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Conserved domains on  [gi|42600565|gb|AAS21129|]
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At3g62780 [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 ...
 5-130 2.18e-34

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: 121.18  E-value: 2.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565   5 SLEINVTSAKGLKKV---SKMDVFVAVKLSGdpkcsdHREQRTQAARDGGTSPKWsNDVMKFILDQNLAEANRLVITFKI 81
Cdd:cd04051   1 TLEITIISAEDLKNVnlfGKMKVYAVVWIDP------SHKQSTPVDRDGGTNPTW-NETLRFPLDERLLQQGRLALTIEV 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42600565  82 KCEQRGGVDKDIGEVHVQVKELLDHLGNDKTGQRyVTYQI----GKSKADISF 130
Cdd:cd04051  74 YCERPSLGDKLIGEVRVPLKDLLDGASPAGELRF-LSYQLrrpsGKPQGVLNF 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 ...
 5-130 2.18e-34

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: 121.18  E-value: 2.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565   5 SLEINVTSAKGLKKV---SKMDVFVAVKLSGdpkcsdHREQRTQAARDGGTSPKWsNDVMKFILDQNLAEANRLVITFKI 81
Cdd:cd04051   1 TLEITIISAEDLKNVnlfGKMKVYAVVWIDP------SHKQSTPVDRDGGTNPTW-NETLRFPLDERLLQQGRLALTIEV 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42600565  82 KCEQRGGVDKDIGEVHVQVKELLDHLGNDKTGQRyVTYQI----GKSKADISF 130
Cdd:cd04051  74 YCERPSLGDKLIGEVRVPLKDLLDGASPAGELRF-LSYQLrrpsGKPQGVLNF 125
C2 pfam00168
C2 domain;
6-111 2.86e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.48  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565     6 LEINVTSAKGLKKV---SKMDVFVAVKLSgdpkcSDHREQRTQAARDGGtSPKWsNDVMKFildqNLAEANRLVITFKIK 82
Cdd:pfam00168   3 LTVTVIEAKNLPPKdgnGTSDPYVKVYLL-----DGKQKKKTKVVKNTL-NPVW-NETFTF----SVPDPENAVLEIEVY 71

                          90       100
                  ....*....|....*....|....*....
gi 42600565    83 CEQRGGVDKDIGEVHVQVKELLDHLGNDK 111
Cdd:pfam00168  72 DYDRFGRDDFIGEVRIPLSELDSGEGLDG 100
 
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 ...
 5-130 2.18e-34

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: 121.18  E-value: 2.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565   5 SLEINVTSAKGLKKV---SKMDVFVAVKLSGdpkcsdHREQRTQAARDGGTSPKWsNDVMKFILDQNLAEANRLVITFKI 81
Cdd:cd04051   1 TLEITIISAEDLKNVnlfGKMKVYAVVWIDP------SHKQSTPVDRDGGTNPTW-NETLRFPLDERLLQQGRLALTIEV 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42600565  82 KCEQRGGVDKDIGEVHVQVKELLDHLGNDKTGQRyVTYQI----GKSKADISF 130
Cdd:cd04051  74 YCERPSLGDKLIGEVRVPLKDLLDGASPAGELRF-LSYQLrrpsGKPQGVLNF 125
C2 pfam00168
C2 domain;
6-111 2.86e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.48  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565     6 LEINVTSAKGLKKV---SKMDVFVAVKLSgdpkcSDHREQRTQAARDGGtSPKWsNDVMKFildqNLAEANRLVITFKIK 82
Cdd:pfam00168   3 LTVTVIEAKNLPPKdgnGTSDPYVKVYLL-----DGKQKKKTKVVKNTL-NPVW-NETFTF----SVPDPENAVLEIEVY 71

                          90       100
                  ....*....|....*....|....*....
gi 42600565    83 CEQRGGVDKDIGEVHVQVKELLDHLGNDK 111
Cdd:pfam00168  72 DYDRFGRDDFIGEVRIPLSELDSGEGLDG 100
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 6-109 2.15e-07

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.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.22  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565   6 LEINVTSAKGLKKV---SKMDVFVAVKLSGdpkcsdHREQRTQAARDGgTSPKWsNDVMKFILDQNLAEanrlVITFKIK 82
Cdd:cd00030   1 LRVTVIEARNLPAKdlnGKSDPYVKVSLGG------KQKFKTKVVKNT-LNPVW-NETFEFPVLDPESD----TLTVEVW 68

                        90       100
                ....*....|....*....|....*..
gi 42600565  83 CEQRGGVDKDIGEVHVQVKELLDHLGN 109
Cdd:cd00030  69 DKDRFSKDDFLGEVEIPLSELLDSGKE 95
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 6-134 5.68e-05

C2 domain first 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 first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 41.77  E-value: 5.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565   6 LEINVTSAKGLKKVSKM----DVFVAVKLSGDPKCSdhreqRTQAARDgGTSPKWsnDVMKFILDQNLAEanRLVITFKI 81
Cdd:cd04044   4 LAVTIKSARGLKGSDIIggtvDPYVTFSISNRRELA-----RTKVKKD-TSNPVW--NETKYILVNSLTE--PLNLTVYD 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42600565  82 KCEQRGgvDKDIGEVHVQVKELLdhlgnDKTGQRYVTYQI---GKSKADISFTYSF 134
Cdd:cd04044  74 FNDKRK--DKLIGTAEFDLSSLL-----QNPEQENLTKNLlrnGKPVGELNYDLRF 122
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 6-131 5.75e-05

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: 41.93  E-value: 5.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565   6 LEINVTSAKGLKK---VSKMDVFVAVKLSGdpkcsdhREQRTQAARDGGTSPKWsNDvmKFILDQNLAEANRLV-ITFKI 81
Cdd:cd04049   3 LEVLLISAKGLQDtdfLGKIDPYVIIQCRT-------QERKSKVAKGDGRNPEW-NE--KFKFTVEYPGWGGDTkLILRI 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42600565  82 kceqrggVDKD-------IGEVHVQVKELLDhLGNDKtGQRYVT---YQIGksKADISFT 131
Cdd:cd04049  73 -------MDKDnfsdddfIGEATIHLKGLFE-EGVEP-GTAELVpakYNVV--LEDDTYK 121
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 2-63 8.27e-03

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. 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 synaptotagmin1. 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: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 35.69  E-value: 8.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42600565   2 GTrsLEINVTSAKGL---KKVSKMDVFVAVKLsgdpkcsDHREQRTQAARDGGTSPKWSNDvMKF 63
Cdd:cd08681   1 GT--LVVVVLKARNLpnkRKLDKQDPYCVLRI-------GGVTKKTKTDFRGGQHPEWDEE-LRF 55
 
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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