPR000008
PANTHER 518 613 96 PTHR10857:SF24 none none IPR031116
PANTHER 1 481 481 PTHR10857 none none none
PANTHER 518 613 96 PTHR10857 none none none
Gene3D 176 289 114 G3DSA:2.60.40.150 none none IPR000008
Gene3D 54 166 113 G3DSA:2.60.40.150 none none IPR000008
SUPERFAMILY 197 290 94 SSF49562 none none IPR000008
SUPERFAMILY 338 475 138 SSF53300 none none IPR002035
PANTHER 1 481 481 PTHR10857:SF24 none none IPR031116
SMART 338 577 240 SM00327 none von Willebrand factor (vWF) type A domain IPR002035
SMART 49 162 114 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 192 296 105 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
ProSiteProfiles 197 281 85 PS50004 none C2 domain profile. IPR000008
Pfam 511 542 32 PF07002 none Copine IPR010734
Pfam 359 475 117 PF07002 none Copine IPR010734
ProSiteProfiles 54 147 94 PS50004 none C2 domain profile. IPR000008
SUPERFAMILY 54 167 114 SSF49562 none none IPR000008

0 Localization

8 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_QTL7_Delta.F Qrob_Chr09 9 v_5944_442 s_1BA1PC_866 23.51 10,96 35,74 lod 4.1466 0.041
Bourran2_2003_QTL11_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 4,16 48,16 lod 2,3 5,1
Bourran2_2004_QTL12_peak_Bud_burst_3P Qrob_Chr09 9 s_1BDO6G_250 s_1A83AM_496 34,31 9,31 44,31 lod 3,6 7,6
Bourran2_2004_QTL14_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,83 10,33 22,33 lod 3,8 9
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran2_2015_nSecLBD_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 35,81 34,88 37,45 lod 4.4 10.4
PM_1999_QTL15_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 9,16 47,16 lod 3,6 6,5
Bourran1_2003_QTL5_peak_Bud_burst_3P Qrob_Chr09 9 s_1ATM17_504 s_1AYZFM_899 29,81 19,81 41,81 lod 3,3 8,9

0 Targeting