NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19921130|ref|NP_609488|]
View 

lethal (2) giant discs 1, isoform A [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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); ...
 661-814 1.66e-84

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: 265.71  E-value: 1.66e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 661 LTDSELEIVVVRGI-SYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGV 739
Cdd:cd08690   1 DSSIELTIVRCIGIpLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKRHGL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921130 740 KFEIYSRGGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILTKQMEHITEKWLVL 814
Cdd:cd08690  81 KFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
362-420 2.25e-22

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 90.82  E-value: 2.25e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    362 LEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPP 420
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
260-318 7.99e-22

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 89.28  E-value: 7.99e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    260 VTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPP 318
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
499-557 3.00e-21

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 87.74  E-value: 3.00e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    499 MKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPP 557
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
142-200 5.47e-20

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 83.89  E-value: 5.47e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    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); ...
 661-814 1.66e-84

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: 265.71  E-value: 1.66e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 661 LTDSELEIVVVRGI-SYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGV 739
Cdd:cd08690   1 DSSIELTIVRCIGIpLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKRHGL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921130 740 KFEIYSRGGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILTKQMEHITEKWLVL 814
Cdd:cd08690  81 KFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
362-420 2.25e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 90.82  E-value: 2.25e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    362 LEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPP 420
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
260-318 7.99e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 89.28  E-value: 7.99e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    260 VTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPP 318
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
499-557 3.00e-21

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 87.74  E-value: 3.00e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    499 MKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPP 557
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
142-200 5.47e-20

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 83.89  E-value: 5.47e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    142 LSIIKQRLEMYKQAEANAKTAGDSGKARRFGRGLKTLKDLHRQAAAGKSINVDDIPPEV 200
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
666-778 9.03e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 59.25  E-value: 9.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130   666 LEIVVVRGIsyNVAnPKD----VDTYVRVEfplLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKF 741
Cdd:pfam00168   3 LTVTVIEAK--NLP-PKDgngtSDPYVKVY---LLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAV--------LEI 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 19921130   742 EIYSRGGFLRsDTLIGTVNVKLQPLETKCEIHDTYDL 778
Cdd:pfam00168  69 EVYDYDRFGR-DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 666-768 4.27e-09

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: 54.42  E-value: 4.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130    666 LEIVVVRGISYNVANPKD-VDTYVRVEfpLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEIY 744
Cdd:smart00239   2 LTVKIISARNLPPKDKGGkSDPYVKVS--LDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAE--------LEIEVY 71

                           90       100
                   ....*....|....*....|....
gi 19921130    745 SRGGFLRsDTLIGTVNVKLQPLET 768
Cdd:smart00239  72 DKDRFGR-DDFIGQVTIPLSDLLL 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); ...
 661-814 1.66e-84

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: 265.71  E-value: 1.66e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 661 LTDSELEIVVVRGI-SYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGV 739
Cdd:cd08690   1 DSSIELTIVRCIGIpLPSGWNPKDLDTYVKFEFPYPNEEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKRHGL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921130 740 KFEIYSRGGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILTKQMEHITEKWLVL 814
Cdd:cd08690  81 KFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
362-420 2.25e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 90.82  E-value: 2.25e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    362 LEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPP 420
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
260-318 7.99e-22

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 89.28  E-value: 7.99e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    260 VTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPP 318
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
499-557 3.00e-21

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 87.74  E-value: 3.00e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    499 MKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPP 557
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
142-200 5.47e-20

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 83.89  E-value: 5.47e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 19921130    142 LSIIKQRLEMYKQAEANAKTAGDSGKARRFGRGLKTLKDLHRQAAAGKSINVDDIPPEV 200
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
666-778 9.03e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 59.25  E-value: 9.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130   666 LEIVVVRGIsyNVAnPKD----VDTYVRVEfplLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKF 741
Cdd:pfam00168   3 LTVTVIEAK--NLP-PKDgngtSDPYVKVY---LLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAV--------LEI 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 19921130   742 EIYSRGGFLRsDTLIGTVNVKLQPLETKCEIHDTYDL 778
Cdd:pfam00168  69 EVYDYDRFGR-DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 666-768 4.27e-09

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: 54.42  E-value: 4.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130    666 LEIVVVRGISYNVANPKD-VDTYVRVEfpLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEIY 744
Cdd:smart00239   2 LTVKIISARNLPPKDKGGkSDPYVKVS--LDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAE--------LEIEVY 71

                           90       100
                   ....*....|....*....|....
gi 19921130    745 SRGGFLRsDTLIGTVNVKLQPLET 768
Cdd:smart00239  72 DKDRFGR-DDFIGQVTIPLSDLLL 94
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 666-778 7.97e-09

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: 53.61  E-value: 7.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 666 LEIVVV--RGISYNVANPKdVDTYVRVEFpllnDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEI 743
Cdd:cd00030   1 LRVTVIeaRNLPAKDLNGK-SDPYVKVSL----GGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDT--------LTVEV 67

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19921130 744 YSRGGFLRsDTLIGTVNVKLQPLETKCEIHD-TYDL 778
Cdd:cd00030  68 WDKDRFSK-DDFLGEVEIPLSELLDSGKEGElWLPL 102
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 681-786 1.06e-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: 45.62  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 681 PKDVDTYVRVEFPLlNDESFKTKtnVIRDTSSPDYDERFKVDIQRTNRQfqrifkrhgVKFEIYSRGGFlRSDTLIGTVN 760
Cdd:cd04044  21 GGTVDPYVTFSISN-RRELARTK--VKKDTSNPVWNETKYILVNSLTEP---------LNLTVYDFNDK-RKDKLIGTAE 87

                        90       100
                ....*....|....*....|....*..
gi 19921130 761 VKLQPLETKCEIHD-TYDLMDGRKQVG 786
Cdd:cd04044  88 FDLSSLLQNPEQENlTKNLLRNGKPVG 114
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 668-779 1.30e-04

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: 42.26  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 668 IVVVRGISYNVANPKD--VDTYVRVEfpLLNDESFKT--KTNVIRDTSSPDYDERFKVDIQRTnrQFQRIFKRHGVKfei 743
Cdd:cd04030  19 IVTVHKCRNLPPCDSSdiPDPYVRLY--LLPDKSKSTrrKTSVKKDNLNPVFDETFEFPVSLE--ELKRRTLDVAVK--- 91

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19921130 744 YSRGGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLM 779
Cdd:cd04030  92 NSKSFLSREKKLLGQVLIDLSDLDLSKGFTQWYDLT 127
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 685-791 2.72e-04

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A domains. 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 41.57  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 685 DTYVRVEfpLLNDESFKTKTNVIRDTSSPDYDERF------KVDIQRTNRQFQRIfkrhgvKFEIYSRggflrsDTLIGt 758
Cdd:cd08388  39 DPYVKLQ--LLPEKEHKVKTRVLRKTRNPVYDETFtfygipYNQLQDLSLHFAVL------SFDRYSR------DDVIG- 103

                        90       100       110
                ....*....|....*....|....*....|...
gi 19921130 759 vnvklqplETKCEIHDTYDLMDGRKQVGGKLEV 791
Cdd:cd08388 104 --------EVVCPLAGADLLNEGELLVSREIQP 128
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 664-791 2.04e-03

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: 38.80  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 664 SELEIVVVRGISYNVANPKDVDTYVRVefplLNDESFKTKTNVIRDTSSPDYDERFKVDIQ-RTNRQFqRIFKRHGvkfe 742
Cdd:cd04021   2 SQLQITVESAKLKSNSKSFKPDPYVEV----TVDGQPPKKTEVSKKTSNPKWNEHFTVLVTpQSTLEF-KVWSHHT---- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19921130 743 iysrggfLRSDTLIGTVNVKLQP-LET---KCE-IHDTYDLMDGRK---QVGGKLEV 791
Cdd:cd04021  73 -------LKADVLLGEASLDLSDiLKNhngKLEnVKLTLNLSSENKgssVKVGELTV 122
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
 700-798 2.58e-03

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 463310  Cd Length: 143  Bit Score: 39.15  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130   700 FKTKTNVIRDTSSPDYDE--RFKVdiqRTNRQFQRIFKRHGVKFEIY-SRGgflrSD-TLIGTVNVKLQPLETKCE--IH 773
Cdd:pfam11618  44 FETQTTPVVRGLNPFYDFtsQYKV---TVDDLFLQYLQTNSLTLELHqALG----VDfKTLAAAQLRLHGLLEDRGgrIH 116

                          90       100
                  ....*....|....*....|....*..
gi 19921130   774 DTYDL--MDGRKQVGGKLEVKIRVRNP 798
Cdd:pfam11618 117 GTVTLtgVEGEIQIIGTLEYWIRLRVP 143
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 685-765 3.99e-03

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. 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-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 38.01  E-value: 3.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 685 DTYVrvefpLLNDESFK---TKTNVIRDTSSPDYDERFKVDIQRTNRQFqrifkrhgVKFEIYSRgGFLRSDTLIGTVNV 761
Cdd:cd04043  23 DPYV-----TLVDTNGKrriAKTRTIYDTLNPRWDEEFELEVPAGEPLW--------ISATVWDR-SFVGKHDLCGRASL 88


                ....
gi 19921130 762 KLQP 765
Cdd:cd04043  89 KLDP 92
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 685-773 4.73e-03

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 38.01  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921130 685 DTYVRVEfpLLNDESFKTKTNVIRDTSSPDYDERFKVDIqrtnrQFQRIfKRHGVKFEIYSRGGFLRSDtLIGTVNVKLQ 764
Cdd:cd08390  37 DPFVKVC--LLPDERRSLQSKVKRKTQNPNFDETFVFQV-----SFKEL-QRRTLRLSVYDVDRFSRHC-IIGHVLFPLK 107


                ....*....
gi 19921130 765 PLETKCEIH 773
Cdd:cd08390 108 DLDLVKGGV 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH