NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2239095365|ref|XP_048109704|]
View 

cytosolic phospholipase A2 [Alosa alosa]

Protein Classification

cPLA2 family C2 domain-containing protein( domain architecture ID 10134213)

cPLA2 (cytosolic phospholipase A2) family C2 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 144-726 0e+00

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: 894.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 144 LRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKPRYlpNSPQEVPVIAVVGSGGGFRAMVGFSGVMKALYESGVLDCTT 223
Cdd:cd07200     1 LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKV--TSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 224 YIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLLPQHVTNYIQALWAKKAHGQPVTFADIFGMLIGET 303
Cdd:cd07200    79 YVAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 304 LIPARMDTKLTELQEKVTEAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYE 383
Cdd:cd07200   159 LIKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 384 ENPLHFLMGIWGSAFSILFNRVLGvkdtgpsgstmeeeleqirpadivgadnidndeeprkggsegkdgeeefhqraqas 463
Cdd:cd07200   239 ENPLHFLMGVWGSAFSILFNRVLG-------------------------------------------------------- 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 464 wvqrmvsslfsdsslFNTREGRAGKVHNFMLGLNLNTSMPFSPFSDYMYsqvaEEEVDAVTDPDEFDRIYEPLDVKSKKI 543
Cdd:cd07200   263 ---------------RNSREGRAGKVHNFMLGLNLNTSYPLSPLSDLAT----DEPEAAVADADEFERIYEPLDTKSKKI 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 544 HVVDSGLTYNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPKVFDREGLKECYVFKP 623
Cdd:cd07200   324 HVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFKP 403

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 624 NKDDKnCPTVIHFVLVNINFRQFKAPGVPRETEKDKEFADFDIFDDPNTPYSTFNFQYPNHAFQQLHDLMEFNTLNNIEV 703
Cdd:cd07200   404 KNDDD-CPTVIHFVLCNINFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNNIDV 482

                         570       580
                  ....*....|....*....|...
gi 2239095365 704 IKEAIKDSVVYRKENPTRCSVSL 726
Cdd:cd07200   483 IKDAIRESIEKRRRNPSRCSVSL 505
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 21-138 1.94e-53

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: 180.15  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGalgDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVMDE 100
Cdd:cd04036     3 TVRVLRATNITKG---DLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYVMDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2239095365 101 TLGTVTYEIGKLKVGQTETVPFSIGK--TTKVYLEMSLEV 138
Cdd:cd04036    80 HLGTVLFDVSKLKLGEKVRVTFSLNPqgKEELEVEFLLEL 119
 
Name Accession Description Interval E-value
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 144-726 0e+00

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: 894.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 144 LRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKPRYlpNSPQEVPVIAVVGSGGGFRAMVGFSGVMKALYESGVLDCTT 223
Cdd:cd07200     1 LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKV--TSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 224 YIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLLPQHVTNYIQALWAKKAHGQPVTFADIFGMLIGET 303
Cdd:cd07200    79 YVAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 304 LIPARMDTKLTELQEKVTEAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYE 383
Cdd:cd07200   159 LIKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 384 ENPLHFLMGIWGSAFSILFNRVLGvkdtgpsgstmeeeleqirpadivgadnidndeeprkggsegkdgeeefhqraqas 463
Cdd:cd07200   239 ENPLHFLMGVWGSAFSILFNRVLG-------------------------------------------------------- 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 464 wvqrmvsslfsdsslFNTREGRAGKVHNFMLGLNLNTSMPFSPFSDYMYsqvaEEEVDAVTDPDEFDRIYEPLDVKSKKI 543
Cdd:cd07200   263 ---------------RNSREGRAGKVHNFMLGLNLNTSYPLSPLSDLAT----DEPEAAVADADEFERIYEPLDTKSKKI 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 544 HVVDSGLTYNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPKVFDREGLKECYVFKP 623
Cdd:cd07200   324 HVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFKP 403

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 624 NKDDKnCPTVIHFVLVNINFRQFKAPGVPRETEKDKEFADFDIFDDPNTPYSTFNFQYPNHAFQQLHDLMEFNTLNNIEV 703
Cdd:cd07200   404 KNDDD-CPTVIHFVLCNINFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNNIDV 482

                         570       580
                  ....*....|....*....|...
gi 2239095365 704 IKEAIKDSVVYRKENPTRCSVSL 726
Cdd:cd07200   483 IKDAIRESIEKRRRNPSRCSVSL 505
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 132-665 0e+00

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 590.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  132 LEMSLEVCSDLDLRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKPRYLPNSP---QEVPVIAVVGSGGGFRAMVGFSG 208
Cdd:smart00022  16 PYNVSCPSDIPLVRFSMGLSDNETEFLQKRKDYTNEAMKSFLGRANSNFLDSSLlnsSDVPKIAIAGSGGGFRAMVGGAG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  209 VMKALYE-------SGVLDCTTYIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLL---PQHVTNYIQ 278
Cdd:smart00022  96 VLKAMDNrtdghglGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEINSEWMFSVSINNPGINLlltAQFYKSIVD 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  279 ALWAKKAHGQPVTFADIFGMLIGETLIPA--RMDTKLTEL--QEKVTEAQCPLPLFTCLHVKPDVSELMFADWV-EFSPY 353
Cdd:smart00022 176 AVWKKKDAGFNISLTDIWGRALSYNLFDSlgGPNYTLSSLrdQEKFQNAEMPLPIFVADGRKPGESVINFNDTVfEFSPF 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  354 EIGM--AKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGIWGSAFSILFNRVLGVKdtgpSGSTMEEELEQIRPADIV 431
Cdd:smart00022 256 EFGSwdPKLNAFMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGTSSSLFNRFLLVL----SNSTMEESLIKIIIKHIL 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  432 GADNIDNDEEprkgGSEGKDGEEEFhqraqaSWVQRMVSSLFSDSSLFNTREgragkvhnfmlGLNLNTSMPFSPFSDYM 511
Cdd:smart00022 332 KDLSSDSDDI----AIYPPNPFKDD------AYVQRMLTNSLGDSDLLNLVD-----------GGEDGENIPLSPLLQPE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  512 YSQVAEEEVDAVTDPDEFDRIYEPLdVKSKKIHVVDSGLTYNLPYPLILRPQRGVDLIISFDFSARPSDSS-----PPFK 586
Cdd:smart00022 391 RSVDVIFAVDASADTDEFWPNGSSL-VKTYERHVVDQGLTFNLPFPYVPDTQTFVNLGLSTKPTFFGCDSSnltyiPPLV 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  587 ELLLAEKWARMNKLPFPKIDPKVFDREGLK-ECYVFKP--NKDDKNCptVIHFVLVNINFRQFKAPGVPRETEKDKEFAD 663
Cdd:smart00022 470 VYLPNEKWAYNSNISTFKISYSVFEREGLIkNGYEFATvnNSTDDDC--FIHCVACAIIFRKQEAPNVTLPSECSKCFYN 547


                   ..
gi 2239095365  664 FD 665
Cdd:smart00022 548 YC 549
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 191-670 0e+00

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: 531.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 191 IAVVGSGGGFRAMVGFSGVMKALY--------ESGVLDCTTYIAGLSGSTWYMSTL-----YSHPEFPSRgPGQINQELM 257
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALDnrtdnetgLGGLLQSATYLAGLSGGSWLVGSLavnnfTSVQDFPDK-PEDISIWDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 258 RSVSSNPLRLLLPQHVTNY---IQALWAKKAHGQPVTFADIFGMLIGETLIPA---RMDTKLTEL--QEKVTEAQCPLPL 329
Cdd:pfam01735  80 NHSIFNPGGLNIPQNIKRYddiVDAVWKKKNAGFNVSLTDIWGRALSYTLIPSlrgGPNYTWSSLrdAEWFQNAEMPFPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 330 FTCLHVKPDVSELMF-ADWVEFSPYEIG--MAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGIWGSAFSILFNRVL 406
Cdd:pfam01735 160 IVADGRKPGTTVINLnATVFEFSPYEFGswDPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVMGTSSTLFNQFL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 407 GVKDTgpsgSTMEEELEQIRPADIVGADNIDNDEEPRKGGSEGKDGEEEfHQRAQASWVQrmvsslfsDSSLFNTREGRA 486
Cdd:pfam01735 240 LVINS----TSSLPSFLNIIIKHILKDLSEDSDDISQYPPNPFQDANDI-NQNATNSIVD--------SDTLFLVDGGED 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 487 GkvHNFMLGLNLNTSMPFSPFSDYMYSQVAEE-EVDAVTDPDEFDRIYEPLDVKSKKIHVVDSGLTYNLpYPLILRP-QR 564
Cdd:pfam01735 307 G--QNIPLWPLLQPERDVDVIFAVDNSADTDNdWPDGVSLVDTYERQFEPLQVKGKKFPYVPDGNTFVN-LGLNTRPtFF 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 565 GVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPKVFDREGLKECyVFKPNKDD--KNCPTVIHFVLVNIN 642
Cdd:pfam01735 384 GCDARNLTDLSARVSDSTPPLVVYLPNEPWSYMSNLSTFKISYNDSERQGLIEN-GFEAATQDneTDDPTFAHCVACAII 462

                         490       500
                  ....*....|....*....|....*...
gi 2239095365 643 FRQFKAPGVPRETEKDKEFADFDIFDDP 670
Cdd:pfam01735 463 RRKLERLNITLPSECEQCFENYCWNGTV 490
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 21-138 1.94e-53

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: 180.15  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGalgDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVMDE 100
Cdd:cd04036     3 TVRVLRATNITKG---DLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYVMDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2239095365 101 TLGTVTYEIGKLKVGQTETVPFSIGK--TTKVYLEMSLEV 138
Cdd:cd04036    80 HLGTVLFDVSKLKLGEKVRVTFSLNPqgKEELEVEFLLEL 119
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 21-116 2.26e-18

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: 80.99  E-value: 2.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365   21 KVTVLRAENVTKGalgDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVM-D 99
Cdd:smart00239   3 TVKIISARNLPPK---DKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGrD 79

                           90
                   ....*....|....*..
gi 2239095365  100 ETLGTVTYEIGKLKVGQ 116
Cdd:smart00239  80 DFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
22-124 4.96e-18

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 80.06  E-value: 4.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTKGalgDLLDTPDPYVELFIpTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYV-MDE 100
Cdd:pfam00168   5 VTVIEAKNLPPK---DGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRFgRDD 80

                          90       100
                  ....*....|....*....|....
gi 2239095365 101 TLGTVTYEIGKLKVGQTETVPFSI 124
Cdd:pfam00168  81 FIGEVRIPLSELDSGEGLDGWYPL 104
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
43-128 2.12e-05

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 48.22  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365   43 DPYVELFIptAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYV-MDETLGTVTYEIGKLKVGQTET-- 119
Cdd:COG5038   1062 DPFVKLFL--NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGeKNDLLGTAEIDLSKLEPGGTTNsn 1139


                   ....*....
gi 2239095365  120 VPFSiGKTT 128
Cdd:COG5038   1140 IPLD-GKTF 1147
PLN02952 PLN02952
phosphoinositide phospholipase C
 37-100 1.58e-03

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 41.91  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2239095365  37 DLLDTPDPYVELFIPTAP--ESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDanYVMDE 100
Cdd:PLN02952  492 DSYSPPDFYTKMYIVGVPadNAKKKTKIIEDNWYPAWNEEFSFPLTVPELALLRIEVRE--YDMSE 555
 
Name Accession Description Interval E-value
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 144-726 0e+00

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: 894.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 144 LRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKPRYlpNSPQEVPVIAVVGSGGGFRAMVGFSGVMKALYESGVLDCTT 223
Cdd:cd07200     1 LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKV--TSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 224 YIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLLPQHVTNYIQALWAKKAHGQPVTFADIFGMLIGET 303
Cdd:cd07200    79 YVAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 304 LIPARMDTKLTELQEKVTEAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYE 383
Cdd:cd07200   159 LIKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 384 ENPLHFLMGIWGSAFSILFNRVLGvkdtgpsgstmeeeleqirpadivgadnidndeeprkggsegkdgeeefhqraqas 463
Cdd:cd07200   239 ENPLHFLMGVWGSAFSILFNRVLG-------------------------------------------------------- 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 464 wvqrmvsslfsdsslFNTREGRAGKVHNFMLGLNLNTSMPFSPFSDYMYsqvaEEEVDAVTDPDEFDRIYEPLDVKSKKI 543
Cdd:cd07200   263 ---------------RNSREGRAGKVHNFMLGLNLNTSYPLSPLSDLAT----DEPEAAVADADEFERIYEPLDTKSKKI 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 544 HVVDSGLTYNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPKVFDREGLKECYVFKP 623
Cdd:cd07200   324 HVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFKP 403

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 624 NKDDKnCPTVIHFVLVNINFRQFKAPGVPRETEKDKEFADFDIFDDPNTPYSTFNFQYPNHAFQQLHDLMEFNTLNNIEV 703
Cdd:cd07200   404 KNDDD-CPTVIHFVLCNINFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNNIDV 482

                         570       580
                  ....*....|....*....|...
gi 2239095365 704 IKEAIKDSVVYRKENPTRCSVSL 726
Cdd:cd07200   483 IKDAIRESIEKRRRNPSRCSVSL 505
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 132-665 0e+00

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 590.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  132 LEMSLEVCSDLDLRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKPRYLPNSP---QEVPVIAVVGSGGGFRAMVGFSG 208
Cdd:smart00022  16 PYNVSCPSDIPLVRFSMGLSDNETEFLQKRKDYTNEAMKSFLGRANSNFLDSSLlnsSDVPKIAIAGSGGGFRAMVGGAG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  209 VMKALYE-------SGVLDCTTYIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLL---PQHVTNYIQ 278
Cdd:smart00022  96 VLKAMDNrtdghglGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEINSEWMFSVSINNPGINLlltAQFYKSIVD 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  279 ALWAKKAHGQPVTFADIFGMLIGETLIPA--RMDTKLTEL--QEKVTEAQCPLPLFTCLHVKPDVSELMFADWV-EFSPY 353
Cdd:smart00022 176 AVWKKKDAGFNISLTDIWGRALSYNLFDSlgGPNYTLSSLrdQEKFQNAEMPLPIFVADGRKPGESVINFNDTVfEFSPF 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  354 EIGM--AKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGIWGSAFSILFNRVLGVKdtgpSGSTMEEELEQIRPADIV 431
Cdd:smart00022 256 EFGSwdPKLNAFMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGTSSSLFNRFLLVL----SNSTMEESLIKIIIKHIL 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  432 GADNIDNDEEprkgGSEGKDGEEEFhqraqaSWVQRMVSSLFSDSSLFNTREgragkvhnfmlGLNLNTSMPFSPFSDYM 511
Cdd:smart00022 332 KDLSSDSDDI----AIYPPNPFKDD------AYVQRMLTNSLGDSDLLNLVD-----------GGEDGENIPLSPLLQPE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  512 YSQVAEEEVDAVTDPDEFDRIYEPLdVKSKKIHVVDSGLTYNLPYPLILRPQRGVDLIISFDFSARPSDSS-----PPFK 586
Cdd:smart00022 391 RSVDVIFAVDASADTDEFWPNGSSL-VKTYERHVVDQGLTFNLPFPYVPDTQTFVNLGLSTKPTFFGCDSSnltyiPPLV 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  587 ELLLAEKWARMNKLPFPKIDPKVFDREGLK-ECYVFKP--NKDDKNCptVIHFVLVNINFRQFKAPGVPRETEKDKEFAD 663
Cdd:smart00022 470 VYLPNEKWAYNSNISTFKISYSVFEREGLIkNGYEFATvnNSTDDDC--FIHCVACAIIFRKQEAPNVTLPSECSKCFYN 547


                   ..
gi 2239095365  664 FD 665
Cdd:smart00022 548 YC 549
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
 144-709 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: 577.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 144 LRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKPrylpNSPQEVPVIAVVGSGGGFRAMVGFSGVMKALYESGVLDCTT 223
Cdd:cd00147     1 VRLASDLCDEEKEFLEKRRKVVAKALKKFLGLEND----LNPDEVPVIAILGSGGGYRAMTGGAGALKALDEGGLLDCVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 224 YIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLLPQHVTNYIQALWAKKAHGQPVTFADIFGMLIGET 303
Cdd:cd00147    77 YLSGLSGSTWLMASLYSNPDWSQKDLDEAIEWLKRHVIKSPLLLFSPERLKYYAKELEEKKKAGFNVSLTDFWGLLLGYT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 304 LIPARMDTKLTELQEKVTEAQCPLPLFTCLHVKPDV-SELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKY 382
Cdd:cd00147   157 LLKELTDSSLSDQREFVQNGQNPLPIYTALNVKPGEtSINDFATWFEFTPYEVGFPKYGAFIPTEYFGSKFFMGRLVKKI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 383 EENPLHFLMGIWGSAFSILFNrvlgvkdtgpsgstmeeeleqirpadivgadnidndeeprkggsegkdgeeefhqraqa 462
Cdd:cd00147   237 PEDRLGFLMGTWGSAFSIILL----------------------------------------------------------- 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 463 swvqrmvsslfsdsslfntregRAGKVHNFMLGLNLNTSMPfspfsdymysqvaeeevdavtdpdefdRIYEPLDVKSKK 542
Cdd:cd00147   258 ----------------------DAGKYPNFFYGLNLHKSYL---------------------------RSPNPLITSSDT 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 543 IHVVDSGLTYN-LPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPKV-FDREGLKECYV 620
Cdd:cd00147   289 LHLVDAGLDINnIPLPPLLRPERDVDVILSFDFSADDPDWPNGLKLVATYERQASSNGIPFPKIPDSVtFDNLGLKECYV 368

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 621 FKPnKDDKNCPTVIHFVLVNINFRQFkapgvpretekdkefadfdIFDDPNTPYSTFNFQYPNHAFQQLHDLMEFNTLNN 700
Cdd:cd00147   369 FFG-CDDPDAPLVVYFPLVNDTFRKY-------------------DFDDPNSPYSTFNLSYTDEEFDRLLELAFYNVTNN 428


                  ....*....
gi 2239095365 701 IEVIKEAIK 709
Cdd:cd00147   429 KDTILQALR 437
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 191-670 0e+00

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: 531.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 191 IAVVGSGGGFRAMVGFSGVMKALY--------ESGVLDCTTYIAGLSGSTWYMSTL-----YSHPEFPSRgPGQINQELM 257
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALDnrtdnetgLGGLLQSATYLAGLSGGSWLVGSLavnnfTSVQDFPDK-PEDISIWDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 258 RSVSSNPLRLLLPQHVTNY---IQALWAKKAHGQPVTFADIFGMLIGETLIPA---RMDTKLTEL--QEKVTEAQCPLPL 329
Cdd:pfam01735  80 NHSIFNPGGLNIPQNIKRYddiVDAVWKKKNAGFNVSLTDIWGRALSYTLIPSlrgGPNYTWSSLrdAEWFQNAEMPFPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 330 FTCLHVKPDVSELMF-ADWVEFSPYEIG--MAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGIWGSAFSILFNRVL 406
Cdd:pfam01735 160 IVADGRKPGTTVINLnATVFEFSPYEFGswDPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVMGTSSTLFNQFL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 407 GVKDTgpsgSTMEEELEQIRPADIVGADNIDNDEEPRKGGSEGKDGEEEfHQRAQASWVQrmvsslfsDSSLFNTREGRA 486
Cdd:pfam01735 240 LVINS----TSSLPSFLNIIIKHILKDLSEDSDDISQYPPNPFQDANDI-NQNATNSIVD--------SDTLFLVDGGED 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 487 GkvHNFMLGLNLNTSMPFSPFSDYMYSQVAEE-EVDAVTDPDEFDRIYEPLDVKSKKIHVVDSGLTYNLpYPLILRP-QR 564
Cdd:pfam01735 307 G--QNIPLWPLLQPERDVDVIFAVDNSADTDNdWPDGVSLVDTYERQFEPLQVKGKKFPYVPDGNTFVN-LGLNTRPtFF 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 565 GVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPKVFDREGLKECyVFKPNKDD--KNCPTVIHFVLVNIN 642
Cdd:pfam01735 384 GCDARNLTDLSARVSDSTPPLVVYLPNEPWSYMSNLSTFKISYNDSERQGLIEN-GFEAATQDneTDDPTFAHCVACAII 462

                         490       500
                  ....*....|....*....|....*...
gi 2239095365 643 FRQFKAPGVPRETEKDKEFADFDIFDDP 670
Cdd:pfam01735 463 RRKLERLNITLPSECEQCFENYCWNGTV 490
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 133-716 1.82e-128

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: 392.85  E-value: 1.82e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 133 EMSLEvcsDLDLRFSLALCDKEKLFRQTRREKVMLGIKKLLNMEKprylpnSPQ--EVPVIAVVGSGGGFRAMVGFSGVM 210
Cdd:cd07201     4 EESSE---DLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEE------DLQedEVPVVAVMTTGGGTRALTSMYGSL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 211 KALYESGVLDCTTYIAGLSGSTWYMSTLYSHPEFPSRGPGQINQELMRSVSSNPLRLLLPQHVTNYIQALWAKKAHGQPV 290
Cdd:cd07201    75 LGLQKLGLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 291 TFADIFGMLIGETLIPARMDTKLTELQEKVTEAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFG 370
Cdd:cd07201   155 SFIDLWGLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFREWVEFTPYEVGFLKYGAFIPAEDFG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 371 SKFFMGTVVKKYEENPLHFLMGIWGSAFSILFNRVLgvKDTGPSGstmeeeleqirpadivgadniDNDEEPRKGGSEGK 450
Cdd:cd07201   235 SEFFMGRLMKKLPESRICFLQGMWSSIFSLNLLDAW--YLATGSE---------------------DFWHRWTRDKVNDI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 451 DGEEEFHQRAQASWVQRMVSSLFSDSSLFNTREGR--AGKVHNFMLGLNLNTSmpfspfsdymYSQVAEEEVDAVTDPDE 528
Cdd:cd07201   292 EDEPPLPPRPPERLTTLLTPGGPLSQAFRDFLTSRptVSQYFNFLRGLQLHND----------YLENKGFSTWKDTHLDA 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 529 FDRIYEPldvKSKKIHVVDSGLTYNLPYPLILRPQRGVDLIISFDFSarpsdSSPPFKELLLAEKWARMNKLPFPKIDPK 608
Cdd:cd07201   362 FPNQLTP---SEDHLCLVDTAFFINTSYPPLLRPERKVDVILSLNYS-----LGSQFEPLKQASEYCSEQGIPFPKIELS 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 609 VFDREGLKECYVFKpNKDDKNCPTVIHFVLVNINFRQFKAPGVPRETEKDKEFADFDifDDPNTPYSTFNFQYPNHAFQQ 688
Cdd:cd07201   434 PEDQENLKECYVFE-DADNPEAPIVLHFPLVNDTFRKYKAPGVERSPEEMAQGGVDV--SSSDSPYATRNLTYTEEDFDK 510

                         570       580
                  ....*....|....*....|....*...
gi 2239095365 689 LHDLMEFNTLNNIEVIKEAIKDSVVYRK 716
Cdd:cd07201   511 LVKLTSYNVLNNKDLILQALRLAVERKK 538
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
 143-708 2.99e-59

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: 206.56  E-value: 2.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 143 DLRFSLALCDKEKLFRQTRREKVMLGIKKL-LNMEKprylpnspqeVPVIAVVGSGGGFRAMVGFSGVMKALYESGVLDC 221
Cdd:cd07202     2 EVRIAPGLNKEEKAAVVKRRKDVLQSLQKLgINADK----------APVIAVLGSGGGLRAMIACLGVLSELDKAGLLDC 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 222 TTYIAGLSGSTWYMSTLYSHPEFPSRGPGqINQELMR---SVSSNPLRLLlpqhvTNYIQAlwAKKAHgqpVTFADIFGM 298
Cdd:cd07202    72 VTYLAGVSGSTWCMSSLYTEPDWSTKLQT-VEDELKRrlqKVSWDFAYAL-----KKEIQA--AKSDN---FSLTDFWAY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 299 LIGETLIPARMDTKLTELQEKVTEAQCPLPLFTCL-HVKPDVSELMFAD-WVEFSPYEIGMAKYGTFMTPDLFGSKFFMG 376
Cdd:cd07202   141 LVVTTFTKELDESTLSDQRKQSEEGKDPYPIFAAIdKDLSEWKERKTGDpWFEFTPHEAGYPLPGAFVSTTHFGSKFENG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 377 TVVKKYEENPLHFLMGIWGSAFSilfnrvlgvkdtgpsgstmeeeleqirpadivgadnidndeeprkggsegkDGEEEF 456
Cdd:cd07202   221 KLVKQEPERDLLYLRALWGSALA---------------------------------------------------DGEEIA 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 457 HQRAQASWVQrmvsslfsdsslfntregraGKVHNFMlglnlntsmpfspfsdYMYSQVAEeevdavtdpdefdriyEPL 536
Cdd:cd07202   250 KYICMSLWIW--------------------GTTYNFL----------------YKHGDIAD----------------KPA 277

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 537 DVKSKKIHVVDSGLTYNLPYPLILRPQRGVDLIISFDFSArpsdsSPPFKELLLAEKWARMNKLPFPKIDPKVFDR--EG 614
Cdd:cd07202   278 MRSRETLHLMDAGLAINSPYPLVLPPVRNTDLILSFDFSE-----GDPFETIKDTAEYCRKHNIPFPQVDEAKLDQdaEA 352

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 615 LKECYVFKpnkdDKNCPTVIHFVLVNINfrqfkAPGVPRETEKDKEFADFDifddpntPYSTfnfqypnhafQQLHDLME 694
Cdd:cd07202   353 PKDFYVFK----GENGPVVMHFPLFNKV-----NCGDQLEDWRKEYRTFQG-------AYST----------DQVRQLLE 406

                         570
                  ....*....|....
gi 2239095365 695 FNTlNNIEVIKEAI 708
Cdd:cd07202   407 LAK-ANVKNNKEKI 419
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 21-138 1.94e-53

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: 180.15  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGalgDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVMDE 100
Cdd:cd04036     3 TVRVLRATNITKG---DLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYVMDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2239095365 101 TLGTVTYEIGKLKVGQTETVPFSIGK--TTKVYLEMSLEV 138
Cdd:cd04036    80 HLGTVLFDVSKLKLGEKVRVTFSLNPqgKEELEVEFLLEL 119
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 193-418 1.70e-22

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: 94.40  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 193 VVGSGGGFRAMvGFSGVMKALYESGVLDCTTYIAGLSGSTWYMSTLYshpefpsrgpgqinqelmrsvssnplrlllpqh 272
Cdd:cd01819     1 LSFSGGGFRGM-YHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY--------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 273 vtnyiqalwakkahgqpvtfadifgmligetliparmdtkltelqekvteaqcplPLFTCLHVKPDVSE---LMFADWVE 349
Cdd:cd01819    47 -------------------------------------------------------PPSSSLDNKPRQSLeeaLSGKLWVS 71

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2239095365 350 FSPYEIGMAKYGTfmtpdlfgskffmgTVVKKYEENPLHFLMGIWGSAFSILFNRVLGVKDTGPSGSTM 418
Cdd:cd01819    72 FTPVTAGENVLVS--------------RFVSKEELIRALFASGSWPSYFGLIPPAELYTSKSNLKEKGV 126
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 21-116 2.26e-18

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: 80.99  E-value: 2.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365   21 KVTVLRAENVTKGalgDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVM-D 99
Cdd:smart00239   3 TVKIISARNLPPK---DKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGrD 79

                           90
                   ....*....|....*..
gi 2239095365  100 ETLGTVTYEIGKLKVGQ 116
Cdd:smart00239  80 DFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
22-124 4.96e-18

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 80.06  E-value: 4.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTKGalgDLLDTPDPYVELFIpTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYV-MDE 100
Cdd:pfam00168   5 VTVIEAKNLPPK---DGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRFgRDD 80

                          90       100
                  ....*....|....*....|....
gi 2239095365 101 TLGTVTYEIGKLKVGQTETVPFSI 124
Cdd:pfam00168  81 FIGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 21-119 4.86e-17

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: 77.11  E-value: 4.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGalgDLLDTPDPYVELFIptAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVM-D 99
Cdd:cd00030     2 RVTVIEARNLPAK---DLNGKSDPYVKVSL--GGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDRFSkD 76

                          90       100
                  ....*....|....*....|
gi 2239095365 100 ETLGTVTYEIGKLKVGQTET 119
Cdd:cd00030    77 DFLGEVEIPLSELLDSGKEG 96
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
 150-356 9.10e-13

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: 71.63  E-value: 9.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 150 LCDKEKLFRQTRREKVMLGIKKLLnmeKPRYLP-------NSPQEVPVIAVVGSGGGFRAMVGFSGVMKAL---YES--- 216
Cdd:cd07203    20 LSTNEQEYLEKRRSITNSALKDFL---SRANLNgdddldsNNSSNGPRIGIAVSGGGYRAMLTGAGAIAAMdnrTDNate 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 217 ----GVLDCTTYIAGLSGSTWYMSTLYSHpEFPSrgpgqINQELMRSVSSNPLRLLLP---------QHVTNYIQALWAK 283
Cdd:cd07203    97 hglgGLLQSSTYLSGLSGGSWLVGSLASN-NFTS-----VQDLLADSIWNLDHSIFNPygaaivktlNYYTNLANEVAQK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365 284 KAHGQPVTFADIFGMLIGETLIPARMDTKLTEL-----QEKVTEAQCPLPLFTCLHVKP--DVSELMFADWvEFSPYEIG 356
Cdd:cd07203   171 KDAGFNVSLTDIWGRALSYQLFPALRGGPNLTWssirnQSWFQNAEMPFPIIVADGRYPgeTIINLNATVF-EFTPYEFG 249
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 22-112 2.18e-10

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: 58.72  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVtKGAlGDLLDTPDPYVELFIpTAPESRKRTRHIDNNINPKWNETFTFILDpNQENTLKITLMDANYVM-DE 100
Cdd:cd04044     6 VTIKSARGL-KGS-DIIGGTVDPYVTFSI-SNRRELARTKVKKDTSNPVWNETKYILVN-SLTEPLNLTVYDFNDKRkDK 81

                          90
                  ....*....|..
gi 2239095365 101 TLGTVTYEIGKL 112
Cdd:cd04044    82 LIGTAEFDLSSL 93
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 21-115 7.61e-10

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: 57.17  E-value: 7.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGAlGDLLDTPDPYVELFI---PTAPESRKRTRHIDNN-INPKWNETFTFILDPNQENTLKITLMDANY 96
Cdd:cd00275     5 TIKIISGQQLPKPK-GDKGSIVDPYVEVEIhglPADDSAKFKTKVVKNNgFNPVWNETFEFDVTVPELAFLRFVVYDEDS 83

                          90
                  ....*....|....*....
gi 2239095365  97 VMDETLGTVTYEIGKLKVG 115
Cdd:cd00275    84 GDDDFLGQACLPLDSLRQG 102
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 18-119 8.94e-10

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: 56.91  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  18 HKYKVTVLRAENVtKGAlgDLLDTPDPYVELFI-PTA-PESRKRTRHIDNNINPKWNETFTF--ILDPNQEN-TLKITLM 92
Cdd:cd04035    15 SALHCTIIRAKGL-KAM--DANGLSDPYVKLNLlPGAsKATKLRTKTVHKTRNPEFNETLTYygITEEDIQRkTLRLLVL 91

                          90       100
                  ....*....|....*....|....*..
gi 2239095365  93 DANYVMDETLGTVTYEIGKLKVGQTET 119
Cdd:cd04035    92 DEDRFGNDFLGETRIPLKKLKPNQTKQ 118
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 41-110 9.09e-09

C2 domain first and third repeat 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 either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 54.22  E-value: 9.09e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  41 TPDPYVELFIptAPESRKrTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVMDETLGTVTYEIG 110
Cdd:cd08391    27 KSDPYVIVRV--GAQTFK-SKVIKENLNPKWNEVYEAVVDEVPGQELEIELFDEDPDKDDFLGRLSIDLG 93
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
 21-112 1.15e-08

C2 domain first repeat; fungal group; 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: 176006 [Multi-domain]  Cd Length: 111  Bit Score: 53.42  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGALGdlLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENT---LKITLMDANYV 97
Cdd:cd04041     4 VVTIHRATDLPKADFG--TGSSDPYVTASFAKFGKPLYSTRIIRKDLNPVWEETWFVLVTPDEVKAgerLSCRLWDSDRF 81

                          90
                  ....*....|....*.
gi 2239095365  98 -MDETLGTVTYEIGKL 112
Cdd:cd04041    82 tADDRLGRVEIDLKEL 97
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 43-110 2.68e-08

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: 52.70  E-value: 2.68e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2239095365  43 DPYVELFIPTapeSRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVMDETLGTVTYEIG 110
Cdd:cd08378    18 DPVVEVKLGN---YKGSTKAIERTSNPEWNQVFAFSKDRLQGSTLEVSVWDKDKAKDDFLGGVCFDLS 82
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 22-106 6.95e-08

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: 51.82  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTKGalgDLLDTPDPYVELFIpTAPESR---KRTRHIDNNINPKWNETFTFILDPN--QENTLKITLMDANY 96
Cdd:cd00276    18 VVVLKARNLPPS---DGKGLSDPYVKVSL-LQGGKKlkkKKTSVKKGTLNPVFNEAFSFDVPAEqlEEVSLVITVVDKDS 93

                          90
                  ....*....|.
gi 2239095365  97 VM-DETLGTVT 106
Cdd:cd00276    94 VGrNEVIGQVV 104
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 22-111 7.07e-08

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: 51.48  E-value: 7.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTKGALGDLldtPDPYVELFI-P-TAPESRKRTRHIDNNINPKWNETFTF---ILDPNQENTLKITLMDanY 96
Cdd:cd04031    20 VTVLQARDLPPRDDGSL---RNPYVKVYLlPdRSEKSKRRTKTVKKTLNPEWNQTFEYsnvRRETLKERTLEVTVWD--Y 94

                          90
                  ....*....|....*...
gi 2239095365  97 VMDET---LGTVTYEIGK 111
Cdd:cd04031    95 DRDGEndfLGEVVIDLAD 112
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 21-136 1.42e-07

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: 50.89  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGALGDLlDTPDPYVelfIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYVM-D 99
Cdd:cd04024     4 RVHVVEAKDLAAKDRSGK-GKSDPYA---ILSVGAQRFKTQTIPNTLNPKWNYWCEFPIFSAQNQLLKLILWDKDRFAgK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2239095365 100 ETLGTVTYEIGKL-KVGQTETVP-----------FSIGKTTKVYLEMSL 136
Cdd:cd04024    80 DYLGEFDIALEEVfADGKTGQSDkwitlkstrpgKTSVVSGEIHLQFSW 128
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 43-86 1.80e-07

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: 50.72  E-value: 1.80e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2239095365  43 DPYVEL-FIPTA-PESRKRTRHIDNNINPKWNETFTFILDPNQENT 86
Cdd:cd04026    35 DPYVKLkLIPDPkNETKQKTKTIKKTLNPVWNETFTFDLKPADKDR 80
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 19-104 2.40e-07

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: 50.71  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  19 KYKVTVLRAE-----------NVTKGALGDLLDTPDPYVElfIPTAPESRKrTRHIDNNINPKWNETFTF-ILDPNQENT 86
Cdd:cd04018     1 RFIFKIYRAEdlpqmdsgimaNVKKAFLGEKKELVDPYVE--VSFAGQKVK-TSVKKNSYNPEWNEQIVFpEMFPPLCER 77

                          90
                  ....*....|....*....
gi 2239095365  87 LKITLMD-ANYVMDETLGT 104
Cdd:cd04018    78 IKIQIRDwDRVGNDDVIGT 96
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 21-93 3.46e-07

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: 50.02  E-value: 3.46e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2239095365  21 KVTVLRAENVtkgALGDLLdTPDPYVELfipTAPESRKRTRHIDNNINPKWNETFTFILdPNQENTLKITLMD 93
Cdd:cd04038     5 KVRVVRGTNL---AVRDFT-SSDPYVVL---TLGNQKVKTRVIKKNLNPVWNEELTLSV-PNPMAPLKLEVFD 69
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 21-106 1.08e-06

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: 48.50  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVTKGalgDLLDTPDPYV--ELFIP-TAPESRK-RTRHIDNNINPKWNETFTFILDPnQENTLKITLMDANY 96
Cdd:cd04033     3 RVKVLAGIDLAKK---DIFGASDPYVkiSLYDPdGNGEIDSvQTKTIKKTLNPKWNEEFFFRVNP-REHRLLFEVFDENR 78

                          90
                  ....*....|.
gi 2239095365  97 V-MDETLGTVT 106
Cdd:cd04033    79 LtRDDFLGQVE 89
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 15-119 1.50e-06

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: 48.04  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  15 QYS---HKYKVTVLRAENVTkgaLGDLLDTPDPYVELFIptAPE----SRKRTRHIDNNINPKWNETFTFI--LDPNQEN 85
Cdd:cd04030    10 RYSsqrQKLIVTVHKCRNLP---PCDSSDIPDPYVRLYL--LPDksksTRRKTSVKKDNLNPVFDETFEFPvsLEELKRR 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2239095365  86 TLKITLMDANYVMD---ETLGTVTYEIGKLKVGQTET 119
Cdd:cd04030    85 TLDVAVKNSKSFLSrekKLLGQVLIDLSDLDLSKGFT 121
C2B_Tricalbin-like cd04052
C2 domain second repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 41-132 4.11e-06

C2 domain second 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176017 [Multi-domain]  Cd Length: 111  Bit Score: 46.06  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  41 TPDPYVELFIPTapESRKRTRHIDNNINPKWNETFTFILdPNQENT-LKITLMDANYVMDETLGTVTYEIGKL----KVG 115
Cdd:cd04052    12 LLSPYAELYLNG--KLVYTTRVKKKTNNPSWNASTEFLV-TDRRKSrVTVVVKDDRDRHDPVLGSVSISLNDLidatSVG 88

                          90
                  ....*....|....*..
gi 2239095365 116 QtETVPFSIGKTTKVYL 132
Cdd:cd04052    89 Q-QWFPLSGNGQGRIRI 104
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 21-132 5.38e-06

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: 46.02  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVtKGAlgDLLDTPDPYVELFIPTapESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYV-MD 99
Cdd:cd04040     2 TVDVISAENL-PSA--DRNGKSDPFVKFYLNG--EKVFKTKTIKKTLNPVWNESFEVPVPSRVRAVLKVEVYDWDRGgKD 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2239095365 100 ETLGTVTYEIGKLKVGQTE--TVPFS---IGKTTKVYL 132
Cdd:cd04040    77 DLLGSAYIDLSDLEPEETTelTLPLDgqgGGKLGAVFL 114
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 22-106 1.22e-05

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 45.30  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTKGALGDLLDtpdPYVELFIptAPESRKRTR-HIDNNINPKWNETFTFILDPN----QENTLKITLMDANY 96
Cdd:cd04051     4 ITIISAEDLKNVNLFGKMK---VYAVVWI--DPSHKQSTPvDRDGGTNPTWNETLRFPLDERllqqGRLALTIEVYCERP 78

                          90
                  ....*....|.
gi 2239095365  97 VM-DETLGTVT 106
Cdd:cd04051    79 SLgDKLIGEVR 89
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 18-108 1.40e-05

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: 44.95  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  18 HKYKVTVLRAENVTKGALGDLldtPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYV 97
Cdd:cd04043     1 HLFTIRIVRAENLKADSSNGL---SDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRSFV 77

                          90
                  ....*....|..
gi 2239095365  98 -MDETLGTVTYE 108
Cdd:cd04043    78 gKHDLCGRASLK 89
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
 21-104 1.40e-05

C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and plays a role in lymphocyte-mediated cytotoxicity. Mutations in perforin leads to familial hemophagocytic lymphohistiocytosis type 2. The function of perforin is calcium dependent and the C2 domain is thought to confer this binding to target cell membranes. 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: 175998 [Multi-domain]  Cd Length: 127  Bit Score: 44.94  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAEnvtkGALGDLLDTPDPYVELFIPTapeSRKRTRHIDNNINPKWNETFTF---ILDPNQEntLKITLMDA-NY 96
Cdd:cd04032    31 TVTVLRAT----GLWGDYFTSTDGYVKVFFGG---QEKRTEVIWNNNNPRWNATFDFgsvELSPGGK--LRFEVWDRdNG 101


                  ....*...
gi 2239095365  97 VMDETLGT 104
Cdd:cd04032   102 WDDDLLGT 109
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
43-128 2.12e-05

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 48.22  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365   43 DPYVELFIptAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANYV-MDETLGTVTYEIGKLKVGQTET-- 119
Cdd:COG5038   1062 DPFVKLFL--NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGeKNDLLGTAEIDLSKLEPGGTTNsn 1139


                   ....*....
gi 2239095365  120 VPFSiGKTT 128
Cdd:COG5038   1140 IPLD-GKTF 1147
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 19-119 3.58e-05

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: 44.31  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  19 KYKVTVLRAENVTKGALGDLldtPDPYVE--LFIPTAPESRKRTRHIDNNINPKWNETFTFILDPN--QENTLKITLMDA 94
Cdd:cd08402    16 KLTVVILEAKNLKKMDVGGL---SDPYVKihLMQNGKRLKKKKTTIKKRTLNPYYNESFSFEVPFEqiQKVHLIVTVLDY 92

                          90       100
                  ....*....|....*....|....*
gi 2239095365  95 NYVmdetlGTvTYEIGKLKVGQTET 119
Cdd:cd08402    93 DRI-----GK-NDPIGKVVLGCNAT 111
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 19-94 3.95e-05

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). 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 type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 43.83  E-value: 3.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2239095365  19 KYKVTVLRAENVTKGalgDLLDTPDPYVELFIPTapESRKRTRHIDNNINPKWNETFTFILDPNqeNTLKITLMDA 94
Cdd:cd08382     1 KVRLTVLCADGLAKR---DLFRLPDPFAVITVDG--GQTHSTDVAKKTLDPKWNEHFDLTVGPS--SIITIQVFDQ 69
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 22-93 6.30e-05

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: 43.56  E-value: 6.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2239095365  22 VTVLRAENVtkgALGDLLDTPDPYVELFIPTAPE--SRKRTRHIDNNINPKWNETFTF--ILDPNQENTLKITLMD 93
Cdd:cd08405    19 VNIIKARNL---KAMDINGTSDPYVKVWLMYKDKrvEKKKTVIKKRTLNPVFNESFIFniPLERLRETTLIITVMD 91
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 21-119 1.16e-04

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: 42.32  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVtkgALGDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFILDPN---QENTLKITLMDAN-Y 96
Cdd:cd08386    19 TLKILKAVEL---PAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYeklQQRVLYLQVLDYDrF 95

                          90       100
                  ....*....|....*....|...
gi 2239095365  97 VMDETLGTVTYEIGKLKVGQTET 119
Cdd:cd08386    96 SRNDPIGEVSLPLNKVDLTEEQT 118
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 19-96 1.64e-04

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 42.17  E-value: 1.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2239095365  19 KYKVTVLRAENVTKGalgDLLDTPDPYVELFIPtapESRKRTRHIDNNINPKWNETFTFILDpNQENTLKITLMDANY 96
Cdd:cd04027     2 KISITVVCAQGLIAK---DKTGTSDPYVTVQVG---KTKKRTKTIPQNLNPVWNEKFHFECH-NSSDRIKVRVWDEDD 72
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 37-77 1.70e-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: 41.79  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2239095365  37 DLLDTPDPYVELFIPTAPESRK----RTRHIDNNINPKWNETFTF 77
Cdd:cd04048    16 DVLSKSDPFVVVYVKTGGSGQWveigRTEVIKNNLNPDFVTTFTV 60
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 19-123 1.85e-04

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


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 41.94  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  19 KYKVTVLRAENVTKGalgDLLDTPDPYVELFIPtapESRKRTRHIDNNINPKWNETFTF-ILDPNQENTLKItlmDANYV 97
Cdd:cd04022     1 KLVVEVVDAQDLMPK---DGQGSSSAYVELDFD---GQKKRTRTKPKDLNPVWNEKLVFnVSDPSRLSNLVL---EVYVY 71

                          90       100
                  ....*....|....*....|....*.
gi 2239095365  98 MDETLGTVTYEIGKLKVGQTETVPFS 123
Cdd:cd04022    72 NDRRSGRRRSFLGRVRISGTSFVPPS 97
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 23-106 1.98e-04

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


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 41.86  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  23 TVLRAENVTKgalgdLLDTPDPYVELfipTAPESRKRTRHIDNNINPKWNETFTF----ILDPNQEntLKITLMDAN-YV 97
Cdd:cd08373     1 LVVSLKNLPG-----LKGKGDRIAKV---TFRGVKKKTRVLENELNPVWNETFEWplagSPDPDES--LEIVVKDYEkVG 70


                  ....*....
gi 2239095365  98 MDETLGTVT 106
Cdd:cd08373    71 RNRLIGSAT 79
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 17-104 2.00e-04

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 41.88  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  17 SHKYKVTVLRAE-NVTKGALGdlldtPDPYVELFIPTapESRKRTRHIDNNINPKWNETFTFILDPNQENTLKItLMDAN 95
Cdd:cd04021     1 KSQLQITVESAKlKSNSKSFK-----PDPYVEVTVDG--QPPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKV-WSHHT 72


                  ....*....
gi 2239095365  96 YVMDETLGT 104
Cdd:cd04021    73 LKADVLLGE 81
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 14-115 2.51e-04

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. 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: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 41.64  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  14 QQYSHKYKVTVLRAENVTKGalgDLLDTPDPYVELFIPTAPE--SRKRTRHIDNNINPKWNETFTFILDPNQENTLKITL 91
Cdd:cd08404    11 QPTTNRLTVVVLKARHLPKM---DVSGLADPYVKVNLYYGKKriSKKKTHVKKCTLNPVFNESFVFDIPSEELEDISVEF 87

                          90       100
                  ....*....|....*....|....
gi 2239095365  92 MdanyVMDETLGTVTYEIGKLKVG 115
Cdd:cd08404    88 L----VLDSDRVTKNEVIGRLVLG 107
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 22-115 3.62e-04

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: 41.18  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVtkgALGDLLDTPDPYVELFIptAPESRKRTRHIDN----NINPKWNETFTFILDPNQ--ENTLKITlmdan 95
Cdd:cd08384    17 VGIIRCVNL---AAMDANGYSDPFVKLYL--KPDAGKKSKHKTQvkkkTLNPEFNEEFFYDIKHSDlaKKTLEIT----- 86

                          90       100
                  ....*....|....*....|
gi 2239095365  96 yVMDETLGTVTYEIGKLKVG 115
Cdd:cd08384    87 -VWDKDIGKSNDYIGGLQLG 105
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
22-112 3.85e-04

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 43.98  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365   22 VTVLRAENVtKGALGDLLDTPDPYVElfIPTAPESRKRTRHIDNNINPKWNETFtFILDPNQENTLKITLMDANYVM-DE 100
Cdd:COG5038    440 VKIKSAEGL-KKSDSTINGTVDPYIT--VTFSDRVIGKTRVKKNTLNPVWNETF-YILLNSFTDPLNLSLYDFNSFKsDK 515

                           90
                   ....*....|..
gi 2239095365  101 TLGTVTYEIGKL 112
Cdd:COG5038    516 VVGSTQLDLALL 527
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 37-121 4.50e-04

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. 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 have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 40.78  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  37 DLLDTPDPYVELFIPTapESRKRTRHIDNNINPKWNETFTF-ILDPNQENTLKITL--MDA-NYVMDETLGTVT------ 106
Cdd:cd04049    17 DFLGKIDPYVIIQCRT--QERKSKVAKGDGRNPEWNEKFKFtVEYPGWGGDTKLILriMDKdNFSDDDFIGEATihlkgl 94

                          90
                  ....*....|....*
gi 2239095365 107 YEIGKLKvGQTETVP 121
Cdd:cd04049    95 FEEGVEP-GTAELVP 108
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 22-120 7.90e-04

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 40.03  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTkgALGDLLDTPDPYVELFIPTAPESRKRTRHIDNNINPKWNETFTFI-LDPNQENTLKITLM----DaNY 96
Cdd:cd08388    20 VNIIECRDLP--AMDEQSGTSDPYVKLQLLPEKEHKVKTRVLRKTRNPVYDETFTFYgIPYNQLQDLSLHFAvlsfD-RY 96

                          90       100
                  ....*....|....*....|....
gi 2239095365  97 VMDETLGTVTYEIGKLKVGQTETV 120
Cdd:cd08388    97 SRDDVIGEVVCPLAGADLLNEGEL 120
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 42-127 9.85e-04

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: 39.08  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  42 PDPYVELfipTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDANyvMDETLGTVTYEIGKLKVGQTETV- 120
Cdd:cd04050    21 PSPYVEL---TVGKTTQKSKVKERTNNPVWEEGFTFLVRNPENQELEIEVKDDK--TGKSLGSLTLPLSELLKEPDLTLd 95


                  ....*...
gi 2239095365 121 -PFSIGKT 127
Cdd:cd04050    96 qPFPLDNS 103
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 15-93 9.99e-04

C2A domain first repeat present in Synaptotagmins 1, 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 1, a member of 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 as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 39.56  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  15 QYSHKY-------KVTVLRAENVTkgALgDLLDTPDPYVELFIptAPESRKR--TRHIDNNINPKWNETFTFILDPN--Q 83
Cdd:cd08385     6 QFSLDYdfqsnqlTVGIIQAADLP--AM-DMGGTSDPYVKVYL--LPDKKKKfeTKVHRKTLNPVFNETFTFKVPYSelG 80

                          90
                  ....*....|
gi 2239095365  84 ENTLKITLMD 93
Cdd:cd08385    81 NKTLVFSVYD 90
PLN02952 PLN02952
phosphoinositide phospholipase C
 37-100 1.58e-03

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 41.91  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2239095365  37 DLLDTPDPYVELFIPTAP--ESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDanYVMDE 100
Cdd:PLN02952  492 DSYSPPDFYTKMYIVGVPadNAKKKTKIIEDNWYPAWNEEFSFPLTVPELALLRIEVRE--YDMSE 555
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 43-103 1.74e-03

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: 39.29  E-value: 1.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2239095365  43 DPYVELfipTAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDAN-YVMDETLG 103
Cdd:cd08375    37 DPYCEV---SMGSQEHKTKVVSDTLNPKWNSSMQFFVKDLEQDVLCITVFDRDfFSPDDFLG 95
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 23-129 2.10e-03

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: 38.62  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  23 TVLRAENVTKGalgDLLDTPDPYVELFIPTAP-ESR--KRTRHidnninPKWNETFTFILDPNQENTLKITLMDANYV-M 98
Cdd:cd04025     5 HVLEARDLAPK---DRNGTSDPFVRVFYNGQTlETSvvKKSCY------PRWNEVFEFELMEGADSPLSVEVWDWDLVsK 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2239095365  99 DETLGTVTYEIGKLKVGQTETVPFSIGKTTK 129
Cdd:cd04025    76 NDFLGKVVFSIQTLQQAKQEEGWFRLLPDPR 106
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
 22-121 2.16e-03

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. 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: 176011 [Multi-domain]  Cd Length: 126  Bit Score: 38.80  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  22 VTVLRAENVTKGalgDLLDTPDPYVelfIPTAPESRKRTRHIDNNINPKWNETFTFIL-DPNQEntLKITLMDANYVMDE 100
Cdd:cd04046     7 VHVHSAEGLSKQ---DSGGGADPYV---IIKCEGESVRSPVQKDTLSPEFDTQAIFYRkKPRSP--IKIQVWNSNLLCDE 78

                          90       100
                  ....*....|....*....|.
gi 2239095365 101 TLGTVTYEIGKLKVGQTETVP 121
Cdd:cd04046    79 FLGQATLSADPNDSQTLRTLP 99
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 40-77 2.18e-03

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: 39.61  E-value: 2.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2239095365  40 DTPDPYVELFI--PTAPESRKRTRHIDNNINPKWNETFTF 77
Cdd:cd04020    46 GTSDSFVKCYLlpDKSKKSKQKTPVVKKSVNPVWNHTFVY 85
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
 25-78 2.41e-03

C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1)) is a newly identified HECT-type E3 ubiquitin protein ligase highly expressed in favorable neuroblastomas. In vertebrates it is found primarily in neuronal tissues, including the spinal cord. NEDL1 is thought to normally function in the quality control of cellular proteins by eliminating misfolded proteins. This is thought to be accomplished via a mechanism analogous to that of ER-associated degradation by forming tight complexes and aggregating misfolded proteins that have escaped ubiquitin-mediated degradation. NEDL1, is composed of a C2 domain, two WW domains, and a ubiquitin ligase Hect domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176073 [Multi-domain]  Cd Length: 137  Bit Score: 38.92  E-value: 2.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2239095365  25 LRAENVTKGALGDlldtPDPYVELFIPTAPES----------RKRTRHIDNNINPKW-NETFTFI 78
Cdd:cd08691     8 LQARNLKKGMFFN----PDPYVKISIQPGKRHifpalphhgqECRTSIVENTINPVWhREQFVFV 68
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 15-115 2.81e-03

C2 domain second repeat present in Synaptotagmin 15; 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. 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: 176054 [Multi-domain]  Cd Length: 137  Bit Score: 38.86  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  15 QYSHKYKVTVLRAENVTKGALGDLldtpDPYVE--LFIPTAPESRKRTRHIDNNINPKWNETFTFILDPNQENT--LKIT 90
Cdd:cd08409    12 PTLNRLTVVVLRARGLRQLDHAHT----SVYVKvsLMIHNKVVKTKKTEVVDGAASPSFNESFSFKVTSRQLDTasLSLS 87

                          90       100
                  ....*....|....*....|....*
gi 2239095365  91 LMDANYVMDETLgtvtyeIGKLKVG 115
Cdd:cd08409    88 VMQSGGVRKSKL------LGRVVLG 106
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 14-93 4.60e-03

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


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 37.62  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  14 QQYSHKYKVTVLRAENVTkgALGDLLDTPDPYVELFIptAPESR--KRTRHIDNNINPKWNETFTFILDPN--QENTLKI 89
Cdd:cd08390    10 DLEEEQLTVSLIKARNLP--PRTKDVAHCDPFVKVCL--LPDERrsLQSKVKRKTQNPNFDETFVFQVSFKelQRRTLRL 85


                  ....
gi 2239095365  90 TLMD 93
Cdd:cd08390    86 SVYD 89
C2_plant_PLD cd04015
C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...
 41-75 4.71e-03

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. 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: 175982 [Multi-domain]  Cd Length: 158  Bit Score: 38.44  E-value: 4.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2239095365  41 TPDPYVELFIPTApesR-KRTRHIDNNINPKWNETF 75
Cdd:cd04015    57 TSDPYATVDLAGA---RvARTRVIENSENPVWNESF 89
C2C_MCTP_PRT_plant cd04019
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 21-105 4.74e-03

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


Pssm-ID: 175986 [Multi-domain]  Cd Length: 150  Bit Score: 38.42  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENVtkgALGDLLDTPDPYVELFIptAPESRKRTRHIDNNINPKWNETFTFILDPNQENTLKITLMDA-NYVMD 99
Cdd:cd04019     3 RVTVIEAQDL---VPSDKNRVPEVFVKAQL--GNQVLRTRPSQTRNGNPSWNEELMFVAAEPFEDHLILSVEDRvGPNKD 77


                  ....*.
gi 2239095365 100 ETLGTV 105
Cdd:cd04019    78 EPLGRA 83
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 21-105 5.07e-03

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


Pssm-ID: 176010 [Multi-domain]  Cd Length: 120  Bit Score: 37.57  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2239095365  21 KVTVLRAENV-TKGALGDLldtpDPYVELFIptAPESRKRTRHIDNNINPKWNETFTF-ILDPNQenTLKITLMDANYV- 97
Cdd:cd04045     4 RLHIRKANDLkNLEGVGKI----DPYVRVLV--NGIVKGRTVTISNTLNPVWDEVLYVpVTSPNQ--KITLEVMDYEKVg 75


                  ....*...
gi 2239095365  98 MDETLGTV 105
Cdd:cd04045    76 KDRSLGSV 83
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 21-77 7.05e-03

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: 37.28  E-value: 7.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2239095365  21 KVTVLRAENVtkgALGDLLDTPDPYVELFIPTApesRKRTRHIDNNINPKWNETFTF 77
Cdd:cd08377     4 QVKVIRASGL---AAADIGGKSDPFCVLELVNA---RLQTHTIYKTLNPEWNKIFTF 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH