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Conserved domains on  [gi|386769453|ref|NP_001245976|]
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lethal (2) giant discs 1, isoform B [Drosophila melanogaster]

Protein Classification

C2 domain-containing protein; PLC family C2 domain-containing protein( domain architecture ID 10653458)

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| PLC (phosphoinositide-specific phospholipases C) family C2 domain-containing protein similar to PLCs that are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG)

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); ...
661-832 2.55e-80

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: 254.92  E-value: 2.55e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 661 LTDSELEIVVVRGI-SYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGV 739
Cdd:cd08690    1 DSSIELTIVRCIGIpLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKRHGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 740 KFEIYSRGcsidccglsrklplccfrGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILT 819
Cdd:cd08690   81 KFEVYHKG------------------GFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTG 142
                        170
                 ....*....|...
gi 386769453 820 KQMEHITEKWLVL 832
Cdd:cd08690  143 KQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
362-420 1.34e-22

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 91.59  E-value: 1.34e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   362 LEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPP 420
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
260-318 4.69e-22

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 90.05  E-value: 4.69e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   260 VTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPP 318
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
499-557 1.76e-21

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 88.51  E-value: 1.76e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   499 MKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPP 557
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
142-200 3.34e-20

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 84.66  E-value: 3.34e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   142 LSIIKQRLEMYKQAEANAKTAGDSGKARRFGRGLKTLKDLHRQAAAGKSINVDDIPPEV 200
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
 
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); ...
661-832 2.55e-80

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: 254.92  E-value: 2.55e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 661 LTDSELEIVVVRGI-SYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGV 739
Cdd:cd08690    1 DSSIELTIVRCIGIpLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKRHGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 740 KFEIYSRGcsidccglsrklplccfrGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILT 819
Cdd:cd08690   81 KFEVYHKG------------------GFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTG 142
                        170
                 ....*....|...
gi 386769453 820 KQMEHITEKWLVL 832
Cdd:cd08690  143 KQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
362-420 1.34e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 91.59  E-value: 1.34e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   362 LEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPP 420
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
260-318 4.69e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 90.05  E-value: 4.69e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   260 VTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPP 318
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
499-557 1.76e-21

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 88.51  E-value: 1.76e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   499 MKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPP 557
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
142-200 3.34e-20

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 84.66  E-value: 3.34e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   142 LSIIKQRLEMYKQAEANAKTAGDSGKARRFGRGLKTLKDLHRQAAAGKSINVDDIPPEV 200
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
666-796 6.65e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 51.17  E-value: 6.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453  666 LEIVVVRGIsyNVAnPKD----VDTYVRVEfplLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKF 741
Cdd:pfam00168   3 LTVTVIEAK--NLP-PKDgngtSDPYVKVY---LLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAV--------LEI 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386769453  742 EIYSrgcsidccglsrklplccfRGFLRSDTLIGTVNVKLQPLETKCEIHDTYDL 796
Cdd:pfam00168  69 EVYD-------------------YDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
666-786 8.69e-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: 45.17  E-value: 8.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453   666 LEIVVVRGISYNVANPKD-VDTYVRVEfpLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEIY 744
Cdd:smart00239   2 LTVKIISARNLPPKDKGGkSDPYVKVS--LDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAE--------LEIEVY 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 386769453   745 SRGCsidccglsrklplccfrgfLRSDTLIGTVNVKLQPLET 786
Cdd:smart00239  72 DKDR-------------------FGRDDFIGQVTIPLSDLLL 94
 
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); ...
661-832 2.55e-80

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: 254.92  E-value: 2.55e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 661 LTDSELEIVVVRGI-SYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGV 739
Cdd:cd08690    1 DSSIELTIVRCIGIpLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKRHGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 740 KFEIYSRGcsidccglsrklplccfrGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILT 819
Cdd:cd08690   81 KFEVYHKG------------------GFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTG 142
                        170
                 ....*....|...
gi 386769453 820 KQMEHITEKWLVL 832
Cdd:cd08690  143 KQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
362-420 1.34e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 91.59  E-value: 1.34e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   362 LEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPP 420
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
260-318 4.69e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 90.05  E-value: 4.69e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   260 VTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPP 318
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
499-557 1.76e-21

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 88.51  E-value: 1.76e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   499 MKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPP 557
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
142-200 3.34e-20

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 84.66  E-value: 3.34e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769453   142 LSIIKQRLEMYKQAEANAKTAGDSGKARRFGRGLKTLKDLHRQAAAGKSINVDDIPPEV 200
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
666-796 6.65e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 51.17  E-value: 6.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453  666 LEIVVVRGIsyNVAnPKD----VDTYVRVEfplLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKF 741
Cdd:pfam00168   3 LTVTVIEAK--NLP-PKDgngtSDPYVKVY---LLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAV--------LEI 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386769453  742 EIYSrgcsidccglsrklplccfRGFLRSDTLIGTVNVKLQPLETKCEIHDTYDL 796
Cdd:pfam00168  69 EVYD-------------------YDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
666-786 8.69e-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: 45.17  E-value: 8.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453   666 LEIVVVRGISYNVANPKD-VDTYVRVEfpLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEIY 744
Cdd:smart00239   2 LTVKIISARNLPPKDKGGkSDPYVKVS--LDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAE--------LEIEVY 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 386769453   745 SRGCsidccglsrklplccfrgfLRSDTLIGTVNVKLQPLET 786
Cdd:smart00239  72 DKDR-------------------FGRDDFIGQVTIPLSDLLL 94
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
666-796 1.02e-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: 45.14  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 666 LEIVVV--RGISYNVANPKdVDTYVRVEFpllnDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEI 743
Cdd:cd00030    1 LRVTVIeaRNLPAKDLNGK-SDPYVKVSL----GGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDT--------LTVEV 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 386769453 744 YSrgcsidccglsrklplccfRGFLRSDTLIGTVNVKLQPLETKCEIHD-TYDL 796
Cdd:cd00030   68 WD-------------------KDRFSKDDFLGEVEIPLSELLDSGKEGElWLPL 102
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
668-723 2.19e-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: 2.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769453 668 IVVVRGISYNVANPKD--VDTYVRVEfpLLNDESFKT--KTNVIRDTSSPDYDERFKVDI 723
Cdd:cd04030   19 IVTVHKCRNLPPCDSSdiPDPYVRLY--LLPDKSKSTrrKTSVKKDNLNPVFDETFEFPV 76
 
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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