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Conserved domains on  [gi|401709971|ref|NP_001257913|]
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coiled-coil and C2 domain-containing protein 1B [Rattus norvegicus]

Protein Classification

C2 domain-containing protein; copine family C2 domain-containing protein( domain architecture ID 10251568)

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; copine family C2 domain-containing protein similar to copine, which is a C2 domain-containing, calcium-dependent, phospholipid-binding protein that may function in membrane trafficking and other calcium-dependent processes

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); ...
 688-845 4.36e-85

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: 268.02  E-value: 4.36e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 688 LNSTEMHLIIVRGMNLPapPGVTPDDLDAFVRFEFHYPNsDQAQKSKTAVVKNTNSPEFEQVFKLNINRNHRGFRRVIQS 767
Cdd:cd08690    1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971 768 KGIKFEIFHKGSFFRSDKLVGTAHLKLERLEKECEIREIMEVLDGRKPTGGKLEVKVRLREPLSSQDVQMVTENWLVL 845
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
385-439 8.53e-18

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 77.72  E-value: 8.53e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 401709971   385 LDALQQRLNRYREAGIQARASGDERKARMHDRIAKQYQDAIRAHQAGRKVDFAEL 439
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSEL 55
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
280-337 1.72e-17

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 76.95  E-value: 1.72e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   280 ALLLARQREYKAAALSAKRAGDLDRARELMRIGKRFGTVLEALEKGQPVDLSGMPPAP 337
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
529-586 1.90e-17

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 76.95  E-value: 1.90e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   529 VTLLEARKLQYQRAALQAKRRQDLEQAKSHLRVAKSLEAQIIQARAGQPIDLSKVPSP 586
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPP 58
DM14 super family cl02734
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
169-226 3.97e-08

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


The actual alignment was detected with superfamily member smart00685:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 50.38  E-value: 3.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   169 ALLEERIQNYREAAASAKEAGEAAKARRCERGLKTLESQLATVRKGGKICEDEIPPPV 226
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 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); ...
 688-845 4.36e-85

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: 268.02  E-value: 4.36e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 688 LNSTEMHLIIVRGMNLPapPGVTPDDLDAFVRFEFHYPNsDQAQKSKTAVVKNTNSPEFEQVFKLNINRNHRGFRRVIQS 767
Cdd:cd08690    1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971 768 KGIKFEIFHKGSFFRSDKLVGTAHLKLERLEKECEIREIMEVLDGRKPTGGKLEVKVRLREPLSSQDVQMVTENWLVL 845
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
385-439 8.53e-18

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 77.72  E-value: 8.53e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 401709971   385 LDALQQRLNRYREAGIQARASGDERKARMHDRIAKQYQDAIRAHQAGRKVDFAEL 439
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSEL 55
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
280-337 1.72e-17

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 76.95  E-value: 1.72e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   280 ALLLARQREYKAAALSAKRAGDLDRARELMRIGKRFGTVLEALEKGQPVDLSGMPPAP 337
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
529-586 1.90e-17

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 76.95  E-value: 1.90e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   529 VTLLEARKLQYQRAALQAKRRQDLEQAKSHLRVAKSLEAQIIQARAGQPIDLSKVPSP 586
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPP 58
C2 pfam00168
C2 domain;
694-809 2.44e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 61.18  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971  694 HLIIVRGMNLPAPPGVTPddLDAFVRFEFHypnsDQAQKSKTAVVKNTNSPEFEQVFKLNINRNhrgfrrviQSKGIKFE 773
Cdd:pfam00168   4 TVTVIEAKNLPPKDGNGT--SDPYVKVYLL----DGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIE 69

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 401709971  774 IFHKGSFFRsDKLVGTAHLKLERLEKECEIREIMEV 809
Cdd:pfam00168  70 VYDYDRFGR-DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 693-803 2.86e-10

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: 57.88  E-value: 2.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971   693 MHLIIVRGMNLPAPPGvtPDDLDAFVRFEFhypNSDQAQKSKTAVVKNTNSPEFEQVFKLNINRNhrgfrrviQSKGIKF 772
Cdd:smart00239   2 LTVKIISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEI 68

                           90       100       110
                   ....*....|....*....|....*....|.
gi 401709971   773 EIFHKGSfFRSDKLVGTAHLKLERLEKECEI 803
Cdd:smart00239  69 EVYDKDR-FGRDDFIGQVTIPLSDLLLGGRH 98
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
169-226 3.97e-08

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 50.38  E-value: 3.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   169 ALLEERIQNYREAAASAKEAGEAAKARRCERGLKTLESQLATVRKGGKICEDEIPPPV 226
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
713-817 1.58e-03

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 42.44  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971  713 DLDAFVRFEFHypnsdQAQKSKTAVVKNTNSPEFEQVFKLNINRnhrgfrrviQSKGIKFEIFHKGSFfRSDKLVGTAHL 792
Cdd:COG5038   458 TVDPYITVTFS-----DRVIGKTRVKKNTLNPVWNETFYILLNS---------FTDPLNLSLYDFNSF-KSDKVVGSTQL 522

                          90       100
                  ....*....|....*....|....*.
gi 401709971  793 KLERLEKECEIR-EIMEVLDGRKPTG 817
Cdd:COG5038   523 DLALLHQNPVKKnELYEFLRNTKNVG 548
 
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); ...
 688-845 4.36e-85

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: 268.02  E-value: 4.36e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 688 LNSTEMHLIIVRGMNLPapPGVTPDDLDAFVRFEFHYPNsDQAQKSKTAVVKNTNSPEFEQVFKLNINRNHRGFRRVIQS 767
Cdd:cd08690    1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971 768 KGIKFEIFHKGSFFRSDKLVGTAHLKLERLEKECEIREIMEVLDGRKPTGGKLEVKVRLREPLSSQDVQMVTENWLVL 845
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
385-439 8.53e-18

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 77.72  E-value: 8.53e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 401709971   385 LDALQQRLNRYREAGIQARASGDERKARMHDRIAKQYQDAIRAHQAGRKVDFAEL 439
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSEL 55
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
280-337 1.72e-17

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 76.95  E-value: 1.72e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   280 ALLLARQREYKAAALSAKRAGDLDRARELMRIGKRFGTVLEALEKGQPVDLSGMPPAP 337
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
529-586 1.90e-17

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 76.95  E-value: 1.90e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   529 VTLLEARKLQYQRAALQAKRRQDLEQAKSHLRVAKSLEAQIIQARAGQPIDLSKVPSP 586
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPP 58
C2 pfam00168
C2 domain;
694-809 2.44e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 61.18  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971  694 HLIIVRGMNLPAPPGVTPddLDAFVRFEFHypnsDQAQKSKTAVVKNTNSPEFEQVFKLNINRNhrgfrrviQSKGIKFE 773
Cdd:pfam00168   4 TVTVIEAKNLPPKDGNGT--SDPYVKVYLL----DGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIE 69

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 401709971  774 IFHKGSFFRsDKLVGTAHLKLERLEKECEIREIMEV 809
Cdd:pfam00168  70 VYDYDRFGR-DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 693-805 9.17e-11

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: 59.39  E-value: 9.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 693 MHLIIVRGMNLPAPPgvTPDDLDAFVRFEFhypnsDQAQKSKTAVVKNTNSPEFEQVFKLNINRNhrgfrrviQSKGIKF 772
Cdd:cd00030    1 LRVTVIEARNLPAKD--LNGKSDPYVKVSL-----GGKQKFKTKVVKNTLNPVWNETFEFPVLDP--------ESDTLTV 65

                         90       100       110
                 ....*....|....*....|....*....|...
gi 401709971 773 EIFHKGSFFRsDKLVGTAHLKLERLEKECEIRE 805
Cdd:cd00030   66 EVWDKDRFSK-DDFLGEVEIPLSELLDSGKEGE 97
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 693-803 2.86e-10

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: 57.88  E-value: 2.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971   693 MHLIIVRGMNLPAPPGvtPDDLDAFVRFEFhypNSDQAQKSKTAVVKNTNSPEFEQVFKLNINRNhrgfrrviQSKGIKF 772
Cdd:smart00239   2 LTVKIISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEI 68

                           90       100       110
                   ....*....|....*....|....*....|.
gi 401709971   773 EIFHKGSfFRSDKLVGTAHLKLERLEKECEI 803
Cdd:smart00239  69 EVYDKDR-FGRDDFIGQVTIPLSDLLLGGRH 98
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
169-226 3.97e-08

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 50.38  E-value: 3.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 401709971   169 ALLEERIQNYREAAASAKEAGEAAKARRCERGLKTLESQLATVRKGGKICEDEIPPPV 226
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 681-797 9.48e-05

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs 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). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 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. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 42.91  E-value: 9.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 681 TVRIFSelnstemhliivrGMNLPAPPGVTPDDLDAFVRFEFHYPNSDQAQKSKTAVVK-NTNSPEFEQVFKLNINRNHR 759
Cdd:cd00275    5 TIKIIS-------------GQQLPKPKGDKGSIVDPYVEVEIHGLPADDSAKFKTKVVKnNGFNPVWNETFEFDVTVPEL 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 401709971 760 GFrrviqskgIKFEIFHKGSFfrSDKLVGTAHLKLERL 797
Cdd:cd00275   72 AF--------LRFVVYDEDSG--DDDFLGQACLPLDSL 99
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 731-789 3.00e-04

C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175978 [Multi-domain]  Cd Length: 111  Bit Score: 41.02  E-value: 3.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 401709971 731 QKSKTAVVKNTNSPEFEQVFKLNINRNhrgfRRVIQSKGIKFEIFHKGSfFRSDKLVGT 789
Cdd:cd04011   32 QKKYTSVKKGTNCPFYNEYFFFNFHES----PDELFDKIIKISVYDSRS-LRSDTLIGS 85
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 697-813 3.21e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 41.20  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 697 IVRGMNLPAPPGVTpddlDAFVRFEFHYPnsdqAQKSKTAVVKNTNSPEFEQVFKLNINRNhrgfrrviqSKGIKFEIFH 776
Cdd:cd08678    5 NIKANGLSEAAGSS----NPYCVLEMDEP----PQKYQSSTQKNTSNPFWDEHFLFELSPN---------SKELLFEVYD 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 401709971 777 KGSFFRSdKLVGTAHLKLERLEKECEIREIMEvLDGR 813
Cdd:cd08678   68 NGKKSDS-KFLGLAIVPFDELRKNPSGRQIFP-LQGR 102
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 695-786 3.74e-04

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 41.41  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 695 LIIVRGMNLPAPPGVTPddLDAFVRFEFHYPNSDQAQKsKTAVVKNTNSPEFEQVFKLNINRNHrgfrrvIQSKGIKFEI 774
Cdd:cd00276   18 VVVLKARNLPPSDGKGL--SDPYVKVSLLQGGKKLKKK-KTSVKKGTLNPVFNEAFSFDVPAEQ------LEEVSLVITV 88

                         90
                 ....*....|..
gi 401709971 775 FHKGSFFRSDKL 786
Cdd:cd00276   89 VDKDSVGRNEVI 100
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 697-794 7.90e-04

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: 40.32  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 697 IVRGMNLPAPPGVtpDDLDAFVRFefhypnSDQAQKS---KTAVVKNTNSPEFEQVFKLNINRNhrgfrrviQSKGIKFE 773
Cdd:cd04043    7 IVRAENLKADSSN--GLSDPYVTL------VDTNGKRriaKTRTIYDTLNPRWDEEFELEVPAG--------EPLWISAT 70

                         90       100
                 ....*....|....*....|.
gi 401709971 774 IFHKgSFFRSDKLVGTAHLKL 794
Cdd:cd04043   71 VWDR-SFVGKHDLCGRASLKL 90
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 734-794 8.96e-04

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: 39.95  E-value: 8.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401709971 734 KTAVVKNTNSPEFEQVFKLNINRnhrgfrrviQSKgIKFEIFHKGSfFRSDKLVGTAHLKL 794
Cdd:cd04021   37 KTEVSKKTSNPKWNEHFTVLVTP---------QST-LEFKVWSHHT-LKADVLLGEASLDL 86
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
713-817 1.58e-03

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 42.44  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971  713 DLDAFVRFEFHypnsdQAQKSKTAVVKNTNSPEFEQVFKLNINRnhrgfrrviQSKGIKFEIFHKGSFfRSDKLVGTAHL 792
Cdd:COG5038   458 TVDPYITVTFS-----DRVIGKTRVKKNTLNPVWNETFYILLNS---------FTDPLNLSLYDFNSF-KSDKVVGSTQL 522

                          90       100
                  ....*....|....*....|....*.
gi 401709971  793 KLERLEKECEIR-EIMEVLDGRKPTG 817
Cdd:COG5038   523 DLALLHQNPVKKnELYEFLRNTKNVG 548
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 713-817 2.07e-03

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: 39.08  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 713 DLDAFVRFEFHYPNSDqaqkSKTAVVKNTNSPEFEQVFKLNIN--RNHrgfrrviqskgIKFEIFHKGSFfRSDKLVGTA 790
Cdd:cd04044   23 TVDPYVTFSISNRREL----ARTKVKKDTSNPVWNETKYILVNslTEP-----------LNLTVYDFNDK-RKDKLIGTA 86

                         90       100
                 ....*....|....*....|....*...
gi 401709971 791 HLKLERLEKECEIREI-MEVLDGRKPTG 817
Cdd:cd04044   87 EFDLSSLLQNPEQENLtKNLLRNGKPVG 114
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 689-794 4.10e-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: 38.02  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709971 689 NSTEMHLIIV--RGMNLPAPpgvTPDDL-DAFVRFEFhYPNSDQAQKSKTAVVKNTNSPEFEQVFKLNI---NRNHRGFR 762
Cdd:cd04030   12 SSQRQKLIVTvhKCRNLPPC---DSSDIpDPYVRLYL-LPDKSKSTRRKTSVKKDNLNPVFDETFEFPVsleELKRRTLD 87

                         90       100       110
                 ....*....|....*....|....*....|..
gi 401709971 763 RVIQSkgikfeifHKGSFFRSDKLVGTAHLKL 794
Cdd:cd04030   88 VAVKN--------SKSFLSREKKLLGQVLIDL 111
 
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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