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Conserved domains on  [gi|755554899|ref|XP_011244411|]
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C2 domain-containing protein 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMP_C2CD2 cd21682
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 53-229 3.91e-91

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2 (C2CD2); C2CD2, also called transmembrane protein 24-like (TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2, which may be implicated in lipid transport.


:

Pssm-ID: 439238  Cd Length: 175  Bit Score: 281.06  E-value: 3.91e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899  53 ESDTLLSWILTRDSWGNQWQAAWVTALNYEAEKRGGPLRLSFQKDPrPQSLQLTVEKVSSVVKSTQEKVVICHVVGETLQ 132
Cdd:cd21682    1 EADALLSWALSLKSWRSQWRRAWVTALNEEARKRGGPLLLTFEEDG-LQQLELVVSQVSSFVKSAQEKVVSCQVVGEKLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 133 FLVSAGPASATGSECQLYDVHLSPFHLKVEFHMEEKREDIQIRWSFTHVPETAIKIQPQAPGEQAlGVNMLSEALEDLFK 212
Cdd:cd21682   80 FSVSAAPASPTAAGPQLYSVKLSPLHLQLELHMKEKREDIQVSWSFSHLDETNLQVQPKATQEVD-ETSASSEALKDILK 158

                        170
                 ....*....|....*..
gi 755554899 213 HLVNAASPSVFLSTKPT 229
Cdd:cd21682  159 QLLCSASPSVVLSTRPA 175
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 260-385 5.54e-39

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd08678:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 126  Bit Score: 140.19  E-value: 5.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 260 LQVKNIRVSLINHpGASGLSHVCVAQLNDPEQRFISTLVRNTTDLSWEEEFTFELNAKSKELVLQISQDGCSSE-GLLGI 338
Cdd:cd08678    1 LLVKNIKANGLSE-AAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSDsKFLGL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755554899 339 ATIHLDLFRKQPNGPQTFRLISGTEPDSLVLGSVTAEFSYVEPGELK 385
Cdd:cd08678   80 AIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP 126
 
Name Accession Description Interval E-value
SMP_C2CD2 cd21682
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 53-229 3.91e-91

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2 (C2CD2); C2CD2, also called transmembrane protein 24-like (TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2, which may be implicated in lipid transport.


Pssm-ID: 439238  Cd Length: 175  Bit Score: 281.06  E-value: 3.91e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899  53 ESDTLLSWILTRDSWGNQWQAAWVTALNYEAEKRGGPLRLSFQKDPrPQSLQLTVEKVSSVVKSTQEKVVICHVVGETLQ 132
Cdd:cd21682    1 EADALLSWALSLKSWRSQWRRAWVTALNEEARKRGGPLLLTFEEDG-LQQLELVVSQVSSFVKSAQEKVVSCQVVGEKLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 133 FLVSAGPASATGSECQLYDVHLSPFHLKVEFHMEEKREDIQIRWSFTHVPETAIKIQPQAPGEQAlGVNMLSEALEDLFK 212
Cdd:cd21682   80 FSVSAAPASPTAAGPQLYSVKLSPLHLQLELHMKEKREDIQVSWSFSHLDETNLQVQPKATQEVD-ETSASSEALKDILK 158

                        170
                 ....*....|....*..
gi 755554899 213 HLVNAASPSVFLSTKPT 229
Cdd:cd21682  159 QLLCSASPSVVLSTRPA 175
SMP_C2CD2L pfam18696
Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain ...
 71-222 1.03e-73

Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain found in phospholipid transfer proteins such as C2CD2L-like (also known as TMEM24). The TMEM24-SMP domain is shown to bind glycerolipids with a preference for phosphatidylinositol (PI).The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and hence insulin secretion. The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP for (tubular lipid-binding proteins) it adopts TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.


Pssm-ID: 465835  Cd Length: 152  Bit Score: 234.85  E-value: 1.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899   71 WQAAWVTALNYEAEKRGGPLRLSFQKDPRPQSLQLTVEKVSSVVKSTQEKVVICHVVGETLQFLVSAGPASATGSECQLY 150
Cdd:pfam18696   1 WQRAWVRALNEEACRRGGPLQLTFEEDGLQQPLELAVSQVSSFDKSAQEKVVSCHVVGEALQFPVSVTQQSPAAVSPQTY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755554899  151 DVHLSPFHLKVEFHMEEKREDIQIRWSFTHVPETAIKIQPQAPGEQALGVNMLSEALEDLFKHLVNAASPSV 222
Cdd:pfam18696  81 QVTLSPLHLQLELHMEEKEEDIQISWSFSHLPELSLQVTPKAQQEQVNETAAVSETLKDLLKDLLSSASPSV 152
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 260-385 5.54e-39

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: 140.19  E-value: 5.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 260 LQVKNIRVSLINHpGASGLSHVCVAQLNDPEQRFISTLVRNTTDLSWEEEFTFELNAKSKELVLQISQDGCSSE-GLLGI 338
Cdd:cd08678    1 LLVKNIKANGLSE-AAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSDsKFLGL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755554899 339 ATIHLDLFRKQPNGPQTFRLISGTEPDSLVLGSVTAEFSYVEPGELK 385
Cdd:cd08678   80 AIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP 126
C2 pfam00168
C2 domain;
282-358 2.47e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.85  E-value: 2.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755554899  282 CVAQLNDPEQRFISTLVRNTTDLSWEEEFTFEL-NAKSKELVLQI-SQDGCSSEGLLGIATIHLDLFRKQPNGPQTFRL 358
Cdd:pfam00168  26 VKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVpDPENAVLEIEVyDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 259-341 6.52e-03

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: 36.70  E-value: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899   259 KLQVKNIRVSLINHPGASGLS--HVCVAQLNDPEQRFISTLVRNTTDLSWEEEFTFELN-AKSKELVLQI-SQDGCSSEG 334
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSdpYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPpPELAELEIEVyDKDRFGRDD 80


                   ....*..
gi 755554899   335 LLGIATI 341
Cdd:smart00239  81 FIGQVTI 87
 
Name Accession Description Interval E-value
SMP_C2CD2 cd21682
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 53-229 3.91e-91

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2 (C2CD2); C2CD2, also called transmembrane protein 24-like (TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2, which may be implicated in lipid transport.


Pssm-ID: 439238  Cd Length: 175  Bit Score: 281.06  E-value: 3.91e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899  53 ESDTLLSWILTRDSWGNQWQAAWVTALNYEAEKRGGPLRLSFQKDPrPQSLQLTVEKVSSVVKSTQEKVVICHVVGETLQ 132
Cdd:cd21682    1 EADALLSWALSLKSWRSQWRRAWVTALNEEARKRGGPLLLTFEEDG-LQQLELVVSQVSSFVKSAQEKVVSCQVVGEKLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 133 FLVSAGPASATGSECQLYDVHLSPFHLKVEFHMEEKREDIQIRWSFTHVPETAIKIQPQAPGEQAlGVNMLSEALEDLFK 212
Cdd:cd21682   80 FSVSAAPASPTAAGPQLYSVKLSPLHLQLELHMKEKREDIQVSWSFSHLDETNLQVQPKATQEVD-ETSASSEALKDILK 158

                        170
                 ....*....|....*..
gi 755554899 213 HLVNAASPSVFLSTKPT 229
Cdd:cd21682  159 QLLCSASPSVVLSTRPA 175
SMP_C2CD2L pfam18696
Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain ...
 71-222 1.03e-73

Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain found in phospholipid transfer proteins such as C2CD2L-like (also known as TMEM24). The TMEM24-SMP domain is shown to bind glycerolipids with a preference for phosphatidylinositol (PI).The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and hence insulin secretion. The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP for (tubular lipid-binding proteins) it adopts TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.


Pssm-ID: 465835  Cd Length: 152  Bit Score: 234.85  E-value: 1.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899   71 WQAAWVTALNYEAEKRGGPLRLSFQKDPRPQSLQLTVEKVSSVVKSTQEKVVICHVVGETLQFLVSAGPASATGSECQLY 150
Cdd:pfam18696   1 WQRAWVRALNEEACRRGGPLQLTFEEDGLQQPLELAVSQVSSFDKSAQEKVVSCHVVGEALQFPVSVTQQSPAAVSPQTY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755554899  151 DVHLSPFHLKVEFHMEEKREDIQIRWSFTHVPETAIKIQPQAPGEQALGVNMLSEALEDLFKHLVNAASPSV 222
Cdd:pfam18696  81 QVTLSPLHLQLELHMEEKEEDIQISWSFSHLPELSLQVTPKAQQEQVNETAAVSETLKDLLKDLLSSASPSV 152
SMP_C2CD2-like cd21664
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 54-229 5.33e-45

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2-like (C2CD2L) and similar proteins; This family includes C2 domain-containing protein 2 (C2CD2) and C2CD2-like (C2CD2L). C2CD2 (also called transmembrane protein 24-like or TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also called transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum (ER) to the cell membrane. It is a Ca2+-regulated component of ER-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2 and C2CD2L which binds glycerolipids with a preference for phosphatidylinositol (PI). The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis; hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and subsequent insulin secretion.


Pssm-ID: 439224  Cd Length: 175  Bit Score: 158.67  E-value: 5.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899  54 SDTLLSWILTRDSWGNQWQAAWVTALNYEAEKRGGPLRLSFQKDPrPQSLQLTVEKVSSVVKSTQEKVVICHVVGETLQF 133
Cdd:cd21664    2 LNSVLNWIYTQYCNTPELVEAWLKALNEQARRAGSSVQVTFERIQ-SGSLPPKFTHVSTVAEPNDSLVVTCQVESEGLRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 134 LVSAGPASATGSECQLYDVHLSPFHLKVEFHMEEKREDIQIRWSFTHVPETAIKIQPQAPGEQALGVNMLsEALEDLFKH 213
Cdd:cd21664   81 QVFATQQTAQSVKLSNCDVSVTKLSGKLRCHGRTLGEELQISVSFEDRPDLKLNIKPKNGSPTAEDSVDL-DVVEEIVRN 159

                        170
                 ....*....|....*.
gi 755554899 214 LVNAASPSVFLSTKPT 229
Cdd:cd21664  160 AIASATTTFVLPTQAT 175
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 260-385 5.54e-39

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: 140.19  E-value: 5.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 260 LQVKNIRVSLINHpGASGLSHVCVAQLNDPEQRFISTLVRNTTDLSWEEEFTFELNAKSKELVLQISQDGCSSE-GLLGI 338
Cdd:cd08678    1 LLVKNIKANGLSE-AAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSDsKFLGL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755554899 339 ATIHLDLFRKQPNGPQTFRLISGTEPDSLVLGSVTAEFSYVEPGELK 385
Cdd:cd08678   80 AIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP 126
SMP_C2CD2L cd21683
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 57-209 1.96e-16

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2-like (C2CD2L); C2CD2L, also called phospholipid transfer protein C2CD2L, or C2CD2-like, or transmembrane protein 24 (TMEM24), is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2L, which may be implicated in lipid transport.


Pssm-ID: 439239  Cd Length: 177  Bit Score: 77.82  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899  57 LLSWILTRDSWGNQWQAAWVTALNYEAEKRGGPLRLSFQKDPR-PQSLQltVEKVSSVVKSTQEKVVICHVVGETLQFLV 135
Cdd:cd21683    5 LLTSLFAFKSFRENWQRAWVRALNEQACRNGSSLQITFEESPQlPASAS--ISHVTCTDQSDHSMVLHCNLSADAVKFPV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755554899 136 SAGPASATGSECQLYDVHLSPFHLKVEFHMEE-KREDIQIRWSFTHVPETAI----KIQPQAPGEQALGVNMLSEALED 209
Cdd:cd21683   83 SVTQQSPAAVSMDTYQVTLAPLQAQVEVCLEEvENEGLLVSWTFKDRPDLSLtvtpRQQQQEGNEGKADLSTIQDLIED 161
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 260-358 2.40e-06

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 46.68  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899 260 LQVKNIRVSLINHPGASGLSHV-CVAQLnDPEQRFISTLVRNTTDLSWEEEFTFEL-NAKSKELVLQI-SQDGCSSEGLL 336
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPyVKVSL-GGKQKFKTKVVKNTLNPVWNETFEFPVlDPESDTLTVEVwDKDRFSKDDFL 79

                         90       100
                 ....*....|....*....|...
gi 755554899 337 GIATIHL-DLFRKQPNGPQTFRL 358
Cdd:cd00030   80 GEVEIPLsELLDSGKEGELWLPL 102
C2 pfam00168
C2 domain;
282-358 2.47e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.85  E-value: 2.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755554899  282 CVAQLNDPEQRFISTLVRNTTDLSWEEEFTFEL-NAKSKELVLQI-SQDGCSSEGLLGIATIHLDLFRKQPNGPQTFRL 358
Cdd:pfam00168  26 VKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVpDPENAVLEIEVyDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 259-341 6.52e-03

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: 36.70  E-value: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755554899   259 KLQVKNIRVSLINHPGASGLS--HVCVAQLNDPEQRFISTLVRNTTDLSWEEEFTFELN-AKSKELVLQI-SQDGCSSEG 334
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSdpYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPpPELAELEIEVyDKDRFGRDD 80


                   ....*..
gi 755554899   335 LLGIATI 341
Cdd:smart00239  81 FIGQVTI 87
 
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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