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Conserved domains on  [gi|6324870|ref|NP_014939|]
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uncharacterized protein YOR296W [Saccharomyces cerevisiae S288C]

Protein Classification

C2 domain-containing protein( domain architecture ID 10134257)

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

CATH:  2.60.40.150
Gene Ontology:  GO:0005544|GO:0005509
PubMed:  8976547|9632630
SCOP:  3000965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 856-986 1.36e-54

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: 185.93  E-value: 1.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   856 QVYTLRIIGAENIKGFSKTGLSNTYVSMRNITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHPHSRlk 935
Cdd:cd04043    1 HLFTIRIVRAENLKADSSNGLSDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRSFVG-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6324870   936 nlaEDDLCGKANMKFTPRKLKDDGFPIDFSLTLNPQGTLYCQISLESEKID 986
Cdd:cd04043   79 ---KHDLCGRASLKLDPKRFGDDGLPREIWLDLDTQGRLLLRVSMEGERDD 126
 
Name Accession Description Interval E-value
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 856-986 1.36e-54

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: 185.93  E-value: 1.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   856 QVYTLRIIGAENIKGFSKTGLSNTYVSMRNITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHPHSRlk 935
Cdd:cd04043    1 HLFTIRIVRAENLKADSSNGLSDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRSFVG-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6324870   936 nlaEDDLCGKANMKFTPRKLKDDGFPIDFSLTLNPQGTLYCQISLESEKID 986
Cdd:cd04043   79 ---KHDLCGRASLKLDPKRFGDDGLPREIWLDLDTQGRLLLRVSMEGERDD 126
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 859-951 2.37e-12

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: 64.43  E-value: 2.37e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870      859 TLRIIGAENIKGFSKTGLSNTYVSMRNITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHphsrlKNLA 938
Cdd:smart00239    3 TVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDK-----DRFG 77

                            90
                    ....*....|...
gi 6324870      939 EDDLCGKANMKFT 951
Cdd:smart00239   78 RDDFIGQVTIPLS 90
C2 pfam00168
C2 domain;
859-968 6.88e-12

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 63.11  E-value: 6.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870     859 TLRIIGAENIKGFSKTGLSNTYVSMRnITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHphsrlKNLA 938
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNGTSDPYVKVY-LLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDY-----DRFG 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 6324870     939 EDDLCGKANMKFTPrklKDDGFPIDFSLTL 968
Cdd:pfam00168   78 RDDFIGEVRIPLSE---LDSGEGLDGWYPL 104
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
859-980 3.62e-03

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 41.67  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   859 TLRIIGAENIKGFSKTGLSNTYVSmrnITLQ-REIGTTKIVARSITPKWDEEFVFESPfGKSNDImFTIwhhpHSRLKNL 937
Cdd:COG5038 1043 TIMLRSGENLPSSDENGYSDPFVK---LFLNeKSVYKTKVVKKTLNPVWNEEFTIEVL-NRVKDV-LTI----NVNDWDS 1113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6324870   938 AE-DDLCGKANMkftPRKLKDDGFPIDFSLTLNPQGTLYCQISL 980
Cdd:COG5038 1114 GEkNDLLGTAEI---DLSKLEPGGTTNSNIPLDGKTFIVLDGTL 1154
 
Name Accession Description Interval E-value
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 856-986 1.36e-54

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: 185.93  E-value: 1.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   856 QVYTLRIIGAENIKGFSKTGLSNTYVSMRNITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHPHSRlk 935
Cdd:cd04043    1 HLFTIRIVRAENLKADSSNGLSDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRSFVG-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6324870   936 nlaEDDLCGKANMKFTPRKLKDDGFPIDFSLTLNPQGTLYCQISLESEKID 986
Cdd:cd04043   79 ---KHDLCGRASLKLDPKRFGDDGLPREIWLDLDTQGRLLLRVSMEGERDD 126
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 859-951 2.37e-12

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: 64.43  E-value: 2.37e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870      859 TLRIIGAENIKGFSKTGLSNTYVSMRNITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHphsrlKNLA 938
Cdd:smart00239    3 TVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDK-----DRFG 77

                            90
                    ....*....|...
gi 6324870      939 EDDLCGKANMKFT 951
Cdd:smart00239   78 RDDFIGQVTIPLS 90
C2 pfam00168
C2 domain;
859-968 6.88e-12

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 63.11  E-value: 6.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870     859 TLRIIGAENIKGFSKTGLSNTYVSMRnITLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHphsrlKNLA 938
Cdd:pfam00168    4 TVTVIEAKNLPPKDGNGTSDPYVKVY-LLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDY-----DRFG 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 6324870     939 EDDLCGKANMKFTPrklKDDGFPIDFSLTL 968
Cdd:pfam00168   78 RDDFIGEVRIPLSE---LDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 859-968 8.86e-12

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: 62.85  E-value: 8.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   859 TLRIIGAENIKGFSKTGLSNTYVSMRniTLQREIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHphsrlKNLA 938
Cdd:cd00030    2 RVTVIEARNLPAKDLNGKSDPYVKVS--LGGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDK-----DRFS 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 6324870   939 EDDLCGKAnmKFTPRKLKDDGFPIDFSLTL 968
Cdd:cd00030   75 KDDFLGEV--EIPLSELLDSGKEGELWLPL 102
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 859-948 9.71e-04

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 40.86  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   859 TLRIIGAENIKGFSKTGLSNTYVSMRNITLQR--EIGTTKIVARSITPKWDEEFVFESPFGKSNDIMFTIWHHPHSRlkn 936
Cdd:cd08405   18 TVNIIKARNLKAMDINGTSDPYVKVWLMYKDKrvEKKKTVIKKRTLNPVFNESFIFNIPLERLRETTLIITVMDKDR--- 94

                         90
                 ....*....|..
gi 6324870   937 LAEDDLCGKANM 948
Cdd:cd08405   95 LSRNDLIGKIYL 106
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
859-980 3.62e-03

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 41.67  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   859 TLRIIGAENIKGFSKTGLSNTYVSmrnITLQ-REIGTTKIVARSITPKWDEEFVFESPfGKSNDImFTIwhhpHSRLKNL 937
Cdd:COG5038 1043 TIMLRSGENLPSSDENGYSDPFVK---LFLNeKSVYKTKVVKKTLNPVWNEEFTIEVL-NRVKDV-LTI----NVNDWDS 1113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6324870   938 AE-DDLCGKANMkftPRKLKDDGFPIDFSLTLNPQGTLYCQISL 980
Cdd:COG5038 1114 GEkNDLLGTAEI---DLSKLEPGGTTNSNIPLDGKTFIVLDGTL 1154
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 859-951 4.05e-03

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; 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: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 38.70  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   859 TLRIIGAENIKGFSKTGLSNTYVSMRNITLQREigtTKIVARSITPKWDEEFVFESpFGKSNDIMFTIWHHphsrlknla 938
Cdd:cd04027    4 SITVVCAQGLIAKDKTGTSDPYVTVQVGKTKKR---TKTIPQNLNPVWNEKFHFEC-HNSSDRIKVRVWDE--------- 70

                         90
                 ....*....|...
gi 6324870   939 EDDLCGKANMKFT 951
Cdd:cd04027   71 DDDIKSRLKQKFT 83
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 857-973 7.54e-03

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 37.63  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324870   857 VYTLRIIGAENIKGFSKTGLSNTYVSMRNITLQREIGTTKIVARSITPKWDEEFvfespfgksndiMFTIwhhpHSRLKN 936
Cdd:cd04036    1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETF------------EFRI----QSQVKN 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6324870   937 LAE----------DDLCGKAnmKFTPRKLKdDGFPIDFSLTLNPQGT 973
Cdd:cd04036   65 VLEltvmdedyvmDDHLGTV--LFDVSKLK-LGEKVRVTFSLNPQGK 108
 
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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