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Conserved domains on  [gi|1825951472|ref|XP_033059659|]
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C2 domain-containing protein 3 isoform X10 [Trachypithecus francoisi]

Protein Classification

C2 domain-containing protein 3( domain architecture ID 10171496)

C2 domain-containing protein 3 (C2CD3) is a putative calcium-dependent lipid-binding protein, a component of the centrioles that acts as a positive regulator of centriole elongation

CATH:  2.60.40.150
Gene Ontology:  GO:0060271|GO:0061511|GO:0005509
PubMed:  8976547|9632630
SCOP:  3000965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_C2cd3 cd08683
C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel ...
 1199-1341 2.30e-83

C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. 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: 176065 [Multi-domain]  Cd Length: 143  Bit Score: 269.68  E-value: 2.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472 1199 ISVQIIRACGLQAAAKALAEQEPALQFSATVGVNASVTTHLSFLPQGEQRRTHPVACSFCPEFSHHVEFTCNLVTQHCSG 1278
Cdd:cd08683      1 LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFPCNLVVQRNSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825951472 1279 EACFLAELLEFAEVIFAVYHENTKSASDIISIESCKEYLLGVVKVPTKELLIKRSGITGWYPI 1341
Cdd:cd08683     81 EAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGWYPI 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1679-1747 1.25e-05

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: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1825951472 1679 TQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWHK--GDEERVIGFASVDLSPLLSGFQFVCGWYNI 1747
Cdd:cd00030     36 TKVVKNTLNPVWNET----FEFPVLDPESDTLTVEVWDKdrFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
 
Name Accession Description Interval E-value
C2_C2cd3 cd08683
C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel ...
 1199-1341 2.30e-83

C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. 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: 176065 [Multi-domain]  Cd Length: 143  Bit Score: 269.68  E-value: 2.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472 1199 ISVQIIRACGLQAAAKALAEQEPALQFSATVGVNASVTTHLSFLPQGEQRRTHPVACSFCPEFSHHVEFTCNLVTQHCSG 1278
Cdd:cd08683      1 LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFPCNLVVQRNSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825951472 1279 EACFLAELLEFAEVIFAVYHENTKSASDIISIESCKEYLLGVVKVPTKELLIKRSGITGWYPI 1341
Cdd:cd08683     81 EAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGWYPI 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1679-1747 1.25e-05

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: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1825951472 1679 TQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWHK--GDEERVIGFASVDLSPLLSGFQFVCGWYNI 1747
Cdd:cd00030     36 TKVVKNTLNPVWNET----FEFPVLDPESDTLTVEVWDKdrFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
C2 pfam00168
C2 domain;
1679-1747 2.21e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 45.00  E-value: 2.21e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1825951472 1679 TQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWHKG--DEERVIGFASVDLSPLLSGfQFVCGWYNI 1747
Cdd:pfam00168   39 TKVVKNTLNPVWNET----FTFSVPDPENAVLEIEVYDYDrfGRDDFIGEVRIPLSELDSG-EGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 1637-1738 6.24e-05

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: 43.63  E-value: 6.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472  1637 VSILVERAMHLSLKGSPLTerkvSIPSCCVSFATADKSSpVYTQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWH 1716
Cdd:smart00239    2 LTVKIISARNLPPKDKGGK----SDPYVKVSLDGDPKEK-KKTKVVKNTLNPVWNET----FEFEVPPPELAELEIEVYD 72

                            90       100
                    ....*....|....*....|....
gi 1825951472  1717 KG--DEERVIGFASVDLSPLLSGF 1738
Cdd:smart00239   73 KDrfGRDDFIGQVTIPLSDLLLGG 96
 
Name Accession Description Interval E-value
C2_C2cd3 cd08683
C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel ...
 1199-1341 2.30e-83

C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. 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: 176065 [Multi-domain]  Cd Length: 143  Bit Score: 269.68  E-value: 2.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472 1199 ISVQIIRACGLQAAAKALAEQEPALQFSATVGVNASVTTHLSFLPQGEQRRTHPVACSFCPEFSHHVEFTCNLVTQHCSG 1278
Cdd:cd08683      1 LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFPCNLVVQRNSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825951472 1279 EACFLAELLEFAEVIFAVYHENTKSASDIISIESCKEYLLGVVKVPTKELLIKRSGITGWYPI 1341
Cdd:cd08683     81 EAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGWYPI 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1679-1747 1.25e-05

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: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1825951472 1679 TQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWHK--GDEERVIGFASVDLSPLLSGFQFVCGWYNI 1747
Cdd:cd00030     36 TKVVKNTLNPVWNET----FEFPVLDPESDTLTVEVWDKdrFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
C2 pfam00168
C2 domain;
1679-1747 2.21e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 45.00  E-value: 2.21e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1825951472 1679 TQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWHKG--DEERVIGFASVDLSPLLSGfQFVCGWYNI 1747
Cdd:pfam00168   39 TKVVKNTLNPVWNET----FTFSVPDPENAVLEIEVYDYDrfGRDDFIGEVRIPLSELDSG-EGLDGWYPL 104
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 1637-1736 3.21e-05

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc 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.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 45.35  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472 1637 VSILVERAmhlSLKGSplteRKVSIPSCCVSFaTADKSSPVYTQVVENTDSPIWNFQQQsrlskeLLLDPQQTLVFKVW- 1715
Cdd:cd04021      4 LQITVESA---KLKSN----SKSFKPDPYVEV-TVDGQPPKKTEVSKKTSNPKWNEHFT------VLVTPQSTLEFKVWs 69

                           90       100
                   ....*....|....*....|..
gi 1825951472 1716 -HKGDEERVIGFASVDLSPLLS 1736
Cdd:cd04021     70 hHTLKADVLLGEASLDLSDILK 91
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 1637-1738 6.24e-05

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: 43.63  E-value: 6.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472  1637 VSILVERAMHLSLKGSPLTerkvSIPSCCVSFATADKSSpVYTQVVENTDSPIWNFQqqsrLSKELLLDPQQTLVFKVWH 1716
Cdd:smart00239    2 LTVKIISARNLPPKDKGGK----SDPYVKVSLDGDPKEK-KKTKVVKNTLNPVWNET----FEFEVPPPELAELEIEVYD 72

                            90       100
                    ....*....|....*....|....
gi 1825951472  1717 KG--DEERVIGFASVDLSPLLSGF 1738
Cdd:smart00239   73 KDrfGRDDFIGQVTIPLSDLLLGG 96
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 1669-1760 5.31e-03

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: 38.75  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825951472 1669 ATADKSSPVYTQVVENTDS-PIWNFQQQSRLSKELLLDPQQTLVFKVWHKG--DEERVIGFASVDLSPLLSGF----QFV 1741
Cdd:cd04051     27 VWIDPSHKQSTPVDRDGGTnPTWNETLRFPLDERLLQQGRLALTIEVYCERpsLGDKLIGEVRVPLKDLLDGAspagELR 106

                           90
                   ....*....|....*....
gi 1825951472 1742 CGWYNITDFSGECQGQIKV 1760
Cdd:cd04051    107 FLSYQLRRPSGKPQGVLNF 125
 
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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