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Conserved domains on  [gi|2065208889|ref|NP_001382399|]
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cytosolic phospholipase A2 epsilon isoform 4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 284-826 0e+00

Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans.


:

Pssm-ID: 132840 [Multi-domain]  Cd Length: 541  Bit Score: 917.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 284 MKSSPCSDTLDVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKL 363
Cdd:cd07201     1 LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 364 NFLDASTYITGLSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFW 443
Cdd:cd07201    81 GLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 444 GKLIEYSLGDKKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMG 523
Cdd:cd07201   161 GLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFMG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 524 RLMKRIPEPEMCYMLGLWSSIFSLNLLDAWNLSHTSEEFFYRWTRERLHDIEDDPILPEIPrcddNPLETTVVIPTTWLS 603
Cdd:cd07201   241 RLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFWHRWTRDKVNDIEDEPPLPPRP----PERLTTLLTPGGPLS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 604 NTFREILTRRPFVSEFHNFLYGMQLHTDYLQNRQFSMWKDTVLDTFPNQLTQFAKHLNLLDTAFFVNSSYAPLLRPERKV 683
Cdd:cd07201   317 QAFRDFLTSRPTVSQYFNFLRGLQLHNDYLENKGFSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKV 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 684 DLIIHLNYCAGSQTKPLKQTCEYCTEQKIPFPSFSILEDDN-SLKECYVMENPQEPDAPIVAYFPLISDTFQKYKAPGVE 762
Cdd:cd07201   397 DVILSLNYSLGSQFEPLKQASEYCSEQGIPFPKIELSPEDQeNLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVE 476

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208889 763 RSPDELELGQLNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALRLAMEKKRMR 826
Cdd:cd07201   477 RSPEEMAQGGVDVSSSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAVERKKQR 540
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 38-146 8.32e-49

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: 168.21  E-value: 8.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLtQND 117
Cdd:cd04036     1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYV-MDD 79

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 118 HLLTVLYDLSKLCLRNKTHVKFPLNPEGM 146
Cdd:cd04036    80 HLGTVLFDVSKLKLGEKVRVTFSLNPQGK 108
cPLA2_C2 pfam18695
Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a ...
 178-285 1.01e-35

Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking.


:

Pssm-ID: 465834  Cd Length: 111  Bit Score: 130.84  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 178 CLEVHAESRRPRKRKKNKDLLVMVTDSFENTQRVPPCQEPCYPNSACFHYPKYSQPQLYAEAPKSHCNFRLCCCG-THRN 256
Cdd:pfam18695   1 CLEVQVDSRGSKKEQGKKDLQLTVPGSYEGTQTISLGPEPGCPDPFCFHYPKYWEPELHVELPKSSVLQSGWNSDlEKET 80

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 257 DPVCQPLNCLSDGQVTTLPVGENYELHMK 285
Cdd:pfam18695  81 SKLTVPLKSLPLGQEVTVPLPEGQELHLR 109
 
Name Accession Description Interval E-value
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 284-826 0e+00

Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans.


Pssm-ID: 132840 [Multi-domain]  Cd Length: 541  Bit Score: 917.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 284 MKSSPCSDTLDVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKL 363
Cdd:cd07201     1 LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 364 NFLDASTYITGLSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFW 443
Cdd:cd07201    81 GLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 444 GKLIEYSLGDKKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMG 523
Cdd:cd07201   161 GLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFMG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 524 RLMKRIPEPEMCYMLGLWSSIFSLNLLDAWNLSHTSEEFFYRWTRERLHDIEDDPILPEIPrcddNPLETTVVIPTTWLS 603
Cdd:cd07201   241 RLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFWHRWTRDKVNDIEDEPPLPPRP----PERLTTLLTPGGPLS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 604 NTFREILTRRPFVSEFHNFLYGMQLHTDYLQNRQFSMWKDTVLDTFPNQLTQFAKHLNLLDTAFFVNSSYAPLLRPERKV 683
Cdd:cd07201   317 QAFRDFLTSRPTVSQYFNFLRGLQLHNDYLENKGFSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKV 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 684 DLIIHLNYCAGSQTKPLKQTCEYCTEQKIPFPSFSILEDDN-SLKECYVMENPQEPDAPIVAYFPLISDTFQKYKAPGVE 762
Cdd:cd07201   397 DVILSLNYSLGSQFEPLKQASEYCSEQGIPFPKIELSPEDQeNLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVE 476

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208889 763 RSPDELELGQLNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALRLAMEKKRMR 826
Cdd:cd07201   477 RSPEEMAQGGVDVSSSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAVERKKQR 540
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 38-146 8.32e-49

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: 168.21  E-value: 8.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLtQND 117
Cdd:cd04036     1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYV-MDD 79

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 118 HLLTVLYDLSKLCLRNKTHVKFPLNPEGM 146
Cdd:cd04036    80 HLGTVLFDVSKLKLGEKVRVTFSLNPQGK 108
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 280-767 2.09e-45

Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.


Pssm-ID: 214474  Cd Length: 549  Bit Score: 171.84  E-value: 2.09e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  280 YELHMKSSPCSDTLdVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLE--EGLHED-----EVPIIAIMATGGGTRSMVS 352
Cdd:smart00022  14 YAPYNVSCPSDIPL-VRFSMGLSDNETEFLQKRKDYTNEAMKSFLGRAnsNFLDSSllnssDVPKIAIAGSGGGFRAMVG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  353 LYG------------HLLGLqklnfLDASTYITGLSGATWTMATLYSDPEWSSKNLETV--VFEARRHVVKDKMPALFPD 418
Cdd:smart00022  93 GAGvlkamdnrtdghGLGGL-----LQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEInsEWMFSVSINNPGINLLLTA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  419 QLYK-WREDLQKHSQEGYKTTFTDFWGKLIEYSLGDK-----------KNECKLSDqraalcrGQNPLPIYLTINVKDDV 486
Cdd:smart00022 168 QFYKsIVDAVWKKKDAGFNISLTDIWGRALSYNLFDSlggpnytlsslRDQEKFQN-------AEMPLPIFVADGRKPGE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  487 SNQDFREW-FEFSPYEVGM--QKYGAFIPSELFGSEFFMGRLMKRIPEPEMCYMLGLWSSIFSL---NLLDAWNLSHTSE 560
Cdd:smart00022 241 SVINFNDTvFEFSPFEFGSwdPKLNAFMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGTSSSlfnRFLLVLSNSTMEE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  561 EFFYRWTRERLHDI--EDDPILPEIPrcddNPLETtvvipTTWLSNTFREILTRrpfvSEFHNFLYGMQLHTDY----LQ 634
Cdd:smart00022 321 SLIKIIIKHILKDLssDSDDIAIYPP----NPFKD-----DAYVQRMLTNSLGD----SDLLNLVDGGEDGENIplspLL 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  635 NRQFSMWKDTVLDT-------FPN--QLTQ-FAKHLNllDTAFFVNSSYAPLLRPERKVDLIIHLNY----CAGSQTK-- 698
Cdd:smart00022 388 QPERSVDVIFAVDAsadtdefWPNgsSLVKtYERHVV--DQGLTFNLPFPYVPDTQTFVNLGLSTKPtffgCDSSNLTyi 465

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208889  699 -PLKQ---TCEYCTEQKIPFPSFSILEDDNS--LKECYV---MENPQEPDAPIVayFPLISDTFQKYKAPGVERSPDE 767
Cdd:smart00022 466 pPLVVylpNEKWAYNSNISTFKISYSVFEREglIKNGYEfatVNNSTDDDCFIH--CVACAIIFRKQEAPNVTLPSEC 541
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 338-577 5.60e-36

Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain pfam00168. Phospholipase B enzymes catalyze the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.


Pssm-ID: 366778  Cd Length: 490  Bit Score: 142.89  E-value: 5.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 338 IAIMATGGGTRSMVSLYG-------------HLLGLqklnfLDASTYITGLSGATWTMATLYSDpEWSS-----KNLETV 399
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGvlaaldnrtdnetGLGGL-----LQSATYLAGLSGGSWLVGSLAVN-NFTSvqdfpDKPEDI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 400 VFEARRHVVKDKMPALFPDQLYKWR---EDLQKHSQEGYKTTFTDFWGKLIEYSLGDKKNE---CKLSDQRAA--LCRGQ 471
Cdd:pfam01735  75 SIWDLNHSIFNPGGLNIPQNIKRYDdivDAVWKKKNAGFNVSLTDIWGRALSYTLIPSLRGgpnYTWSSLRDAewFQNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 472 NPLPIYLTINVKDDVSNQDFR-EWFEFSPYEVG--MQKYGAFIPSELFGSEFFMGRLMKRIPEPE----MCYMLGLWSSI 544
Cdd:pfam01735 155 MPFPIIVADGRKPGTTVINLNaTVFEFSPYEFGswDPTLNSFTPTEYLGTKFFNGTPVKKGKCVPgfdnAGFVMGTSSTL 234

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2065208889 545 FSLNLLdAWNLSHTSEEFFYRWTRERLHDIEDD 577
Cdd:pfam01735 235 FNQFLL-VINSTSSLPSFLNIIIKHILKDLSED 266
cPLA2_C2 pfam18695
Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a ...
 178-285 1.01e-35

Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking.


Pssm-ID: 465834  Cd Length: 111  Bit Score: 130.84  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 178 CLEVHAESRRPRKRKKNKDLLVMVTDSFENTQRVPPCQEPCYPNSACFHYPKYSQPQLYAEAPKSHCNFRLCCCG-THRN 256
Cdd:pfam18695   1 CLEVQVDSRGSKKEQGKKDLQLTVPGSYEGTQTISLGPEPGCPDPFCFHYPKYWEPELHVELPKSSVLQSGWNSDlEKET 80

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 257 DPVCQPLNCLSDGQVTTLPVGENYELHMK 285
Cdd:pfam18695  81 SKLTVPLKSLPLGQEVTVPLPEGQELHLR 109
C2 pfam00168
C2 domain;
37-141 3.94e-20

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 86.22  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  37 HLLTVRIIGMKNVRQADILSQTDCFVTLWLpTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQN 116
Cdd:pfam00168   1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRFGRD 79

                          90       100
                  ....*....|....*....|....*
gi 2065208889 117 DHLLTVLYDLSKLCLRNKTHVKFPL 141
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 38-135 2.00e-19

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: 84.08  E-value: 2.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889   38 LLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQND 117
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGRDD 80

                           90
                   ....*....|....*...
gi 2065208889  118 HLLTVLYDLSKLCLRNKT 135
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRH 98
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
39-145 3.30e-10

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 64.01  E-value: 3.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889   39 LTVRIIGMKNVRQADILSQTDCFVTLWLptASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDH 118
Cdd:COG5038   1042 LTIMLRSGENLPSSDENGYSDPFVKLFL--NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGEKNDL 1119

                           90       100
                   ....*....|....*....|....*..
gi 2065208889  119 LLTVLYDLSKLCLRNKTHVKFPLNPEG 145
Cdd:COG5038   1120 LGTAEIDLSKLEPGGTTNSNIPLDGKT 1146
 
Name Accession Description Interval E-value
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 284-826 0e+00

Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans.


Pssm-ID: 132840 [Multi-domain]  Cd Length: 541  Bit Score: 917.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 284 MKSSPCSDTLDVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKL 363
Cdd:cd07201     1 LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 364 NFLDASTYITGLSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFW 443
Cdd:cd07201    81 GLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 444 GKLIEYSLGDKKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMG 523
Cdd:cd07201   161 GLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFMG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 524 RLMKRIPEPEMCYMLGLWSSIFSLNLLDAWNLSHTSEEFFYRWTRERLHDIEDDPILPEIPrcddNPLETTVVIPTTWLS 603
Cdd:cd07201   241 RLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFWHRWTRDKVNDIEDEPPLPPRP----PERLTTLLTPGGPLS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 604 NTFREILTRRPFVSEFHNFLYGMQLHTDYLQNRQFSMWKDTVLDTFPNQLTQFAKHLNLLDTAFFVNSSYAPLLRPERKV 683
Cdd:cd07201   317 QAFRDFLTSRPTVSQYFNFLRGLQLHNDYLENKGFSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKV 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 684 DLIIHLNYCAGSQTKPLKQTCEYCTEQKIPFPSFSILEDDN-SLKECYVMENPQEPDAPIVAYFPLISDTFQKYKAPGVE 762
Cdd:cd07201   397 DVILSLNYSLGSQFEPLKQASEYCSEQGIPFPKIELSPEDQeNLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVE 476

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208889 763 RSPDELELGQLNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALRLAMEKKRMR 826
Cdd:cd07201   477 RSPEEMAQGGVDVSSSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAVERKKQR 540
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
 295-817 0e+00

Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. Group IV cPLA2 includes six intercellular enzymes: cPLA2alpha, cPLA2beta, cPLA2gamma, cPLA2delta, cPLA2epsilon, and cPLA2zeta.


Pssm-ID: 132835 [Multi-domain]  Cd Length: 438  Bit Score: 536.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 295 VRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKLNFLDASTYITG 374
Cdd:cd00147     1 VRLASDLCDEEKEFLEKRRKVVAKALKKFLGLENDLNPDEVPVIAILGSGGGYRAMTGGAGALKALDEGGLLDCVTYLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 375 LSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFWGKLIEYSLGDK 454
Cdd:cd00147    81 LSGSTWLMASLYSNPDWSQKDLDEAIEWLKRHVIKSPLLLFSPERLKYYAKELEEKKKAGFNVSLTDFWGLLLGYTLLKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 455 KNECKLSDQRAALCRGQNPLPIYLTINVKDDV-SNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMGRLMKRIPEPE 533
Cdd:cd00147   161 LTDSSLSDQREFVQNGQNPLPIYTALNVKPGEtSINDFATWFEFTPYEVGFPKYGAFIPTEYFGSKFFMGRLVKKIPEDR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 534 MCYMLGLWSSIFSLNLLDAwnlshtseeffyrwtrerlhdieddpilpeiprcddnplettvvipttwlsntfreiltrr 613
Cdd:cd00147   241 LGFLMGTWGSAFSIILLDA------------------------------------------------------------- 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 614 pfvSEFHNFLYGMQLHTDYLqnrqfsmwkdtvldTFPNQLTQFAKHLNLLDTAFFVNSS-YAPLLRPERKVDLIIHLNYC 692
Cdd:cd00147   260 ---GKYPNFFYGLNLHKSYL--------------RSPNPLITSSDTLHLVDAGLDINNIpLPPLLRPERDVDVILSFDFS 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 693 AGSQ--TKPLKQTCEYCTEQ---KIPFP--SFSILEDDNSLKECYVMENPQEPDAPIVAYFPLISDTFQKYkapgversp 765
Cdd:cd00147   323 ADDPdwPNGLKLVATYERQAssnGIPFPkiPDSVTFDNLGLKECYVFFGCDDPDAPLVVYFPLVNDTFRKY--------- 393

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2065208889 766 delelgqlNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALR 817
Cdd:cd00147   394 --------DFDDPNSPYSTFNLSYTDEEFDRLLELAFYNVTNNKDTILQALR 437
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 296-831 4.78e-104

Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog.


Pssm-ID: 132839  Cd Length: 505  Bit Score: 330.56  E-value: 4.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 296 RLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLE--EGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKLNFLDASTYIT 373
Cdd:cd07200     2 RFSMALCDEEKEFRQARKMRVREALRKLLGEEgpKVTSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCATYVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 374 GLSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFWGKLIEYSLGD 453
Cdd:cd07200    82 GLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGETLIK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 454 KKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMGRLMKRIPEPE 533
Cdd:cd07200   162 ERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYPENP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 534 MCYMLGLWSSIFSLnlldawnlshtseeffyrwtrerlhdieddpilpeiprcddnplettvvipttwLSNTFREILTRR 613
Cdd:cd07200   242 LHFLMGVWGSAFSI------------------------------------------------------LFNRVLGRNSRE 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 614 PFVSEFHNFLYGMQLHTDYLQNrQFSMWKDTVLDTFPNQLTQFAKHLNLLDTAFFV----------NSSYAPLLRPERKV 683
Cdd:cd07200   268 GRAGKVHNFMLGLNLNTSYPLS-PLSDLATDEPEAAVADADEFERIYEPLDTKSKKihvvdsgltfNLPYPLILRPQRGV 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 684 DLIIHLNYCAG-SQTKP----LKQTCEYCTEQKIPFPSFSILEDDNS-LKECYVMENPQEPDAPIVAYFPLISDTFQKYK 757
Cdd:cd07200   347 DLIISFDFSARpSDSSPpfkeLLLAEKWARMNGLPFPPIDFKVFDREgLKECYVFKPKNDDDCPTVIHFVLCNINFRNLK 426

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208889 758 APGVER-SPDELELGQ-LNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALRLAMEKKRMRSQCPS 831
Cdd:cd07200   427 APGVPReTEEEKEFANfDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNNIDVIKDAIRESIEKRRRNPSRCS 502
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
 294-814 2.97e-67

Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.


Pssm-ID: 132841 [Multi-domain]  Cd Length: 430  Bit Score: 230.06  E-value: 2.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 294 DVRLGFSLCQEEVEFVQKRKMVVAKTLSQMlqleeGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKLNFLDASTYIT 373
Cdd:cd07202     2 EVRIAPGLNKEEKAAVVKRRKDVLQSLQKL-----GINADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLDCVTYLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 374 GLSGATWTMATLYSDPEWSSkNLETVVFEARRHVVKDKMpalfpDQLYKWREDLQKHSQEGYktTFTDFWGKLIEYSLGD 453
Cdd:cd07202    77 GVSGSTWCMSSLYTEPDWST-KLQTVEDELKRRLQKVSW-----DFAYALKKEIQAAKSDNF--SLTDFWAYLVVTTFTK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 454 KKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQ--DFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMGRLMKRIPE 531
Cdd:cd07202   149 ELDESTLSDQRKQSEEGKDPYPIFAAIDKDLSEWKErkTGDPWFEFTPHEAGYPLPGAFVSTTHFGSKFENGKLVKQEPE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 532 PEMCYMLGLWSSIFSlnlldawnlshtseeffyrwtrerlhDIEddpilpEIprcddnpLETTVVIPTTWLSNtfreilt 611
Cdd:cd07202   229 RDLLYLRALWGSALA--------------------------DGE------EI-------AKYICMSLWIWGTT------- 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 612 rrpfvsefHNFLYGmqlHTDYlqnrqfsmwKDtvldtfPNQLTQfAKHLNLLDTAFFVNSSYAPLLRPERKVDLIIHLNY 691
Cdd:cd07202   263 --------YNFLYK---HGDI---------AD------KPAMRS-RETLHLMDAGLAINSPYPLVLPPVRNTDLILSFDF 315

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 692 CAGSQTKPLKQTCEYCTEQKIPFPSFSILEDDNSLK---ECYVMENpqePDAPIVAYFPLISdtfqkykapgVERSPDEL 768
Cdd:cd07202   316 SEGDPFETIKDTAEYCRKHNIPFPQVDEAKLDQDAEapkDFYVFKG---ENGPVVMHFPLFN----------KVNCGDQL 382

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 2065208889 769 ELGQLNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQ 814
Cdd:cd07202   383 EDWRKEYRTFQGAYSTDQVRQLLELAKANVKNNKEKIMSEIRALAG 428
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 38-146 8.32e-49

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: 168.21  E-value: 8.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLtQND 117
Cdd:cd04036     1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYV-MDD 79

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 118 HLLTVLYDLSKLCLRNKTHVKFPLNPEGM 146
Cdd:cd04036    80 HLGTVLFDVSKLKLGEKVRVTFSLNPQGK 108
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 280-767 2.09e-45

Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.


Pssm-ID: 214474  Cd Length: 549  Bit Score: 171.84  E-value: 2.09e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  280 YELHMKSSPCSDTLdVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLE--EGLHED-----EVPIIAIMATGGGTRSMVS 352
Cdd:smart00022  14 YAPYNVSCPSDIPL-VRFSMGLSDNETEFLQKRKDYTNEAMKSFLGRAnsNFLDSSllnssDVPKIAIAGSGGGFRAMVG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  353 LYG------------HLLGLqklnfLDASTYITGLSGATWTMATLYSDPEWSSKNLETV--VFEARRHVVKDKMPALFPD 418
Cdd:smart00022  93 GAGvlkamdnrtdghGLGGL-----LQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEInsEWMFSVSINNPGINLLLTA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  419 QLYK-WREDLQKHSQEGYKTTFTDFWGKLIEYSLGDK-----------KNECKLSDqraalcrGQNPLPIYLTINVKDDV 486
Cdd:smart00022 168 QFYKsIVDAVWKKKDAGFNISLTDIWGRALSYNLFDSlggpnytlsslRDQEKFQN-------AEMPLPIFVADGRKPGE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  487 SNQDFREW-FEFSPYEVGM--QKYGAFIPSELFGSEFFMGRLMKRIPEPEMCYMLGLWSSIFSL---NLLDAWNLSHTSE 560
Cdd:smart00022 241 SVINFNDTvFEFSPFEFGSwdPKLNAFMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGTSSSlfnRFLLVLSNSTMEE 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  561 EFFYRWTRERLHDI--EDDPILPEIPrcddNPLETtvvipTTWLSNTFREILTRrpfvSEFHNFLYGMQLHTDY----LQ 634
Cdd:smart00022 321 SLIKIIIKHILKDLssDSDDIAIYPP----NPFKD-----DAYVQRMLTNSLGD----SDLLNLVDGGEDGENIplspLL 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  635 NRQFSMWKDTVLDT-------FPN--QLTQ-FAKHLNllDTAFFVNSSYAPLLRPERKVDLIIHLNY----CAGSQTK-- 698
Cdd:smart00022 388 QPERSVDVIFAVDAsadtdefWPNgsSLVKtYERHVV--DQGLTFNLPFPYVPDTQTFVNLGLSTKPtffgCDSSNLTyi 465

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208889  699 -PLKQ---TCEYCTEQKIPFPSFSILEDDNS--LKECYV---MENPQEPDAPIVayFPLISDTFQKYKAPGVERSPDE 767
Cdd:smart00022 466 pPLVVylpNEKWAYNSNISTFKISYSVFEREglIKNGYEfatVNNSTDDDCFIH--CVACAIIFRKQEAPNVTLPSEC 541
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 338-577 5.60e-36

Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain pfam00168. Phospholipase B enzymes catalyze the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.


Pssm-ID: 366778  Cd Length: 490  Bit Score: 142.89  E-value: 5.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 338 IAIMATGGGTRSMVSLYG-------------HLLGLqklnfLDASTYITGLSGATWTMATLYSDpEWSS-----KNLETV 399
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGvlaaldnrtdnetGLGGL-----LQSATYLAGLSGGSWLVGSLAVN-NFTSvqdfpDKPEDI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 400 VFEARRHVVKDKMPALFPDQLYKWR---EDLQKHSQEGYKTTFTDFWGKLIEYSLGDKKNE---CKLSDQRAA--LCRGQ 471
Cdd:pfam01735  75 SIWDLNHSIFNPGGLNIPQNIKRYDdivDAVWKKKNAGFNVSLTDIWGRALSYTLIPSLRGgpnYTWSSLRDAewFQNAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 472 NPLPIYLTINVKDDVSNQDFR-EWFEFSPYEVG--MQKYGAFIPSELFGSEFFMGRLMKRIPEPE----MCYMLGLWSSI 544
Cdd:pfam01735 155 MPFPIIVADGRKPGTTVINLNaTVFEFSPYEFGswDPTLNSFTPTEYLGTKFFNGTPVKKGKCVPgfdnAGFVMGTSSTL 234

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2065208889 545 FSLNLLdAWNLSHTSEEFFYRWTRERLHDIEDD 577
Cdd:pfam01735 235 FNQFLL-VINSTSSLPSFLNIIIKHILKDLSED 266
cPLA2_C2 pfam18695
Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a ...
 178-285 1.01e-35

Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking.


Pssm-ID: 465834  Cd Length: 111  Bit Score: 130.84  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 178 CLEVHAESRRPRKRKKNKDLLVMVTDSFENTQRVPPCQEPCYPNSACFHYPKYSQPQLYAEAPKSHCNFRLCCCG-THRN 256
Cdd:pfam18695   1 CLEVQVDSRGSKKEQGKKDLQLTVPGSYEGTQTISLGPEPGCPDPFCFHYPKYWEPELHVELPKSSVLQSGWNSDlEKET 80

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 257 DPVCQPLNCLSDGQVTTLPVGENYELHMK 285
Cdd:pfam18695  81 SKLTVPLKSLPLGQEVTVPLPEGQELHLR 109
C2 pfam00168
C2 domain;
37-141 3.94e-20

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 86.22  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  37 HLLTVRIIGMKNVRQADILSQTDCFVTLWLpTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQN 116
Cdd:pfam00168   1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRFGRD 79

                          90       100
                  ....*....|....*....|....*
gi 2065208889 117 DHLLTVLYDLSKLCLRNKTHVKFPL 141
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 38-135 2.00e-19

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: 84.08  E-value: 2.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889   38 LLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQND 117
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGRDD 80

                           90
                   ....*....|....*...
gi 2065208889  118 HLLTVLYDLSKLCLRNKT 135
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRH 98
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 39-141 3.33e-19

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: 83.27  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWLptASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDH 118
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSL--GGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDRFSKDDF 78

                          90       100
                  ....*....|....*....|....
gi 2065208889 119 LLTVLYDLSKLCLRNKTHVK-FPL 141
Cdd:cd00030    79 LGEVEIPLSELLDSGKEGELwLPL 102
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
 300-558 6.04e-18

Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B are Group IV cPLA2 homologs. Aspergillus PLA2 is Ca-dependent, yet it does not contain a C2 domain. PLB deacylates both sn-1 and sn-2 chains of phospholipids and are abundantly expressed in fungi. It shows lysophospholipase (lysoPL) and transacylase activities. The active site residues from cPLA2 are also conserved in PLB. Like cPLA2, PLB also has a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). It includes PLB1 from Schizosaccharomyces pombe, PLB2 from Candida glabrata, and PLB3 from Saccharomyces cerevisiae. PLB1, PLB2, and PLB3 show PLB and lysoPL activities; PLB3 is specific for phosphoinositides.


Pssm-ID: 132842  Cd Length: 552  Bit Score: 88.19  E-value: 6.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 300 SLCQEEVEFVQKRKMVVAKTLSQMLQ--------LEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKLN------- 364
Cdd:cd07203    19 GLSTNEQEYLEKRRSITNSALKDFLSranlngddDLDSNNSSNGPRIGIAVSGGGYRAMLTGAGAIAAMDNRTdnatehg 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 365 ---FLDASTYITGLSGATWTMATLYSDpEWSSKN--LETVVFEARRHVVKDKmPALFPDQLYKW---REDLQKHSQEGYK 436
Cdd:cd07203    99 lggLLQSSTYLSGLSGGSWLVGSLASN-NFTSVQdlLADSIWNLDHSIFNPY-GAAIVKTLNYYtnlANEVAQKKDAGFN 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 437 TTFTDFWGKLIEYSLGDKKNE------CKLSDQRAALcRGQNPLPIYLT---------INVKDDVsnqdfrewFEFSPYE 501
Cdd:cd07203   177 VSLTDIWGRALSYQLFPALRGgpnltwSSIRNQSWFQ-NAEMPFPIIVAdgrypgetiINLNATV--------FEFTPYE 247

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065208889 502 VGM--QKYGAFIPSELFGSEFFMGRlmkriPEPEMCY--------MLGLWSSIFSLNLLDaWNLSHT 558
Cdd:cd07203   248 FGSwdPSLNSFTPTEYLGTNVSNGV-----PPNGSCVngfdnagfVMGTSSTLFNQFLLQ-INSTSS 308
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 39-117 1.61e-11

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: 62.44  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWLPTASQK--KLKTRTISNCLHPEWDESFTFQIQTQV--KNVLELSVCDEDTLT 114
Cdd:cd08405    17 ITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRveKKKTVIKKRTLNPVFNESFIFNIPLERlrETTLIITVMDKDRLS 96


                  ...
gi 2065208889 115 QND 117
Cdd:cd08405    97 RND 99
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 39-145 1.83e-11

C2 domain fourth 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 fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176005 [Multi-domain]  Cd Length: 115  Bit Score: 61.82  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWLPTasQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDH 118
Cdd:cd04040     1 LTVDVISAENLPSADRNGKSDPFVKFYLNG--EKVFKTKTIKKTLNPVWNESFEVPVPSRVRAVLKVEVYDWDRGGKDDL 78

                          90       100
                  ....*....|....*....|....*..
gi 2065208889 119 LLTVLYDLSKLCLRNKTHVKFPLNPEG 145
Cdd:cd04040    79 LGSAYIDLSDLEPEETTELTLPLDGQG 105
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 340-562 1.56e-10

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 60.12  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 340 IMATGGGTRSMvSLYGHLLGLQKLNFLDASTYITGLSGATWTMATLYsdpewssknletvvfearrhvvkdkmpalfpdq 419
Cdd:cd01819     1 LSFSGGGFRGM-YHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY--------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889 420 lykwredlqkhsqegykttftdfwgklieyslgdkknecklsdqraalcrgqnplPIYLTINVKDDVSNQ---DFREWFE 496
Cdd:cd01819    47 -------------------------------------------------------PPSSSLDNKPRQSLEealSGKLWVS 71

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208889 497 FSPYEVGMQKYGAfipselfgseffmgRLMKRIPEPEMCYMLGLWSSIFSLNLLDAWNLSHTSEEF 562
Cdd:cd01819    72 FTPVTAGENVLVS--------------RFVSKEELIRALFASGSWPSYFGLIPPAELYTSKSNLKE 123
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
39-145 3.30e-10

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 64.01  E-value: 3.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889   39 LTVRIIGMKNVRQADILSQTDCFVTLWLptASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDH 118
Cdd:COG5038   1042 LTIMLRSGENLPSSDENGYSDPFVKLFL--NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGEKNDL 1119

                           90       100
                   ....*....|....*....|....*..
gi 2065208889  119 LLTVLYDLSKLCLRNKTHVKFPLNPEG 145
Cdd:COG5038   1120 LGTAEIDLSKLEPGGTTNSNIPLDGKT 1146
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 38-143 4.04e-10

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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: 176022 [Multi-domain]  Cd Length: 116  Bit Score: 58.04  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTDCFVTLWLptaSQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQND 117
Cdd:cd08376     1 VVTIVLVEGKNLPPMDDNGLSDPYVKFRL---GNEKYKSKVCSKTLNPQWLEQFDLHLFDDQSQILEIEVWDKDTGKKDE 77

                          90       100
                  ....*....|....*....|....*..
gi 2065208889 118 HLLTVLYDLSKLClRNKTH-VKFPLNP 143
Cdd:cd08376    78 FIGRCEIDLSALP-REQTHsLELELED 103
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 39-117 6.70e-10

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. 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-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 57.66  E-value: 6.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWL-PTAS-QKKLKTRTISNCLHPEWDESFTFQIQTQVKNV-LELSVCDEDTLTQ 115
Cdd:cd04026    15 LTVEVREAKNLIPMDPNGLSDPYVKLKLiPDPKnETKQKTKTIKKTLNPVWNETFTFDLKPADKDRrLSIEVWDWDRTTR 94


                  ..
gi 2065208889 116 ND 117
Cdd:cd04026    95 ND 96
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 38-111 2.62e-09

C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. The cds in this family contain multiple C2 domains as well as a C-terminal PRT domain. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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: 176023 [Multi-domain]  Cd Length: 119  Bit Score: 55.77  E-value: 2.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTDCFVTLWLPTAsqkKLKTRTISNCLHPEWDESFTFQIQtQVKNVLELSVCDED 111
Cdd:cd08377     2 FLQVKVIRASGLAAADIGGKSDPFCVLELVNA---RLQTHTIYKTLNPEWNKIFTFPIK-DIHDVLEVTVYDED 71
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 39-141 4.68e-09

C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176000 [Multi-domain]  Cd Length: 123  Bit Score: 54.98  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLW-LPTASQ-KKLKTRTISNCLHPEWDESFTFQIQT---QVKNVLELSVCDEDTL 113
Cdd:cd04035    17 LHCTIIRAKGLKAMDANGLSDPYVKLNlLPGASKaTKLRTKTVHKTRNPEFNETLTYYGITeedIQRKTLRLLVLDEDRF 96

                          90       100
                  ....*....|....*....|....*...
gi 2065208889 114 tQNDHLLTVLYDLSKLCLRNKTHVKFPL 141
Cdd:cd04035    97 -GNDFLGETRIPLKKLKPNQTKQFNICL 123
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 39-119 9.08e-09

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: 54.51  E-value: 9.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWLPTASQ--KKLKTRTISNCLHPEWDESFTFQI-QTQVKNV-LELSVCDEDTLT 114
Cdd:cd00276    16 LTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKklKKKKTSVKKGTLNPVFNEAFSFDVpAEQLEEVsLVITVVDKDSVG 95


                  ....*
gi 2065208889 115 QNDHL 119
Cdd:cd00276    96 RNEVI 100
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 37-120 1.38e-08

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: 53.81  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  37 HLLTVRIIGMKNVRQADILSQTDCFVTLwLPTASQKKL-KTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDtlTQ 115
Cdd:cd04043     1 HLFTIRIVRAENLKADSSNGLSDPYVTL-VDTNGKRRIaKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRS--FV 77


                  ....*
gi 2065208889 116 NDHLL 120
Cdd:cd04043    78 GKHDL 82
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 38-117 1.54e-08

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 54.25  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSqTDCFVTLWLptaSQKKLKTRTISNCLHPEWDESFTFQIqTQVKNVLELSVCDEDTLTQND 117
Cdd:cd04038     3 LLKVRVVRGTNLAVRDFTS-SDPYVVLTL---GNQKVKTRVIKKNLNPVWNEELTLSV-PNPMAPLKLEVFDKDTFSKDD 77
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 39-130 4.21e-08

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 52.63  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWL-PT---ASQKKLKTRTISNCLHPEWDESFTFQI---QTQVKN-VLELSVCDE 110
Cdd:cd04009    18 LRVEILNARNLLPLDSNGSSDPFVKVELlPRhlfPDVPTPKTQVKKKTLFPLFDESFEFNVppeQCSVEGaLLLFTVKDY 97

                          90       100
                  ....*....|....*....|
gi 2065208889 111 DTLTQNDHLLTVLYDLSKLC 130
Cdd:cd04009    98 DLLGSNDFEGEAFLPLNDIP 117
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 38-119 8.49e-08

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. 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: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 51.58  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTD--CFVTLWLPTASQK--KLKTRTISNCLHPEWDESFTFQIQTQvKNVLELSVCDEDTL 113
Cdd:cd04033     1 ILRVKVLAGIDLAKKDIFGASDpyVKISLYDPDGNGEidSVQTKTIKKTLNPKWNEEFFFRVNPR-EHRLLFEVFDENRL 79


                  ....*.
gi 2065208889 114 TQNDHL 119
Cdd:cd04033    80 TRDDFL 85
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
 39-137 1.18e-07

C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. 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: 176070 [Multi-domain]  Cd Length: 110  Bit Score: 50.77  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQ-TDCFVTLWLptaSQKKLKTRTISNCLHPEW-DESFTFQIQTQV--KNVLELSVCDEDTLT 114
Cdd:cd08688     1 LKVRVVAARDLPVMDRSSDlTDAFVEVKF---GSTTYKTDVVKKSLNPVWnSEWFRFEVDDEElqDEPLQIRVMDHDTYS 77

                          90       100
                  ....*....|....*....|...
gi 2065208889 115 QNDHLLTVLYDLSKLCLRNKTHV 137
Cdd:cd08688    78 ANDAIGKVYIDLNPLLLKDSVSQ 100
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 27-119 1.03e-06

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. 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: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 49.24  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  27 GALKEGSSPCHLLTVRIIGMKNVRQADILSQTDCFV--TLWLPTASQKKLKTRTISNCLHPEWDESFTF-QIQT-QVKNV 102
Cdd:cd04020    17 GALKSKKPSTGELHVWVKEAKNLPALKSGGTSDSFVkcYLLPDKSKKSKQKTPVVKKSVNPVWNHTFVYdGVSPeDLSQA 96

                          90
                  ....*....|....*...
gi 2065208889 103 -LELSVCDEDTLTQNDHL 119
Cdd:cd04020    97 cLELTVWDHDKLSSNDFL 114
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 39-136 1.26e-06

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 48.01  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLW-LPTASQK-KLKTRTISNCLHPEWDESFTFQ---IQTQVKNVLELSVCDEDTL 113
Cdd:cd04031    18 LIVTVLQARDLPPRDDGSLRNPYVKVYlLPDRSEKsKRRTKTVKKTLNPEWNQTFEYSnvrRETLKERTLEVTVWDYDRD 97

                          90       100
                  ....*....|....*....|...
gi 2065208889 114 TQNDHLLTVLYDLSKLCLRNKTH 136
Cdd:cd04031    98 GENDFLGEVVIDLADALLDDEPH 120
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 39-117 2.48e-06

C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 47.78  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFV--TLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQ-TQVKNV-LELSVCDEDTLT 114
Cdd:cd08402    17 LTVVILEAKNLKKMDVGGLSDPYVkiHLMQNGKRLKKKKTTIKKRTLNPYYNESFSFEVPfEQIQKVhLIVTVLDYDRIG 96


                  ...
gi 2065208889 115 QND 117
Cdd:cd08402    97 KND 99
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 39-119 8.62e-06

C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). 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: 176030 [Multi-domain]  Cd Length: 133  Bit Score: 46.19  E-value: 8.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWL-PTASQK-KLKTRTISNCLHPEWDESFTFQIQTQ--VKNVLELSVCDEDTLT 114
Cdd:cd08384    15 LIVGIIRCVNLAAMDANGYSDPFVKLYLkPDAGKKsKHKTQVKKKTLNPEFNEEFFYDIKHSdlAKKTLEITVWDKDIGK 94


                  ....*
gi 2065208889 115 QNDHL 119
Cdd:cd08384    95 SNDYI 99
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 73-132 3.77e-05

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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: 176024 [Multi-domain]  Cd Length: 121  Bit Score: 43.84  E-value: 3.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  73 KLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTqNDHLLTVLYDLSKLCLR 132
Cdd:cd08378    29 KGSTKAIERTSNPEWNQVFAFSKDRLQGSTLEVSVWDKDKAK-DDFLGGVCFDLSEVPTR 87
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 35-131 4.82e-05

C2A domain first 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176032 [Multi-domain]  Cd Length: 125  Bit Score: 43.47  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  35 PCHLLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQ---IQTQVKNVLELSVCDED 111
Cdd:cd08386    14 QESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEgfpYEKLQQRVLYLQVLDYD 93

                          90       100
                  ....*....|....*....|
gi 2065208889 112 TLTQNDHLLTVLYDLSKLCL 131
Cdd:cd08386    94 RFSRNDPIGEVSLPLNKVDL 113
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 39-142 8.79e-05

C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. 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: 176027 [Multi-domain]  Cd Length: 122  Bit Score: 42.67  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADiLSQTDCFVTLWLPTASQK--KLKTRTISNCLHPEWDESFTFQ--IQTQVKN-VLELSVCDEDTL 113
Cdd:cd08381    15 LFVMVMHAKNLPLLD-GSDPDPYVKTYLLPDPQKttKRKTKVVRKTRNPTFNEMLVYDglPVEDLQQrVLQVSVWSHDSL 93

                          90       100
                  ....*....|....*....|....*....
gi 2065208889 114 TQNDHLLTVLYDLSKLCLRNKTHVKFPLN 142
Cdd:cd08381    94 VENEFLGGVCIPLKKLDLSQETEKWYPLG 122
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
 39-117 1.12e-04

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


Pssm-ID: 176055 [Multi-domain]  Cd Length: 135  Bit Score: 42.96  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWLPTASQ--KKLKTRTISNCLHPEWDESFTFQI-QTQVKNV-LELSVCDEDTLT 114
Cdd:cd08410    16 LNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGLKliKTKKTSCMRGTIDPFYNESFSFKVpQEELENVsLVFTVYGHNVKS 95


                  ...
gi 2065208889 115 QND 117
Cdd:cd08410    96 SND 98
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 53-118 1.45e-04

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 42.17  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208889  53 DILSQTDCFVTLWLPTASQKKL----KTRTISNCLHPEWDESFT----FQIQTQVKnvLELSVCDEDTLTQNDH 118
Cdd:cd04048    16 DVLSKSDPFVVVYVKTGGSGQWveigRTEVIKNNLNPDFVTTFTvdyyFEEVQKLR--FEVYDVDSKSKDLSDH 87
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 39-119 1.51e-04

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


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 42.41  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKkLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDH 118
Cdd:cd04024     3 LRVHVVEAKDLAAKDRSGKGKSDPYAILSVGAQR-FKTQTIPNTLNPKWNYWCEFPIFSAQNQLLKLILWDKDRFAGKDY 81


                  .
gi 2065208889 119 L 119
Cdd:cd04024    82 L 82
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 36-129 2.18e-04

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding 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. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 41.70  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  36 CHLLTVRIIGMKnvrqaDILSQTDCFVTLWLptaSQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQ 115
Cdd:cd04025     4 CHVLEARDLAPK-----DRNGTSDPFVRVFY---NGQTLETSVVKKSCYPRWNEVFEFELMEGADSPLSVEVWDWDLVSK 75

                          90
                  ....*....|....
gi 2065208889 116 NDHLLTVLYDLSKL 129
Cdd:cd04025    76 NDFLGKVVFSIQTL 89
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 75-141 2.47e-04

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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: 176007 [Multi-domain]  Cd Length: 121  Bit Score: 41.49  E-value: 2.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065208889  75 KTRTISNCLHPEWDESFTFQIQtQVKNVLELSVCDEDTLTQNDHLLTVLYDLSKLCLRNKTHVKFPL 141
Cdd:cd04042    36 KSKTIYKNLNPVWDEKFTLPIE-DVTQPLYIKVFDYDRGLTDDFMGSAFVDLSTLELNKPTEVKLKL 101
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 66-111 4.89e-04

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: 40.99  E-value: 4.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2065208889  66 LPTASQKKLKTRTIS-NCLHPEWDESFTFQIqtqvkNVLELS-----VCDED 111
Cdd:cd00275    36 LPADDSAKFKTKVVKnNGFNPVWNETFEFDV-----TVPELAflrfvVYDED 82
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 39-143 5.92e-04

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 40.32  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQT-DCFVTLWL-P---TASQKKLKTRTisncLHPEWDESFTFQIQTQ--VKNVLELSVCDED 111
Cdd:cd08390    16 LTVSLIKARNLPPRTKDVAHcDPFVKVCLlPderRSLQSKVKRKT----QNPNFDETFVFQVSFKelQRRTLRLSVYDVD 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2065208889 112 TLTQNDHLLTVLYDLSKLCLRNKTHVKFPLNP 143
Cdd:cd08390    92 RFSRHCIIGHVLFPLKDLDLVKGGVVWRDLEP 123
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 39-119 8.35e-04

C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH 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. The members here have topology I.


Pssm-ID: 176021 [Multi-domain]  Cd Length: 136  Bit Score: 40.45  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQTD--CFVTLwlptASQKKlKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQN 116
Cdd:cd08375    17 LMVVIVEGRDLKPCNSNGKSDpyCEVSM----GSQEH-KTKVVSDTLNPKWNSSMQFFVKDLEQDVLCITVFDRDFFSPD 91


                  ...
gi 2065208889 117 DHL 119
Cdd:cd08375    92 DFL 94
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 38-129 1.52e-03

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


Pssm-ID: 176015 [Multi-domain]  Cd Length: 105  Bit Score: 38.70  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  38 LLTVRIIGMKNVRQADILSQTDCFVTLwlpTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQnd 117
Cdd:cd04050     1 LLFVYLDSAKNLPLAKSTKEPSPYVEL---TVGKTTQKSKVKERTNNPVWEEGFTFLVRNPENQELEIEVKDDKTGKS-- 75

                          90
                  ....*....|..
gi 2065208889 118 hLLTVLYDLSKL 129
Cdd:cd04050    76 -LGSLTLPLSEL 86
C2B_Synaptotagmin-3-5-6-9-10 cd08403
C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a ...
 34-117 1.55e-03

C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 3, a member of class 3 synaptotagmins, is located in the brain and localized to the active zone and plasma membrane. It functions as a Ca2+ sensor for fast exocytosis. It, along with synaptotagmins 5,6, and 10, has disulfide bonds at its N-terminus. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. 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: 176048 [Multi-domain]  Cd Length: 134  Bit Score: 39.41  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  34 SPCHL-----LTVRIIGMKNVRQADILSQTDCFVTLWLPTASQ--KKLKTRTISNCLHPEWDESFTFQIQTQ-VKNV-LE 104
Cdd:cd08403     6 SLCYLptagrLTLTIIKARNLKAMDITGFSDPYVKVSLMCEGRrlKKKKTSVKKNTLNPTYNEALVFDVPPEnVDNVsLI 85

                          90
                  ....*....|...
gi 2065208889 105 LSVCDEDTLTQND 117
Cdd:cd08403    86 IAVVDYDRVGHNE 98
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 39-129 1.80e-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: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  39 LTVRIIGMKNVRQADILSQT-DCFVTLWLpTASQKKLKTRTISNCLHPEWDESFTFQIQTqVKNVLELSVCDE-DTLtqN 116
Cdd:cd04044     4 LAVTIKSARGLKGSDIIGGTvDPYVTFSI-SNRRELARTKVKKDTSNPVWNETKYILVNS-LTEPLNLTVYDFnDKR--K 79

                          90
                  ....*....|....
gi 2065208889 117 DHLL-TVLYDLSKL 129
Cdd:cd04044    80 DKLIgTAEFDLSSL 93
C2_PSD cd04039
C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the ...
 59-135 2.02e-03

C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the biosynthesis of aminophospholipid by converting phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn). There is a single C2 domain present and it is thought to confer PtdSer binding motif that is common to PKC and synaptotagmin. 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: 176004 [Multi-domain]  Cd Length: 108  Bit Score: 38.39  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208889  59 DCFVTLwlpTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNV-LELSVCDEDTLTQNDHLLTVLYDLSKLCLRNKT 135
Cdd:cd04039    27 DPFVII---SFGRRVFRTSWRRHTLNPVFNERLAFEVYPHEKNFdIQFKVLDKDKFSFNDYVATGSLSVQELLNAAPQ 101
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 33-129 2.12e-03

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 38.79  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208889  33 SSPCHLLTVRIIGMKNVRQADILSQTDCFVTLW-LP--TASQKKlKTRTISNCLHPEWDESFTFQI-QTQVKN-VLELSV 107
Cdd:cd04030    12 SSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYlLPdkSKSTRR-KTSVKKDNLNPVFDETFEFPVsLEELKRrTLDVAV 90

                          90       100
                  ....*....|....*....|....
gi 2065208889 108 CDEDTL--TQNDHLLTVLYDLSKL 129
Cdd:cd04030    91 KNSKSFlsREKKLLGQVLIDLSDL 114
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 72-128 2.78e-03

C2 domain third 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 39.15  E-value: 2.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065208889  72 KKLKTRTISNCLHPEWDESFTFQIQ----TQvknVLELSVCDEDTLTQNDHLLTVLYDLSK 128
Cdd:cd04018    46 QKVKTSVKKNSYNPEWNEQIVFPEMfpplCE---RIKIQIRDWDRVGNDDVIGTHFIDLSK 103
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 84-111 7.89e-03

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. 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 synaptotagmin1. 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: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 37.23  E-value: 7.89e-03
                          10        20
                  ....*....|....*....|....*...
gi 2065208889  84 HPEWDESFTFQIQTQVKNVLELSVCDED 111
Cdd:cd08681    46 HPEWDEELRFEITEDKKPILKVAVFDDD 73
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 37-96 8.95e-03

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: 37.67  E-value: 8.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065208889  37 HLLTVRIIGMKNVRQADILsqtDCFVTLWLPTASQK--KLKTRTISNCLHPEWDESFTFQIQ 96
Cdd:cd08690     7 TIVRCIGIPLPSGWNPKDL---DTYVKFEFPYPNEEpqSGKTSTIKDTNSPEYNESFKLNIN 65
 
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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