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Conserved domains on  [gi|42569943|ref|NP_182100|]
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BON association protein 2 [Arabidopsis thaliana]

Protein Classification

C2 domain-containing protein( domain architecture ID 10134346)

C2 domain-containing protein similar to Arabidopsis thaliana BON1-associated protein, which may act as negative regulator of cell death and defense responses and exhibit calcium-dependent phospholipid binding properties

CATH:  2.60.40.150
Gene Ontology:  GO:0005544|GO:0005509
PubMed:  8976547|9632630
SCOP:  3000965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 9-130 2.17e-42

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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.


:

Pssm-ID: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 138.90  E-value: 2.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943   9 SLEIEVISAEGLKVDRKPLKKKTYSVVRIDEKSWAS-KVDELGGSYPIWKDRFDMEMP---INASVRFISIEVYYRTSGS 84
Cdd:cd04051   1 TLEITIISAEDLKNVNLFGKMKVYAVVWIDPSHKQStPVDRDGGTNPTWNETLRFPLDerlLQQGRLALTIEVYCERPSL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42569943  85 GrDKNVGYAKIPVTDFMGGFAPQGHLNFLSYRLRDEYGDKCGIVNV 130
Cdd:cd04051  81 G-DKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSGKPQGVLNF 125
 
Name Accession Description Interval E-value
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 9-130 2.17e-42

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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.


Pssm-ID: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 138.90  E-value: 2.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943   9 SLEIEVISAEGLKVDRKPLKKKTYSVVRIDEKSWAS-KVDELGGSYPIWKDRFDMEMP---INASVRFISIEVYYRTSGS 84
Cdd:cd04051   1 TLEITIISAEDLKNVNLFGKMKVYAVVWIDPSHKQStPVDRDGGTNPTWNETLRFPLDerlLQQGRLALTIEVYCERPSL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42569943  85 GrDKNVGYAKIPVTDFMGGFAPQGHLNFLSYRLRDEYGDKCGIVNV 130
Cdd:cd04051  81 G-DKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSGKPQGVLNF 125
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 9-108 5.95e-09

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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 51.72  E-value: 5.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943      9 SLEIEVISAEGLKVDRKPLKKKTYSVVRID---EKSWASKVDElGGSYPIWKDRFDMEMPiNASVRFISIEVYYRTSGSg 85
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDgdpKEKKKTKVVK-NTLNPVWNETFEFEVP-PPELAELEIEVYDKDRFG- 77

                           90       100
                   ....*....|....*....|...
gi 42569943     86 RDKNVGYAKIPVTDFMGGFAPQG 108
Cdd:smart00239  78 RDDFIGQVTIPLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
10-111 8.71e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 40.38  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943    10 LEIEVISAEGLKVDRKPLKKKTYSVVRI--DEKSWASKVDElGGSYPIWKDRFDMEMPiNASVRFISIEVYYRTSGsGRD 87
Cdd:pfam00168   3 LTVTVIEAKNLPPKDGNGTSDPYVKVYLldGKQKKKTKVVK-NTLNPVWNETFTFSVP-DPENAVLEIEVYDYDRF-GRD 79

                          90       100
                  ....*....|....*....|....
gi 42569943    88 KNVGYAKIPVTDFMGGFAPQGHLN 111
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGLDGWYP 103
 
Name Accession Description Interval E-value
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 9-130 2.17e-42

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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.


Pssm-ID: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 138.90  E-value: 2.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943   9 SLEIEVISAEGLKVDRKPLKKKTYSVVRIDEKSWAS-KVDELGGSYPIWKDRFDMEMP---INASVRFISIEVYYRTSGS 84
Cdd:cd04051   1 TLEITIISAEDLKNVNLFGKMKVYAVVWIDPSHKQStPVDRDGGTNPTWNETLRFPLDerlLQQGRLALTIEVYCERPSL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42569943  85 GrDKNVGYAKIPVTDFMGGFAPQGHLNFLSYRLRDEYGDKCGIVNV 130
Cdd:cd04051  81 G-DKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSGKPQGVLNF 125
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 9-108 5.95e-09

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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 51.72  E-value: 5.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943      9 SLEIEVISAEGLKVDRKPLKKKTYSVVRID---EKSWASKVDElGGSYPIWKDRFDMEMPiNASVRFISIEVYYRTSGSg 85
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDgdpKEKKKTKVVK-NTLNPVWNETFEFEVP-PPELAELEIEVYDKDRFG- 77

                           90       100
                   ....*....|....*....|...
gi 42569943     86 RDKNVGYAKIPVTDFMGGFAPQG 108
Cdd:smart00239  78 RDDFIGQVTIPLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
10-111 8.71e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 40.38  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943    10 LEIEVISAEGLKVDRKPLKKKTYSVVRI--DEKSWASKVDElGGSYPIWKDRFDMEMPiNASVRFISIEVYYRTSGsGRD 87
Cdd:pfam00168   3 LTVTVIEAKNLPPKDGNGTSDPYVKVYLldGKQKKKTKVVK-NTLNPVWNETFTFSVP-DPENAVLEIEVYDYDRF-GRD 79

                          90       100
                  ....*....|....*....|....
gi 42569943    88 KNVGYAKIPVTDFMGGFAPQGHLN 111
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGLDGWYP 103
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 7-135 9.52e-05

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. 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. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 40.60  E-value: 9.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943   7 KRSLEIEVISAEGLKVDRKPLKKKTYSVVRI--------DEKSWASKVDELGGSYPIWKD--RFDMEMPINASVRFisiE 76
Cdd:cd00275   1 PLTLTIKIISGQQLPKPKGDKGSIVDPYVEVeihglpadDSAKFKTKVVKNNGFNPVWNEtfEFDVTVPELAFLRF---V 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42569943  77 VYyrTSGSGRDKNVGYAKIPVTDFMggfapQGhlnflsYR---LRDEYGDKcgIVNVSIMVK 135
Cdd:cd00275  78 VY--DEDSGDDDFLGQACLPLDSLR-----QG------YRhvpLLDSKGEP--LELSTLFVH 124
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 14-100 8.15e-04

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. 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.


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 37.82  E-value: 8.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943  14 VISAEGLKVDRKPLKKKTYSVVRIDEKSWASKVDELGGSyPIWKDRFDMEMP----INASVRFISIEVYYRTSGsGRDKN 89
Cdd:cd08682   5 VLQARGLLCKGKSGTNDAYVIIQLGKEKYSTSVKEKTTS-PVWKEECSFELPgllsGNGNRATLQLTVMHRNLL-GLDKF 82

                        90
                ....*....|.
gi 42569943  90 VGYAKIPVTDF 100
Cdd:cd08682  83 LGQVSIPLNDL 93
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 10-120 9.86e-04

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. 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. Members have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 37.70  E-value: 9.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569943  10 LEIEVISAEGLKvDRKPLKKKTYSVV---RIDEKSwaSKVDELGGSYPIW--KDRFDMEMPINASVRFISIEVYYRTSGS 84
Cdd:cd04049   3 LEVLLISAKGLQ-DTDFLGKIDPYVIiqcRTQERK--SKVAKGDGRNPEWneKFKFTVEYPGWGGDTKLILRIMDKDNFS 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 42569943  85 GrDKNVGYAKIPVTDF--MGGFAPQGHLNFLSYRLRDE 120
Cdd:cd04049  80 D-DDFIGEATIHLKGLfeEGVEPGTAELVPAKYNVVLE 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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