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Conserved domains on  [gi|1250175279|gb|ATI08931|]
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Der f 36 allergen [Dermatophagoides farinae]

Protein Classification

C2 domain-containing protein( domain architecture ID 10445584)

C2 domain-containing protein may be a Ca2+-dependent membrane-targeting protein that binds a wide variety of substances including phospholipids, inositol polyphosphates, and intracellular proteins through its C2 domain

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 pfam00168
C2 domain;
96-208 2.23e-07

C2 domain;


:

Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 47.70  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279  96 GHIDIELISA------SLYEKANAYATVCIMNNslpislpIQDRRnciscsTHVKENTNYPVWNEVCVgssnyLFVSDSR 169
Cdd:pfam00168   1 GRLTVTVIEAknlppkDGNGTSDPYVKVYLLDG-------KQKKK------TKVVKNTLNPVWNETFT-----FSVPDPE 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1250175279 170 VTT---EVWDHHGSNNNVFLGGVTLTIDQLVNHGDNHRQINL 208
Cdd:pfam00168  63 NAVleiEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
 
Name Accession Description Interval E-value
C2 pfam00168
C2 domain;
96-208 2.23e-07

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 47.70  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279  96 GHIDIELISA------SLYEKANAYATVCIMNNslpislpIQDRRnciscsTHVKENTNYPVWNEVCVgssnyLFVSDSR 169
Cdd:pfam00168   1 GRLTVTVIEAknlppkDGNGTSDPYVKVYLLDG-------KQKKK------TKVVKNTLNPVWNETFT-----FSVPDPE 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1250175279 170 VTT---EVWDHHGSNNNVFLGGVTLTIDQLVNHGDNHRQINL 208
Cdd:pfam00168  63 NAVleiEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 102-205 9.97e-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: 45.91  E-value: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279 102 LISASLYEKANAYATVCIMNNslpislpiqdrrncISCSTHVKENTNYPVWNEVCVgsSNYLFVSDSRVTTEVWDHHGSN 181
Cdd:cd00030    11 LPAKDLNGKSDPYVKVSLGGK--------------QKFKTKVVKNTLNPVWNETFE--FPVLDPESDTLTVEVWDKDRFS 74

                          90       100
                  ....*....|....*....|....
gi 1250175279 182 NNVFLGGVTLTIDQLVNHGDNHRQ 205
Cdd:cd00030    75 KDDFLGEVEIPLSELLDSGKEGEL 98
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 102-200 1.00e-06

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: 45.94  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279  102 LISASLYEKANAYATVCIMNnslpislpiqdrRNCISCSTHVKENTNYPVWNEVCVGSSNYLFVSDSRVttEVWDHHGSN 181
Cdd:smart00239  12 LPPKDKGGKSDPYVKVSLDG------------DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEI--EVYDKDRFG 77

                           90
                   ....*....|....*....
gi 1250175279  182 NNVFLGGVTLTIDQLVNHG 200
Cdd:smart00239  78 RDDFIGQVTIPLSDLLLGG 96
 
Name Accession Description Interval E-value
C2 pfam00168
C2 domain;
96-208 2.23e-07

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 47.70  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279  96 GHIDIELISA------SLYEKANAYATVCIMNNslpislpIQDRRnciscsTHVKENTNYPVWNEVCVgssnyLFVSDSR 169
Cdd:pfam00168   1 GRLTVTVIEAknlppkDGNGTSDPYVKVYLLDG-------KQKKK------TKVVKNTLNPVWNETFT-----FSVPDPE 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1250175279 170 VTT---EVWDHHGSNNNVFLGGVTLTIDQLVNHGDNHRQINL 208
Cdd:pfam00168  63 NAVleiEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 102-205 9.97e-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: 45.91  E-value: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279 102 LISASLYEKANAYATVCIMNNslpislpiqdrrncISCSTHVKENTNYPVWNEVCVgsSNYLFVSDSRVTTEVWDHHGSN 181
Cdd:cd00030    11 LPAKDLNGKSDPYVKVSLGGK--------------QKFKTKVVKNTLNPVWNETFE--FPVLDPESDTLTVEVWDKDRFS 74

                          90       100
                  ....*....|....*....|....
gi 1250175279 182 NNVFLGGVTLTIDQLVNHGDNHRQ 205
Cdd:cd00030    75 KDDFLGEVEIPLSELLDSGKEGEL 98
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 102-200 1.00e-06

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: 45.94  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279  102 LISASLYEKANAYATVCIMNnslpislpiqdrRNCISCSTHVKENTNYPVWNEVCVGSSNYLFVSDSRVttEVWDHHGSN 181
Cdd:smart00239  12 LPPKDKGGKSDPYVKVSLDG------------DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEI--EVYDKDRFG 77

                           90
                   ....*....|....*....
gi 1250175279  182 NNVFLGGVTLTIDQLVNHG 200
Cdd:smart00239  78 RDDFIGQVTIPLSDLLLGG 96
C2B_Tricalbin-like cd04052
C2 domain second repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 104-213 4.03e-04

C2 domain second 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176017 [Multi-domain]  Cd Length: 111  Bit Score: 38.74  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279 104 SASLYEKANAYATVcIMNNSLPISlpiqdrrnciscsTHVKENTNYPVWNEVCvgssnYLFVSD---SRVTTEVWDHHGS 180
Cdd:cd04052     6 SESKTGLLSPYAEL-YLNGKLVYT-------------TRVKKKTNNPSWNAST-----EFLVTDrrkSRVTVVVKDDRDR 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1250175279 181 NNNVfLGGVTLTIDQLVNHGD-NHRQINLAMAGG 213
Cdd:cd04052    67 HDPV-LGSVSISLNDLIDATSvGQQWFPLSGNGQ 99
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 126-198 8.29e-04

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.


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 37.93  E-value: 8.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1250175279 126 ISLPIQDRRNCISCSTHVKENTNYPVWNEVCV-----GSSNYlfvsDSRVTTEVWDHHGSNNNVFLGGVTLTIDQLVN 198
Cdd:cd04047    27 ISRQSEDGTWVLVYRTEVIKNTLNPVWKPFTIplqklCNGDY----DRPIKIEVYDYDSSGKHDLIGEFETTLDELLK 100
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 114-200 1.36e-03

C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like 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-I topology.


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 37.74  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279 114 YATVCIMNNSLPISlpiqdRRnciscsTHVKENTNYPVWNE-----VCVGSSNYLF--------VSDSRVTTEVWDHHGS 180
Cdd:cd08675    22 FARVTLNYSSKTDT-----KR------TKVKKKTNNPRFDEafyfeLTIGFSYEKKsfkveeedLEKSELRVELWHASMV 90

                          90       100
                  ....*....|....*....|
gi 1250175279 181 NNNVFLGGVTLTIDQLVNHG 200
Cdd:cd08675    91 SGDDFLGEVRIPLQGLQQAG 110
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 143-202 5.99e-03

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. 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.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 36.15  E-value: 5.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250175279 143 VKENTNyPVWNevcvgssnYLFVSDSrVTTE----------VWDHHGSNNNVFLGGVTLTIDQLVNHGDN 202
Cdd:cd04020    71 VKKSVN-PVWN--------HTFVYDG-VSPEdlsqacleltVWDHDKLSSNDFLGGVRLGLGTGKSYGQA 130
 
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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