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Conserved domains on  [gi|171466141|gb|ACB46290|]
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toll-interacting protein, partial [Haliotis cracherodii]

Protein Classification

C2 domain-containing protein( domain architecture ID 48786)

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

Gene Ontology:  GO:0005509
PubMed:  9632630|8976547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1-75 4.37e-48

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.


The actual alignment was detected with superfamily member cd04016:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 121  Bit Score: 150.56  E-value: 4.37e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171466141   1 PRWNKTVQTYLPNGVDSMYIEIFDERSFTVDDRIAWAHVTIPASSLNGETSDDWYPLSGRQGDEKEGMINLVMSF 75
Cdd:cd04016   47 PRWNKTIQCTLPEGVDSIYIEIFDERAFTMDERIAWTHITIPESVFNGETLDDWYSLSGKQGEDKEGMINLVFSY 121
 
Name Accession Description Interval E-value
C2_Tollip cd04016
C2 domain present in Toll-interacting protein (Tollip); Tollip is a part of the Interleukin-1 ...
 1-75 4.37e-48

C2 domain present in Toll-interacting protein (Tollip); Tollip is a part of the Interleukin-1 receptor (IL-1R) signaling pathway. Tollip is proposed to link serine/threonine kinase IRAK to IL-1Rs as well as inhibiting phosphorylation of IRAK. There is a single C2 domain present in Tollip. 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: 175983 [Multi-domain]  Cd Length: 121  Bit Score: 150.56  E-value: 4.37e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171466141   1 PRWNKTVQTYLPNGVDSMYIEIFDERSFTVDDRIAWAHVTIPASSLNGETSDDWYPLSGRQGDEKEGMINLVMSF 75
Cdd:cd04016   47 PRWNKTIQCTLPEGVDSIYIEIFDERAFTMDERIAWTHITIPESVFNGETLDDWYSLSGKQGEDKEGMINLVFSY 121
C2 pfam00168
C2 domain;
1-57 2.20e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 40.77  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 171466141    1 PRWNKTVQTYLPNGVDSM-YIEIFDERSFTVDDRIawAHVTIPASSL-NGETSDDWYPL 57
Cdd:pfam00168  48 PVWNETFTFSVPDPENAVlEIEVYDYDRFGRDDFI--GEVRIPLSELdSGEGLDGWYPL 104
 
Name Accession Description Interval E-value
C2_Tollip cd04016
C2 domain present in Toll-interacting protein (Tollip); Tollip is a part of the Interleukin-1 ...
 1-75 4.37e-48

C2 domain present in Toll-interacting protein (Tollip); Tollip is a part of the Interleukin-1 receptor (IL-1R) signaling pathway. Tollip is proposed to link serine/threonine kinase IRAK to IL-1Rs as well as inhibiting phosphorylation of IRAK. There is a single C2 domain present in Tollip. 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: 175983 [Multi-domain]  Cd Length: 121  Bit Score: 150.56  E-value: 4.37e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171466141   1 PRWNKTVQTYLPNGVDSMYIEIFDERSFTVDDRIAWAHVTIPASSLNGETSDDWYPLSGRQGDEKEGMINLVMSF 75
Cdd:cd04016   47 PRWNKTIQCTLPEGVDSIYIEIFDERAFTMDERIAWTHITIPESVFNGETLDDWYSLSGKQGEDKEGMINLVFSY 121
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1-57 6.30e-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: 42.05  E-value: 6.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 171466141   1 PRWNKTVQ-TYLPNGVDSMYIEIFDERSFTVDDRIAWAHVTIPASSLNGETSDDWYPL 57
Cdd:cd00030   45 PVWNETFEfPVLDPESDTLTVEVWDKDRFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
C2 pfam00168
C2 domain;
1-57 2.20e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 40.77  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 171466141    1 PRWNKTVQTYLPNGVDSM-YIEIFDERSFTVDDRIawAHVTIPASSL-NGETSDDWYPL 57
Cdd:pfam00168  48 PVWNETFTFSVPDPENAVlEIEVYDYDRFGRDDFI--GEVRIPLSELdSGEGLDGWYPL 104
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 11-75 6.19e-05

C2 domain (first 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 either a single C2 domain or 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: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 39.94  E-value: 6.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171466141  11 LPNGVDSMYIE--IFDERSFTVDDRIawahVTIPASSL-NGETSDDWYPLSGRQGDEKE-GMINLVMSF 75
Cdd:cd08383   53 PPPDVTFFTLSfyNKDKRSKDRDIVI----GKVALSKLdLGQGKDEWFPLTPVDPDSEVqGSVRLRARY 117
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 11-59 7.62e-05

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, which suppresses 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. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. 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: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 39.66  E-value: 7.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 171466141  11 LPNGVDSMYIEIFDERSFTVDDRIAwaHVTIPASSL-NGETSDDWYPLSG 59
Cdd:cd08400   57 LPPDVNSFTISLSNKAKRSKDSEIA--EVTVQLSKLqNGQETDEWYPLSS 104
 
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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