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Conserved domains on  [gi|2217321809|ref|XP_047294976|]
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coiled-coil and C2 domain-containing protein 1A isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 216-373 1.85e-81

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 250.30  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 216 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 295
Cdd:cd08690     1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217321809 296 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 373
Cdd:cd08690    78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
58-116 2.81e-19

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 81.58  E-value: 2.81e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217321809   58 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 116
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
chemoreceptor_sensor super family cl00144
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
 415-482 4.02e-04

4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others.


The actual alignment was detected with superfamily member cd22899:

Pssm-ID: 444710 [Multi-domain]  Cd Length: 116  Bit Score: 40.20  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 415 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 475
Cdd:cd22899    23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                          90
                  ....*....|....
gi 2217321809 476 -------QLQFYTE 482
Cdd:cd22899    98 qidqfvlALQHFAE 111
 
Name Accession Description Interval E-value
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 216-373 1.85e-81

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 250.30  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 216 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 295
Cdd:cd08690     1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217321809 296 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 373
Cdd:cd08690    78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
58-116 2.81e-19

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 81.58  E-value: 2.81e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217321809   58 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 116
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
223-326 8.31e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.09  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 223 LFIVKGINLPTPPGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 302
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 2217321809 303 VHKGGLFKtDRVLGTAQLKLDALE 326
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 225-325 2.64e-08

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: 51.72  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809  225 IVKGINLPTPPGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 304
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|.
gi 2217321809  305 KGGlFKTDRVLGTAQLKLDAL 325
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDL 92
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 415-482 4.02e-04

ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX.


Pssm-ID: 438631 [Multi-domain]  Cd Length: 116  Bit Score: 40.20  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 415 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 475
Cdd:cd22899    23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                          90
                  ....*....|....
gi 2217321809 476 -------QLQFYTE 482
Cdd:cd22899    98 qidqfvlALQHFAE 111
 
Name Accession Description Interval E-value
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 216-373 1.85e-81

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 250.30  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 216 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 295
Cdd:cd08690     1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217321809 296 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 373
Cdd:cd08690    78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
58-116 2.81e-19

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 81.58  E-value: 2.81e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217321809   58 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 116
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
223-326 8.31e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.09  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 223 LFIVKGINLPTPPGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 302
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 2217321809 303 VHKGGLFKtDRVLGTAQLKLDALE 326
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 225-325 2.64e-08

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: 51.72  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809  225 IVKGINLPTPPGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 304
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|.
gi 2217321809  305 KGGlFKTDRVLGTAQLKLDAL 325
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDL 92
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 225-333 1.52e-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: 49.37  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 225 IVKGINLPtpPGLSPGDLDVFVRFdfpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 304
Cdd:cd00030     5 VIEARNLP--AKDLNGKSDPYVKV-----SLGGKQKFKTKVVKNTLNPVWNETFEFPVLDP--------ESDTLTVEVWD 69

                          90       100
                  ....*....|....*....|....*....
gi 2217321809 305 KGGlFKTDRVLGTAQLKLDALEIACEVRE 333
Cdd:cd00030    70 KDR-FSKDDFLGEVEIPLSELLDSGKEGE 97
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 225-345 6.27e-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: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 225 IVKGINLPTPPGLSpGDLDVFVRFDFPYPNVEEaqkdKTSVIKNTDSPEFKEQFKLCINRshrgfrraiQTKGIKFEVVH 304
Cdd:cd04044     8 IKSARGLKGSDIIG-GTVDPYVTFSISNRRELA----RTKVKKDTSNPVWNETKYILVNS---------LTEPLNLTVYD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217321809 305 KGGlFKTDRVLGTAQLKLDALEIACEVREI-LEVLDGRRPTG 345
Cdd:cd04044    74 FND-KRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGKPVG 114
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 225-316 1.41e-04

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 41.80  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 225 IVKGINLPTPPGlsPGDLDVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQTKGIKFEVVH 304
Cdd:cd00276    20 VLKARNLPPSDG--KGLSDPYVKVSL-LQGGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAEQ------LEEVSLVITVVD 90

                          90
                  ....*....|..
gi 2217321809 305 KGGLFKtDRVLG 316
Cdd:cd00276    91 KDSVGR-NEVIG 101
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 251-341 1.91e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. 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: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 41.20  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 251 PYPNVE---EAQKDKTSVIKNTDSPEFKEQFKlcinrshrgFRRAIQTKGIKFEVVHKGGLfKTDRVLGTAQLKLDALEI 327
Cdd:cd08678    20 PYCVLEmdePPQKYQSSTQKNTSNPFWDEHFL---------FELSPNSKELLFEVYDNGKK-SDSKFLGLAIVPFDELRK 89

                          90
                  ....*....|....
gi 2217321809 328 ACEVREILEvLDGR 341
Cdd:cd08678    90 NPSGRQIFP-LQGR 102
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 415-482 4.02e-04

ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX.


Pssm-ID: 438631 [Multi-domain]  Cd Length: 116  Bit Score: 40.20  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 415 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 475
Cdd:cd22899    23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                          90
                  ....*....|....
gi 2217321809 476 -------QLQFYTE 482
Cdd:cd22899    98 qidqfvlALQHFAE 111
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 217-328 1.30e-03

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 38.79  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 217 SSNDMLLFIVKGI-NLPTPpglSPGDL-DVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQ 294
Cdd:cd04030    13 SQRQKLIVTVHKCrNLPPC---DSSDIpDPYVRLYL-LPDKSKSTRRKTSVKKDNLNPVFDETFEFPVSLEE------LK 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217321809 295 TKGIKFEVVHKGGLFKTDR-VLGTAQLKLDALEIA 328
Cdd:cd04030    83 RRTLDVAVKNSKSFLSREKkLLGQVLIDLSDLDLS 117
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 242-333 4.16e-03

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 38.00  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321809 242 LDVFVRFDFPypnveeAQKDKTSVIKNTDSPEFKEQFKLCINrshrgF----RRaiqtkgIKFEVVHKGGLFKTDrVLGT 317
Cdd:cd04018    35 VDPYVEVSFA------GQKVKTSVKKNSYNPEWNEQIVFPEM-----FpplcER------IKIQIRDWDRVGNDD-VIGT 96

                          90
                  ....*....|....*.
gi 2217321809 318 AQLKLDalEIACEVRE 333
Cdd:cd04018    97 HFIDLS--KISNSGDE 110
 
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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