Protein : Qrob_P0027210.2 Q. robur
Protein Identifier  ? Qrob_P0027210.2 Organism . Name  Quercus robur
Score  93.0 Score Type  egn
Protein Description  (M=8) PTHR10857//PTHR10857:SF24 - COPINE // SUBFAMILY NOT NAMED Gene Prediction Quality  validated
Protein length 

Sequence

Length: 635  
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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:100263993 1 634 + 634 Gaps:47 99.16 594 79.12 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250185 1 634 + 634 Gaps:47 99.16 594 79.12 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250282 1 634 + 634 Gaps:47 99.16 594 78.78 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100262302 1 634 + 634 Gaps:47 99.16 594 78.61 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100241932 1 634 + 634 Gaps:47 99.16 594 77.59 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100247065 1 634 + 634 Gaps:47 99.16 594 77.76 0.0 protein BONZAI 3-like
blastp_kegg lcl|rcu:RCOM_1429710 1 629 + 629 Gaps:51 99.83 581 77.24 0.0 copine putative
blastp_kegg lcl|pxb:103962883 1 630 + 630 Gaps:47 98.31 593 75.99 0.0 protein BONZAI 3-like
blastp_kegg lcl|pop:POPTR_0013s03010g 1 630 + 630 Gaps:53 100.00 581 77.97 0.0 POPTRDRAFT_570912 bonzai 3 family protein
blastp_kegg lcl|pmum:103344705 1 634 + 634 Gaps:55 99.83 580 75.99 0.0 protein BONZAI 3
blastp_uniprot_sprot sp|Q5XQC7|BON3_ARATH 1 624 + 624 Gaps:48 98.97 584 72.32 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:53 99.83 578 64.99 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:56 98.29 586 62.33 0.0 Protein BONZAI 2 OS Arabidopsis thaliana GN BON2 PE 1 SV 2
blastp_uniprot_sprot sp|Q9DC53|CPNE8_MOUSE 53 623 + 571 Gaps:75 90.47 577 44.83 3e-117 Copine-8 OS Mus musculus GN Cpne8 PE 2 SV 3
blastp_uniprot_sprot sp|Q8IYJ1|CPNE9_HUMAN 53 623 + 571 Gaps:75 94.39 553 44.83 8e-117 Copine-9 OS Homo sapiens GN CPNE9 PE 1 SV 3
blastp_uniprot_sprot sp|Q86YQ8|CPNE8_HUMAN 53 623 + 571 Gaps:75 92.55 564 44.64 8e-117 Copine-8 OS Homo sapiens GN CPNE8 PE 1 SV 2
blastp_uniprot_sprot sp|O75131|CPNE3_HUMAN 53 624 + 572 Gaps:72 96.83 537 43.85 2e-115 Copine-3 OS Homo sapiens GN CPNE3 PE 1 SV 1
blastp_uniprot_sprot sp|Q99829|CPNE1_HUMAN 53 624 + 572 Gaps:69 95.90 537 42.72 2e-115 Copine-1 OS Homo sapiens GN CPNE1 PE 1 SV 1
blastp_uniprot_sprot sp|Q5BJS7|CPNE9_RAT 53 623 + 571 Gaps:75 94.39 553 44.44 3e-115 Copine-9 OS Rattus norvegicus GN Cpne9 PE 2 SV 1
blastp_uniprot_sprot sp|Q1RLL3|CPNE9_MOUSE 53 623 + 571 Gaps:75 94.39 553 44.44 4e-115 Copine-9 OS Mus musculus GN Cpne9 PE 2 SV 1
rpsblast_cdd gnl|CDD|29232 360 613 + 254 Gaps:10 99.21 254 52.38 7e-86 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 56.16 7e-56 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 53 361 + 309 Gaps:28 100.00 120 57.50 1e-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|176012 55 339 + 285 Gaps:18 89.09 110 57.14 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|201052 59 331 + 273 Gaps:18 96.47 85 47.56 1e-10 pfam00168 C2 C2 domain.
rpsblast_cdd gnl|CDD|197596 59 339 + 281 Gaps:20 89.11 101 46.67 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 59 344 + 286 Gaps:22 95.10 102 42.27 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 390 572 + 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 17 626 + 610 Gaps:93 99.62 529 49.15 1e-145 KOG1327 KOG1327 KOG1327 Copine [Signal transduction mechanisms].

18 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 246 339 94 SSF49562 none none IPR000008
SMART 54 167 114 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 242 346 105 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
Pfam 247 330 84 PF00168 none C2 domain IPR000008
Pfam 59 151 93 PF00168 none C2 domain IPR000008
Pfam 409 555 147 PF07002 none Copine IPR010734
SUPERFAMILY 388 573 186 SSF53300 none none IPR002035
ProSiteProfiles 59 152 94 PS50004 none C2 domain profile. IPR000008
SUPERFAMILY 59 158 100 SSF49562 none none IPR000008
ProSiteProfiles 390 609 220 PS50234 none VWFA domain profile. IPR002035
PANTHER 1 156 156 PTHR10857:SF24 none none IPR031116
PANTHER 202 626 425 PTHR10857:SF24 none none IPR031116
ProSiteProfiles 247 331 85 PS50004 none C2 domain profile. IPR000008
Gene3D 219 338 120 G3DSA:2.60.40.150 none none IPR000008
Gene3D 59 157 99 G3DSA:2.60.40.150 none none IPR000008
PANTHER 1 156 156 PTHR10857 none none none
PANTHER 202 626 425 PTHR10857 none none none
SMART 388 585 198 SM00327 none von Willebrand factor (vWF) type A domain IPR002035

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