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Conserved domains on  [gi|392896996|ref|NP_499651|]
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C2 domain-containing protein [Caenorhabditis elegans]

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;
371-467 4.39e-09

C2 domain;


:

Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.25  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996  371 YLEVTVHQATGLPPieDESGCLASPSTLVSILGRDGDLRSPVFRNSRNPNWNFMARFALS-SERRNLVVKVIHRGALL-D 448
Cdd:pfam00168   2 RLTVTVIEAKNLPP--KDGNGTSDPYVKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPdPENAVLEIEVYDYDRFGrD 79

                          90
                  ....*....|....*....
gi 392896996  449 LPLGFVSIPLPTPNFSRSV 467
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGL 98
 
Name Accession Description Interval E-value
C2 pfam00168
C2 domain;
371-467 4.39e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.25  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996  371 YLEVTVHQATGLPPieDESGCLASPSTLVSILGRDGDLRSPVFRNSRNPNWNFMARFALS-SERRNLVVKVIHRGALL-D 448
Cdd:pfam00168   2 RLTVTVIEAKNLPP--KDGNGTSDPYVKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPdPENAVLEIEVYDYDRFGrD 79

                          90
                  ....*....|....*....
gi 392896996  449 LPLGFVSIPLPTPNFSRSV 467
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGL 98
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 372-471 3.76e-06

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: 45.52  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996 372 LEVTVHQATGLPPIEDESgclaSPSTLVSI-LGRDGDLRSPVFRNSRNPNWNFMARFALSS-ERRNLVVKVIHRGALL-D 448
Cdd:cd00030    1 LRVTVIEARNLPAKDLNG----KSDPYVKVsLGGKQKFKTKVVKNTLNPVWNETFEFPVLDpESDTLTVEVWDKDRFSkD 76

                         90       100
                 ....*....|....*....|...
gi 392896996 449 LPLGFVSIPLPTPNFSRSVYEMT 471
Cdd:cd00030   77 DFLGEVEIPLSELLDSGKEGELW 99
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 371-458 1.80e-04

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: 40.93  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996   371 YLEVTVHQATGLPPieDESGCLASPSTLVSILGRDGD-LRSPVFRNSRNPNWNFMARFALS-SERRNLVVKVIHRGALL- 447
Cdd:smart00239   1 TLTVKIISARNLPP--KDKGGKSDPYVKVSLDGDPKEkKKTKVVKNTLNPVWNETFEFEVPpPELAELEIEVYDKDRFGr 78

                           90
                   ....*....|.
gi 392896996   448 DLPLGFVSIPL 458
Cdd:smart00239  79 DDFIGQVTIPL 89
 
Name Accession Description Interval E-value
C2 pfam00168
C2 domain;
371-467 4.39e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.25  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996  371 YLEVTVHQATGLPPieDESGCLASPSTLVSILGRDGDLRSPVFRNSRNPNWNFMARFALS-SERRNLVVKVIHRGALL-D 448
Cdd:pfam00168   2 RLTVTVIEAKNLPP--KDGNGTSDPYVKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPdPENAVLEIEVYDYDRFGrD 79

                          90
                  ....*....|....*....
gi 392896996  449 LPLGFVSIPLPTPNFSRSV 467
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGL 98
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 372-471 3.76e-06

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: 45.52  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996 372 LEVTVHQATGLPPIEDESgclaSPSTLVSI-LGRDGDLRSPVFRNSRNPNWNFMARFALSS-ERRNLVVKVIHRGALL-D 448
Cdd:cd00030    1 LRVTVIEARNLPAKDLNG----KSDPYVKVsLGGKQKFKTKVVKNTLNPVWNETFEFPVLDpESDTLTVEVWDKDRFSkD 76

                         90       100
                 ....*....|....*....|...
gi 392896996 449 LPLGFVSIPLPTPNFSRSVYEMT 471
Cdd:cd00030   77 DFLGEVEIPLSELLDSGKEGELW 99
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 374-458 5.71e-06

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: 45.91  E-value: 5.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996 374 VTVHQATGLPPiEDESGclaSPSTLVSI-LGRDGDLRSpVFRNSRNPNWNFMARFALS------SERRNLVVKVIHRGAL 446
Cdd:cd08682    3 VTVLQARGLLC-KGKSG---TNDAYVIIqLGKEKYSTS-VKEKTTSPVWKEECSFELPgllsgnGNRATLQLTVMHRNLL 77

                         90
                 ....*....|...
gi 392896996 447 -LDLPLGFVSIPL 458
Cdd:cd08682   78 gLDKFLGQVSIPL 90
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 372-458 2.97e-05

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: 43.76  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996 372 LEVTVHQATGLPpiEDESGCLASPSTLVSILGRDGdLRSPVFRN-SRNPNWNFMARF-----ALSSERRNLVVKVIHRGA 445
Cdd:cd04051    2 LEITIISAEDLK--NVNLFGKMKVYAVVWIDPSHK-QSTPVDRDgGTNPTWNETLRFplderLLQQGRLALTIEVYCERP 78

                         90
                 ....*....|....
gi 392896996 446 LL-DLPLGFVSIPL 458
Cdd:cd04051   79 SLgDKLIGEVRVPL 92
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 372-458 7.03e-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: 42.54  E-value: 7.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996 372 LEVTVHQATGLPPIEDESGCLaSPSTLVSILGRDGDLRSPVFRNSRNPNWNFMARFALSSERRNLVVKVIH-RGALLDLP 450
Cdd:cd04044    4 LAVTIKSARGLKGSDIIGGTV-DPYVTFSISNRRELARTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDfNDKRKDKL 82


                 ....*...
gi 392896996 451 LGFVSIPL 458
Cdd:cd04044   83 IGTAEFDL 90
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 371-458 1.80e-04

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: 40.93  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996   371 YLEVTVHQATGLPPieDESGCLASPSTLVSILGRDGD-LRSPVFRNSRNPNWNFMARFALS-SERRNLVVKVIHRGALL- 447
Cdd:smart00239   1 TLTVKIISARNLPP--KDKGGKSDPYVKVSLDGDPKEkKKTKVVKNTLNPVWNETFEFEVPpPELAELEIEVYDKDRFGr 78

                           90
                   ....*....|.
gi 392896996   448 DLPLGFVSIPL 458
Cdd:smart00239  79 DDFIGQVTIPL 89
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
 374-466 4.82e-03

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. 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: 176011 [Multi-domain]  Cd Length: 126  Bit Score: 37.26  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896996 374 VTVHQATGLPPiEDESGcLASPSTLVSILGRDgdLRSPVFRNSRNPNWNFMARFALSSERRNLVVKVIHRGALLDLPLGF 453
Cdd:cd04046    7 VHVHSAEGLSK-QDSGG-GADPYVIIKCEGES--VRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFLGQ 82

                         90
                 ....*....|...
gi 392896996 454 VSIPlPTPNFSRS 466
Cdd:cd04046   83 ATLS-ADPNDSQT 94
 
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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